Declaration

I do hereby declare that this project entitled

“To study the translation mechanism on

the basis of inheritance”

has been completed under the guidance and

submitted to [Link] Banerjee Mam
&[Link] Mam Head of Biology Department of
Burdwan Model School , is prepared by Amrisha
sen
 Aknowledgement
I am very grateful to everyone who supported me
to complete my project effectively and moreover
on time. My deep acknowledgment and gratitude
go to all those who helped me present these ideas
well. I would like to express my gratitude to my
teacher [Link] Banerjee Mam &
[Link] Mam for their support and guidance
in completing this project. I respect and thank
[Link] Banerjee Mam & [Link] Mam
for giving me an opportunity to do this project and
providing me all the valuable support and
guidance which made me complete the project on
time.

Secondly, I would also like to thank my parents

and friends who helped me a lot in finalizing this
project within the limited time frame

Aim Of the Project

 “To study the translation
mechanism on the basis
of inheritance”

Introduction
Protein Synthesis – Translation

The system via way of means of which

the mRNA codes for a specific protein is
referred to as Translation. In the system,
the ribosome interprets the mRNA
comprised of DNA into a series of
particular amino acids. This chain of
amino acids ends in protein synthesis. It
is a system wherein the fee of ATP is
needed and this power is given via way of
means of the charged tRNA. The entire
equipment of translation is gift
withinside the ribosomes.
The
ribosomes
encompass a
larger
subunit and
a smaller
subunit. The
large
subunit, in
turn,
includes
molecules of
tRNA which can be located near in order
that peptide bond can be advanced on
the price of enough energy. The mRNA
enters the smaller subunit that’s held via
way of means of the molecules of tRNA of
the complementary codon, that exists
withinside the larger subunit. Hence,
codons are held via way of means of
molecules of tRNA, located close to to
every different and a peptide bond is
produced amongst them. When this
system repeats, a massive chain of amino
acids is synthesised. At the stop, codon
ribosome releases the amino acid chain.
Structure of tRNA:

The DNA is transcribed into mRNA on the

basis of their complementarity.
Translation is the process of conversion
of nucleic acid information into amino
acids. There is no complementarity
between amino acids and mRNA. Hence,
translation is not controlled by
complementarity but by the genetic code.

Since amino acids cannot read this

genetic code, they are dependent on an
adapter molecule. This adapter molecule
is called tRNA (transfer RNA).

Structurally, the tRNA is an inverted L-

shaped molecule which has an anticodon
loop and amino acid acceptor end. The
anticodon loop makes bases
complementary to the codes on the
mRNA and amino acid end binds to the
respective amino acids. Thus, it helps in
protein synthesis. Each amino acid has a
specific tRNA. Initiator tRNA initiates the
translation while stop codons have no
tRNA.
The Central Dogma:

Francis Crick proposed that genetic

information flows from DNA → RNA →
Protein, it is known as the central dogma
of molecular biology.
Frequently Asked Questions:
How does protein
synthesis occurs in
prokaryotes?
In prokaryotes, which lack a nucleus, the
processes of both transcription and
translation occur in the cytoplasm. The
protein biosynthesis begins by the
association of a 30s ribosomal subunit
and an mRNA at the AUG codon site. Also
the post-transcriptional modifications are
not required here and the mature mRNA
molecule is immediately produced by
transcription.
Explain: DNA to mRNA to
protein.
Transcription is a process that converts
DNA information into a messenger RNA
(mRNA) molecule in the initial stage.
During transcription, RNA polymerase II
catalyses the synthesis of a pre-mRNA
molecule, later processed to become
mature mRNA. The DNA of a gene acts as
a template for complementary base
pairing. The resulting mRNA contains a
single-stranded copy of the gene that
needs to be converted into a protein
molecule. The mRNA is “read” following
the genetic code, which connects the
DNA sequence to the amino acid
sequence in proteins during translation,
the second major stage in gene
expression. A codon is a collection of
three nucleotides found in mRNA, and
each codon encodes an individual amino
acid (triplet code).
What is the role of amino
acids in protein
synthesis?
Amino acids have a wide range of
functions. Their main job is to serve as
the monomer in producing new proteins.
The nucleotide bases and various
neurotransmitters and hormones are
generated from amino acids, which can
also be utilised as substrates for
biosynthetic reactions.
Components and Steps of
Translation:
The procedure which involves the code of
genetics with a messenger RNA (mRNA)
molecule to get decoded and produce a
particular sequence of amino acids is
known as translation. This takes place in
the cytoplasm and involves three stages –
initiation, elongation and termination.
The core components required for the

process of translation include messenger

RNA, ribosomes and transfer RNA. So as
to start with the process of initiation, the
start codon needs to be recognized.
Further, the greater 60s subunit binds to
finish the initiation complex. After this,
the next step of elongation can begin.
The ribosome involves two tRNA binding
sites. First, there is the P site which
holds the peptide chain and the next is
the A site which accepts the tRNA. From
P site to A site, methionine then moves
so as to
bond a
novel
amino
acid over
there
which
begins
the
growth of
peptide.
The
ribosome
at that point translocates along the
mRNA molecule to the following codon.
At this time, the growing peptide lies at
the P site and the A site can be observed
as exposed for the binding of the next
aminoacyl-tRNA, and thus the cycle goes
on. Thus, it can be observed that the
polypeptide chain goes in the direction
from the N terminal (methionine) to the C
terminal (the final amino acid). After this,
the process of termination can begin. In
this process, a codon enters the A site
and no tRNA molecules bind to these
codons, so the peptide and tRNA in the P
site become hydrolysed, liberating the
polypeptide into the cytoplasm. The
petite and big subunits of the ribosome
detach, prepared for the following round
of translation. Lastly, it can be said that
the process of termination of translation
takes place as a stop codon, or nonsense
codon is encountered.

Translation Mechanism
Translation occurs in three phases: initiation,
elonga tion, and termination. The three
phases are generally similar in bacteria,
archaea, and eukaryotes, and yet they differ
in several ways, particularly during
translation ini tiation, where distinct
mechanisms are used to identify the start
codon..
Translation Initiation:
Translation initiation in all organisms begins
when the small ribosomal subunit binds near
the 5′ end of mRNA and identifies the start
codon sequence. In the next stage, the
initiator tRNA, the tRNA carrying the first
amino acid of the polypeptide, binds to the
start codon. In the final stage of initiation,
the large subunit joins the small subunit to
form an intact ribosome, and translation
begins. During these stages, initiation factor
proteins help control ribosome formation and
binding of the initiator tRNA, and guano sine
triphosphate (GTP) provides energy. The
tRNAs used during translation each carry a
specific amino acid and are identified as
charged tRNAs. In contrast, a tRNA without
an amino acid is uncharged. Specialized
enzymes discussed in a later section are
responsible for recognizing different tRNAs
and charging each one with the correct amino
acid. Starting translation at the authentic
(correct) start co don is essential for
translation of the correct polypeptide
Errant translation starting at the wrong codon, or
even at the wrong nucleotide of the start codon,
may produce an abnormal polypeptide and result
in a nonfunctional pro tein. Thus, critical questions
for biologists studying transla tion initiation were
these: How does the ribosome locate the authentic
start codon? And if more than one AUG (start
codon) sequence occurs near the 5′ end of the
mRNA, how is the authentic start codon identified?
Bacteria and eu karyotes use different
mechanisms to identify the authentic start codon.

Bacterial Translation Initiation:

In E. coli, six critical molecular components

come together to initiate the tran slation
process: (1) mRNA, (2) the small ribosomal
subunit, (3) the large ribosomal subunit, (4)
the initiator tRNA, (5) three essential
initiation factor proteins, and (6) GTP. For
most of translation initiation in bacteria, the
30S ribosomal subunit is affiliated with an
initiation factor (IF) protein called IF3, which
facilitates
binding
between the
mRNA and the
30S subunit.
IF3 also
prevents the
30S subunit
from binding to
the 50S
subunit (Figure
9.6).

The small
subunit–IF3
complex binds near the 5′ end of mRNA,
searching for the AUG sequence that serves
as the start codon. The preinitiation complex
forms when the authentic start codon
sequence is identified by base pairing that
occurs between the 16S rRNA in the 30S ribo
some and a short mRNA sequence located a
few nucleo tides upstream of the start codon
in the 5′ UTR of mRNA (Figure 9.6, 1 ) . John
Shine and Lynn Dalgarno identified the
location and sequence of this region in 1974,
and it is named the Shine–Dalgarno sequence
in recognition of their work. The Shine–
Dalgarno sequence is a purine-rich se quence
of about six nucleotides located three to nine
nucleotides upstream of the start codon. A
complemen tary pyrimidine-rich segment
containing the sequence UCCUCC is found
near the 3′ end of 16S rRNA, and it pairs with
the Shine–Dalgarno sequence to position the
mRNA on the 30S subunit (see Figure 9.6).
The Shine Dalgarno sequence is another
example of a consensus sequence. Like the
consensus sequences we describe for
promoters (Chapter 8) the Shine–Dalgarno
sequence has a characteristic nucleotide
composition and a precise position relative to
the start codon, but its exact nucleo tide
sequence varies slightly from one mRNA to
another (Figure 9.7). In the next step of
translation initiation (Figure 9.6, 2 ), the
initiator tRNA binds to the start codon at
what will be part of the P site after ribosome
assembly. The amino acid on the initiator
tRNA is a modified methionine called N-
formylmethionine (fMet); thus, the charged
initiator tRNA is abbreviated tRNAf Met. This
tRNA has a 3′-UAC-5′ anticodon sequence that
is a complementary mate to the start codon
sequence. An initiation factor (IF) protein
designated IF2 and a molecule of GTP are
bound at the P site to facilitate binding of
tRNAfMet. Initiation factor 1 (IF1) also joins
the complex to forestall attach ment of the
50S subunit. At this point, the 30S initiation
complex, consisting of mRNA bound to the
30S subunit, tRNAfMet located at the start
codon, three initiation fac tors, and a
molecule of GTP, has been formed. In the
final step of initiation (Figure 9.6, 3 ), the 50S
subunit joins the 30S subunit to form the
intact ribosome. The energy for the union of
the two subunits is derived from hydrolysis of
GTP to GDP (guanosine diphosphate). The
dissociation of IF1, IF2, and IF3 accompanies
the joining of subunits that creates the 70S
initiation com plex. This complex is a fully
active ribosome with a P site, an A site, an E
site, and a channel for exit of the
polypeptide. The first tRNA (tRNAfMet) is
already paired with mRNA at the P site, and
the open A site contains the second codon
and is awaiting the next charged tRNA.
Eukaryotic Translation Initiation:

The eukaryotic 40S ribosomal subunit

complexes with three eukaryotic initiation
factor (eIF) proteins eIF1, eIF1A, and eIF3 to
form the preinitiation complex (Figure 9.8,
1 ). In step, 2 the preinitiation complex joins
with
the
initiator tRNA and eIF5. The initiation
complex is formed by binding of the mRNA.
This initiates the process called scanning
(Figure 9.8, 3 ), in which the small ribosomal
subunit moves along the 5′ UTR in search of
the start codon. About 90% of eukaryotic
mRNAs use the first AUG en countered by the
initiation complex as the start codon, but the
remaining 10% use the second or, in some
cases, the third AUG as the start codon. The
initiation complex is able to accurately locate
the authentic start codon be cause the codon
is embedded in a consensus sequence that
reads 5′-ACCAUGG-3′ (the start codon itself is
shown in bold). This consensus sequence is
called the Kozak sequence after Marilyn
Kozak, who discovered it in 1978. Locating
the start codon leads to recruitment of the
60S subunit to the complex, using energy
derived from GTP hydrolysis. This final step 4
in the formation of the 80S ribosome is
accompanied by joining of the two subunits
and dissociation of the eIF proteins. In the
80S ribosome, the initiator tRNAMet is
located at the P site; the A site is vacant,
awaiting arrival of the second tRNA. in
archaea is decidedly eukaryote-like. One
example of this similarity is the archaeal use
of methionine as the common first amino acid
of polypeptide chains. This is like eukaryotes
and unlike bacteria, which use N-fromyl-
methionine. A second aspect of archaeal
translation initiation concerns the presence
of Shine Dalgarno sequences. These are
relatively common in archaeal species that
either do not produce leaderless mRNAs or
produce very few. In contrast, archaeal
species that produce a high proportion of
leaderless mRNA, Shine–Dalgarno sequences
are not as common, although they have been
detected. More significantly from an
evolutionary perspective, Table 9.3 lists
archaeal translation initiation factor proteins
and identifies their homologies to eukaryotic
and bacte rial proteins. Recall from our
discussion in Section 1.4 C 3’ C that amino
acid or nucleic acid sequences (proteins,
DNA, or RNA) that are homologous have a
common ancestral origin. As a consequence,
proteins that have greater degrees of
homology have more recent common
ancestral history than do proteins with lower
levels of homology. If proteins do not share a
common ancestral history, they will not re
veal homology. Based on the homologous
protein information in Table 9.3, it is clear
that translation initiation in ar chaea is more
complex than in bacteria and that known
archaeal initiation factor proteins (aIFs) are
homolo gous in structure and function to
eIFs. This comparison of critical translational
proteins also indicates striking similarity of
translation initiation across the three do
mains of life. Translation in all forms of life
has a common origin. Evolution has acted to
conserve the key protein.
components of translation, with each domain
acquiring its own specific features of
translation. The archaea have multiple
mechanisms of mRNA– ribosome interaction
at translation initiation. This is most apparent
at the 5′ mRNA end where certain archaeal
spe cies have a large percentage—some
studies say more than 50% of their mRNAs—
that appear not to have a 5′ UTR. Those
mRNAs lacking a 5′ UTR are said to be leader
less mRNAs and are apparently missing all or
most of the translation initiating segments,
including the Shine Dalgarno sequence in
some cases. The mechanism through which
leaderless mRNA translation is initiated is not
yet known. Archaeal species producing
mRNAs with 5′ UTRs typically have Shine–
Dalgarno sequences to aid translation
intiation. Analysis of experimental in vitro
translation (translation in a test tube using
ribosomes and trans lationally active
proteins) testing the ability of bacte rial and
eukaryotic ribosomes and translational
proteins to translate leaderless mRNAs from
archaea finds that translation works
efficiently in both in vitro systems. Leaderless
mRNAs are very rare in bacteria or in eu
karyotes, yet they are efficiently translated in
vitro. This finding does not suggest a
translational mechanism, but it has led to
speculation that the leaderless mRNA state
may be ancestral to the state featuring 5′
UTRs. In other words, it is possible that the
last universal common ancestor (LUCA) of
bacteria, archaea, and eukaryotes produced
leaderless mRNAs and that the mRNAs with 5′
UTRs are a more recent development. In this
context, archaeal translation may be
something of a relic reminis cent of the
situation in the LUCA.

Polypeptide Elongation:

Elongation,the second phase of translation,

begins with the recruitment of elongation
factor (EF) proteins into the initiation
complex. Elongation factors facilitate three
steps of polypeptide synthesis:

1). Recruitment of charged tRNAs to the A

site.

2.) Formation of a peptide bond between

sequential amino acids

3.) Translocation of the ribosome in the 3′

direction along mRNA GTP cleavage provides
the energy for each step of elongation in
bacteria, archaea, and eukaryotes
(Foundation Figure 9.9). Moreover, the steps
in the elongation process are the same in all
three types of organisms: although the
elongation factors differ, the ribosomal P, A,
and E sites of all three organisms serve
nearly identical functions. The rates of
elongation are also similar; bacteria add
about 20 new amino acids per second to a
nascent polypeptide chain, and eukaryotes
elongate the polypeptide at a rate of 15
amino acids per second. The elongation rate
in archaea has not been established. Lastly,
numerous studies indicate high fidelity of
translation in all organisms. An error rate of
approximately one amino acid in each 10,000
added to polypeptides is estimated for
bacteria.
Polypeptide Elongation in Bacteria:

Different elonga tion factor proteins (EFs)

and other ribosomal proteins carry out
elongation in a series of steps depicted in
Foundation Figure 9.9, while specifically
describing translation in bacteria, is generally
accurate for all organisms. The energy
required for these steps is generated by
hydrolysis, the cleavage of one phosphate
molecules from guanosine triphosphate
molecules (GTP). Hydrolysis releases energy
and converts nucleotide triphosphates to
nucleotide diphosphates (i.e., GTP S GDP). In
step 1 a charged tRNAs is bound by the
elongation factor EF-Tu and GTP. In step 2 ,
the tRNA affiliates with the correct anticodon
sequence enters the A site. In step 3 tRNA
pairs with the mRNA codon and hydrolysis of
GTP releases EF-Tu-GDP from tRNA. In step
4 , the enzyme peptidyl transferase catalyzes
peptide bond formation between the amino
acid at the P site and the newly recruited
amino acid at the A site. This elongates the
polypeptide and transfers the polypeptide to
the tRNA at the A site. The tRNA at the P site
departs the ribosome through
the E site. In step 5 elongation factor EF-G uses
GTP hydrolysis to, EFs translocate the ribosome by
moving it in the 3′ direction on mRNA. This
translocation step is exactly one codon in length,
that is, three nucleotides. Translocation moves the
tRNA formerly at the A site to the P site, and
opens the A site for binding by a charged tRNA
with the correct anticodon sequence. In step 6 the
next charged tRNA is ready to enter the A site.
Elongation of Eukaryotic and Archaeal Polypeptides:

Evolution has acted to strongly conserve the basic

biochemistry of polypeptide elongation in all three
domains of life. The elongation factors that carry
out polypeptide elongation in eukaryotes and
archaea are shown in Table 9.4. All organisms use
two elongation factors to carry out polypeptide
elongation, and the illustration of polypeptide
elongation in Figure 9.9 is an equally accurate
portrayal of the process in eukaryotes and
archaea. Based on sequence comparisons, the
archaeal and eukaryotic elongation factor
homologs are more alike than are archaeal and
bacterial EFs. This sequence analysis supports the
initial assessment of
Carl Woese that
eukaryotes and
archaea are more
closely related to one
another than either is
to bacteria (see
Section 1.1).
Translation Termination:
The elongation cycle continues until one of the
three stop codons, UAG, UGA, or UAA, enters the A
site of the ribosome. There are no tRNAs with
anticodons comple mentary to stop codons, so the
entry of a stop codon into the A site is a
translation-terminating event. All organ isms use
release factors (RF) to bind a stop codon in the A
site (Figure 9.10). The catalytic activity of RFs
releases the polypeptide bound to tRNA at the P
site. Polypeptide release causes ejection of the RF
from the P site and leads to the separation of the
ribosomal subunits. In bacteria, two release
factors, RF1 and RF2, rec ognize stop codons. RF1
recognizes UAG and UAA.

Translation of Polycistronic mRNA: Each

polypeptide-producing gene in eukaryotes produces
monocistronic mRNA, meaning mRNA that directs the
synthesis of a single kind of polypeptide. The scanning
model for translation described earlier for eukaryotes im
plies that a single start codon is identified in eukaryotic
mRNA to initiate synthesis of one kind of polypeptide
chain. In contrast, groups of bacterial and archaeal
genes often share a single promoter, and the resulting
mRNA transcript contains information that synthesizes
several different poly peptides. These polycistronic
mRNAs are produced as part of operon systems that
regulate the transcription of sets of bacterial genes
functioning in the same metabolic pathway (a form of
regulation we discuss in Chapter 15). Polycistronic
mRNAs consist of multiple polypeptide producing
segments—multiple cistrons—that each con tain
sequence information for translation initiation. In the
case of bacteria, and in all but the leaderless mRNAs in
archaea, the translation-initiating region contains a
Shine–Dalgarno sequence and start and stop codons. An
intercistronic spacer sequence that is not translated
separates the cistrons of polycistronic mRNA and con
tains the Shine–Dalgarno sequences (Figure 9.12).
Bacterial intercistronic spacers are variable in length:
Some are just a few nucleotides long, although most are
30 to 40 nucleotides long. If the intercistronic spacer is a
few nucleotides in length, it is, short enough to be
spanned by a ribosome. In such systems, the ribosome
remains intact after completing synthesis of one poly
peptide, and it translates the other genes encoded in the
polycistronic mRNA as well. On the other hand, for lon
ger intercistronic spacers, the initial ribosome
dissociates and new translation initiation must occur to
translate the next polypeptide encoded by the
polycistronic mRNA

The Genetic Code Translates Messenger RNA into

Polypeptide: Nucleic acids and amino acids are
chemically very different compounds, and there is no
direct mechanism by which mRNA could synthesize a
polypeptide. Nevertheless, the genetic information
carried in the nucleotide sequences of mRNA does
provide a means by which the amino acid sequences of
polypeptides can be specified. The “genetic code” is the
name used to describe the correspon dence between
mRNA codon sequences and individual amino acids.
Converting the sequence of mRNA into a polypeptide
depends on transfer RNA (tRNA) to carry amino acids to
the ribosome. At ribosomes, tRNA pairs with mRNA by
complementary base pairing between mRNA codon nucle
otides and tRNA anticodon nucleotides. Once the correct
tRNA is bound by a codon, it transfers its amino acid to
the end of a growing polypeptide chain. Transfer RNA
mol ecules facilitate the translation of genetic
information from one chemical language (nucleic acid) to
another (amino acid). That is, tRNA is an adaptor
molecule that interprets and then acts on the
information carried in mRNA. Our review of translation
and the genetic code in Chapter 1 depicts a triplet
genetic code: Groups of three consecutive mRNA
nucleotides form codons that each correspond to one
amino acid. The genetic code contains 64 different
codons, more than enough to en code the 20 common
amino acids used to construct poly peptides. The greater
number of codons than amino acids. leads to
redundancy of the genetic code, as evidenced by
the observation that single amino acids are
specified by from one to as many as six different
codons. This redun dancy is explained by aspects
of the base-pairing interac tions between tRNA
anticodons and mRNA codons.
The Genetic Code Displays Third-Base Wobble:

The triplet genetic code is a biological example of

Ockham’s razor, the principle that the simplest
hypoth esis is the
most likely to be correct: During the late 1950s,
arithmetic logic led many researchers to conclude
that the genetic code was most likely triplet. This
simple solu tion to the question of how amino acid
sequences could be coded by nucleic acid
sequences posits that a doublet genetic code (two
nucleotides per codon) could produce just 16 (42)
combinations of codons, which is not enough
different combinations to specify 20 amino acids.
On the other hand, a quadruplet genetic code
would gener ate 44, or 256, different combinations
of codons—far too many for the needs of genomes.
In contrast, a triplet genetic code, yielding 43, or
64 different codons, provides enough variety to
encode 20 amino acids with some, but not
excessive, redundancy (Figure 9.13 and genetic
code information inside the front cover of the
book). Among the 64 codons, 61 specify amino
acids, and the remaining. 3 are the stop codons
that terminate translation. Only two amino
acids, methionine (Met)—with the codon AUG
— and tryptophan (Trp)—with the codon UGG
—are encoded by single codons. The other 18
amino acids are specified by two to six
codons. Codons that specify the same amino
acid are called synonymous codons. Each
transfer RNA molecule carries a particular
amino acid to the ribosome, where
complementary base pairing between each
mRNA codon sequence and the correspond
ing anticodon sequence of a correct tRNA
takes place. Note that this complementary
base pairing requires antiparallel alignment
of the mRNA and tRNA strands. Consider the
codon sequence for aspartic acid (Asp), 5′-
GAC-3′. Base pairing rules predict that the
tRNA anticodon sequence is 3′-CUG-5′ (Figure
9.14). Asp is also specified by a synony mous
codon, 5′-GAU-3′, that pairs with tRNA
carrying the anticodon sequence 5′-CUA-3′.
Transfer RNA molecules with different
anticodon sequences for the same amino acid
are called isoaccepting tRNAs. Does the
presence of synonymous codons and isoac
cepting tRNAs mean that a genome must
provide 61 differ ent tRNA genes and
transcribe a tRNA molecule to match each
codon? The answer is no. In fact, most
genomes have 30 to 50 different tRNA genes.
How does a genome that encodes fewer than
61 different tRNA molecules recognize all 61
functional codons? The answer lies in
relaxation of the strict complementary base-
pairing rules at the third base of the codon.
The mechanics of translation provide for
flexibility in the pairing of the third base, the
3′-most nucleotide, of the codon. Third-base
wobble is the name given to the mechanism
that relaxes the requirement for
complementary base pairing between the
third base of a codon and the corresponding
nucleotide of its anticodon. How does third-
base wobble work? The answer is found in the
chemical structures of nucleotides that
hydrogen bond in base-pairing reactions. A
careful look at
synony mous codons
reveals a pattern to
the chemical
structure of the third
bases in cases of
wobble. With the
exception of the AUA
codon for isoleucine (Ile) and the UGG codon
for tryptophan (Trp), synonymous codons can
be grouped into pairs that have the same two
nucleotides in the first and second positions
and differ only at the third base, where the
synonymous codons either both carry a
purine (A or G) or both carry a pyrimidine (C
or U). For example, consider the synonymous
pairs of codons for histidine (His) and
glutamine (Gln; see Figure 9.13). The first
two bases of each of these codons are C and
A. Both His codons have a pyrimi dine at the
third position, whereas the Gln codons have a
purine in the third position. As you look at
other pairs of synonymous codons in the
genetic code information inside the book
front cover, notice that they also differ only
by car rying the alternative purine or
pyrimidine nucleotide at the third position.
Amino acids specified by four synonymous
codons, such as alanine (Ala), valine (Val),
and glycine (Gly), display an analogous
pattern: Each amino acid is represented by
two pairs of synonymous codons, and the
members of each pair differ in the third
position only, by carrying the alter nate
purine or pyrimidine. The pattern continues
in argi nine (Arg), serine (Ser), and leucine
(Leu), each of which is specified by six
synonymous codons. These sets of codons
each consist of three pairs, each pair having
the same nucleotides in the first two
positions and differing by hav ing the
alternate purine or pyrimidine in the third
position. Third-base wobble occurs through
flexible base pair ing between the wobble
nucleotide—that is, the 3′ nucleo tide of a
codon—and the 5′ nucleotide of an anticodon.
At the wobble position, base pairing between
the nucleo tides of the codon and the
anticodon need not be comple mentary. They
must, however, involve a purine and a
pyrimidine. Third-base wobble pairings are
summarized in Table 9.6. The wobble
nucleotides in different anticodons include all
the RNA nucleotides and also the modified
nucleotide inosine (I). Inosine is structurally
similar to G but lacks the amino group
attached to guanine’s 2 carbon. Because of
this difference, inosine base-pairs with either
purines or pyrimidines. Figure 9.15 shows
three examples of
third-base
wobble, in which
three tRNA
molecules col
lectively
recognize seven
different codons.
Translation Is Followed by Polypeptide Folding,
Processing, and Protein Sorting:
Translation produces polypeptides, but the
production of functional proteins is not
complete until the polypeptides are folded
into their functional tertiary or quaternary
structures. Recall from Section 9.1 that these
steps involve the formation of ionic or
covalent bonds, and they may also involve
specific chemical modifications of amino acids
in polypeptides. In addition, two other
categories of post translational events
provide further modifications and sort the
proteins for transport to their destinations.
Posttranslational Polypeptide Processing:
The removal of one or more amino acids from
a polypep tide is a common form of
posttranslational polypeptide processing.
Earlier in the chapter, we identified AUG as
the usual start codon and noted that it
encodes the modified amino acid N-
formylmethionine (fMet) in bacterial cells and
methionine in eukaryotes. Yet fMet is never
found in func tional bacterial proteins, and
amino acids other than me thionine are
frequently the first amino acid of
polypeptides in eukaryotes. The absence of
fMet from functional bacterial proteins is the
result of posttranslational cleavage of fMet
from each bacterial polypeptide (Figure
9.20a). Similarly, methionine is usually
removed as part of posttranslational
processing in eukaryotes, and the new N-
terminal amino acid is acetylated as part of
the process. In addition to N-terminal amino
acids, other amino acid residues can be
chemically modified as well. One of the most
common modifications of individual amino ac
ids is performed by enzymes known as
kinases that carry out phosphorylation of
proteins by adding a phosphate group to
individual amino acids (Figure 9.20b). This is
an important regulatory process that can
switch a protein from an inactive to an active
form, or vice versa. Other enzymes may add
methyl groups, hydroxyl groups, or acetyl
groups to individual amino acids of
polypeptides. The addition of carbohydrate
side chains to polypeptides to form a
glycoprotein is another important kind of
post translational modification. For example,
in one kind ofposttranslational modification,
the H substance is altered by the protein
products of the IA
and IB alleles of
the ABO blood
group gene (see
Section 4.1).
Posttranslational
processing may
also include the
cleavage of a
polypeptide into
multiple segments
that each form
functional proteins
or that aggregate
after elimination
of one or more
segments to form
a functional
protein.
Production of the
hormone insulin,
which fa cilitates
transport of glucose
into cells, includes two post translational
modification steps that remove segments of
the original polypeptide (Figure 9.20c). The
polypep tide product translated from the
insulin gene is called preproinsulin. It is an
inactive protein that contains a leader
segment, called the pre–amino acid segment,
at the N-terminal end and a connecting
segment, called the pro–amino acid segment,
that separates the A-chain seg ment and the
B-chain segment, the two functional pieces of
the polypeptide. During posttranslational
processing of preproinsulin, the pre–amino
acids of the signal se quence are removed,
after the polypeptide is transported through
the cell membrane, to form proinsulin. Three
disulfide bonds form within and between the
A-chain and B-chain segments, followed by
polypeptide cleavage that removes the pro–
amino acid segment. What results is a
functional insulin molecule consisting of 20
amino acids in the A-chain segment and 31
amino acids in the B-chain segment.

The Signal Hypothesis:

Like the passengers in a busy airline
terminal, the pro teins produced in a cell
have different destinations, to which they
travel
with
the
aid of
a

“ticket” that tells the cell where to transport

them. The destination is often an organelle or
the cell membrane; in certain cases, the
polypeptide is destined for transport out of
the cell. The ticket that communicates the
destination of a polypeptide is a signal
sequence of 15 to 20 or so amino acids at the
N-terminal end. First articulated in the early
1970s by Gunther Blobel, the signal
hypothesis proposes that the first 15 to 20
amino acids of many polypeptides contain an
“address label” in the form of a signal
sequence that designates the protein’s
destination in the cell. Blobel’s hypothesis
proposed that the signal sequence directs
proteins to the endoplasmic reticulum (ER),
where they are sorted for their cellular
destinations. Blobel’s signal hypothesis is
now a widely accepted model for the
identification of the cellular destina tions of
proteins. In fact, follow-up research has
identi fied the mechanism by which proteins
are processed and packaged for export from
a cell. While proteins destined to remain in a
cell are typically translated at “free”
ribosomes (ribosomes that float freely in the
cy toplasm), large numbers of ribosomes are
attached to the rough endoplasmic reticulum
(rough ER) where pro teins destined for
intercellular transport are translated. Figure
9.21 illustrates the translation of
polypeptides
into the cisternal space of the rough ER
where the poly peptides are processed and
packaged for transport to the Golgi
apparatus. In the Golgi apparatus additional
protein processing takes place and the
proteins are packaged into vesicles for
transport to the intercellular destinations.
 Table Of Contents
1)Certificate
2)Declaration
3)Aknowledgement
4)Aim of the
project
5)Introduction
6)Structure Of trna
7)The Central
Dogma
8)Frequently asked
Questions
9)Components and
steps of
translation
10)Translation
Mechanism
11)Bibliography

Bibliography
Books:
1. Trueman’s Elementary Biology for Class 12 and NEET
by K.N. Bhatia and M.P. Tyagi
2. S. Chand’s Biology for class XII by B.P. Pandey
3. Together with Biology by S. Chand, Biology by
Campbell and Reece - 2023-24
4. NCERT Class 12 Biology Textbook

Websites:
1. [Link]
2. [Link]
3. [Link]