Biosintesis Protein

MK. Biokimia
Universitas Udayana

I Nengah Wirajana
Email: nwirajana@gmail.com
Pendahuluan
Anda telah mengetahui bagaimana DNA
direplikasi dan bagaimana DNA ditranskripsi
menjadi RNA.
Kita sekarang akan mempelajari mekanisme
sintesis protein, suatu proses yang disebut
translasi karena empat-hurup alfabet asam
nukleat (GACT) ditranslit menjadi dua puluh
hurup alfabet protein (20 asam amino).
Translasi terjadi dalam ribosom.
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Pendahuluan
Protein Assembly. The ribosome, shown at the right, is a factory for the manufacture of
polypeptides. Amino acids are carried into the ribosome, one at a time, connected to transfer RNA
molecules (blue). Each amino acid is joined to the growing polypeptide chain, which detaches
from the ribosome only once it is completed. This assembly line approach allows even very long
polypeptide chains to be assembled rapidly and with impressive accuracy. [(Left) Doug
Martin/Photo Researchers.]
Sumber :
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Kodon

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Codon Reading Frame
AUG is always the
start codon so all
polypeptides begin
with Methionine
when they are
synthesized
Having a consistent
start codon is
necessary so that
the reading frame
is always the same.
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1. Translasi Urutan Nukleotida
Menjadi Urutan asam Amino
Dasar sintesis protein sama pada
semua mahluk hidup (all kingdoms of
life), menunjukkan fakta bahwa sistem
sintesis protein muncul paling awal
dalam evolusi.
Protein disintesis dalam arah dari
amino-ke-karboksil, dengan
penambahan secara berurutan asam
amino pada ujung karboksil dari rantai
peptida yang sedang tumbuh (lihat
Gambar berikut).
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1. Translasi Urutan Nukleotida Menjadi Urutan asam Amino
Pertumbuhan rantai polipeptida. Protein
disintesis dengan penambahan berurutan
asam amino pada terminal/ujung karboksil.
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1.1. The Synthesis of Long Proteins Requires a
Low Error Frequency
The process of transcription is analogous
to copying, word for word, a page from a
book.
There is no change of alphabet or
vocabulary; so the likelihood of a change
in meaning is small.
Translating the base sequence of an
mRNA molecule into a sequence of amino
acids is similar to translating the page of a
book into another language.
Translation is a complex process,
entailing many steps and dozens of
molecules. The potential for error exists at
each step.
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1.1. The Synthesis of Long Proteins Requires a
Low Error Frequency
The complexity of translation creates a conflict
between two requirements: the process must be not
only accurate, but also fast enough to meet a cell's
needs.
How fast is "fast enough"? In E.coli, translation takes
place at a rate of 40 amino acids per second, a truly
impressive speed considering the complexity of the
process.
How accurate must protein synthesis be? Let us
consider error rates. The probability p of forming a
protein with no errors depends on n, the number of
amino acid residues, and e, the frequency of insertion
of a wrong amino acid:
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1.1.The Synthesis of Long Proteins Requires a Low Error Frequency
Table 1. Accuracy of protein synthesis







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1.2. Transfer RNA Molecules
Have a Common Design
The fidelity of protein synthesis requires the
accurate recognition of three-base codons on
messenger RNA.
Recall that the genetic code relates each amino
acid to a three-letter codon.
An amino acid cannot itself recognize a codon.
Consequently, an amino acid is attached to a
specific tRNA molecule that can recognize the
codon by Watson-Crick base pairing.
Transfer RNA serves as the adapter molecule
that binds to a specific codon and brings with it
an amino acid for incorporation into the
polypeptide chain.
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1.3. The Activated Amino Acid and the Anticodon
of tRNA Are at Opposite Ends of
the L-Shaped Molecule
The most important properties of the tRNA structure are:
1. The molecule is L-shaped (Figure 29.5).
2. There are two apparently continuous segments of double helix.
These segments are like A-form DNA, as expected for an RNA
helix . The base-pairing predicted from the sequence analysis is
correct. The helix containing the 5 and 3 ends stacks on top of the
helix that ends in the TyC loop to form one arm of the L; the
remaining two helices stack to form the other (Figure 29.6).
3. Most of the bases in the nonhelical regions participate in
hydrogenbonding interactions, even if the interactions are not
like those in Watson-Crick base pairs.
4. The CCA terminus containing the amino acid attachment site
extends from one end of the L. This single-stranded region can
change conformation during amino acid activation and protein
synthesis.
5. The anticodon loop is at the other end of the L, making
accessible the three bases that make up the anticodon.
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1.3. The Activated Amino Acid and the Anticodon of tRNA Are at Opposite
Ends of the L-Shaped Molecule
Figure 29.4. General Structure of tRNA Molecules. Comparison of the base
sequences of many tRNAs reveals a number of conserved features.
29.5. L-Shaped tRNA Structure. A skeletal model of yeast phenylalanyl-tRNA reveals
the L-shaped structure. The CCA region is at the end of one arm, and the anticodon loop
is at the end of the other.
Figure 29.6. Helix Stacking in tRNA. The four helices of the secondary structure of
tRNA (see Figure 29.4) stack to form an L-shaped structure.
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2. Aminoacyl-Transfer RNA Synthetases
Read the Genetic Code
The linkage of an amino acid to a tRNA is crucial for
two reasons.
First, the attachment of a given amino acid to a particular
tRNA establishes the genetic code. When an amino acid
has been linked to a tRNA, it will be incorporated into a
growing polypeptide chain at a position dictated by the
anticodon of the tRNA.
Second, the formation of a peptide bond between free
amino acids is not thermodynamically favorable. The
amino acid must first be activated for protein synthesis to
proceed.
The activated intermediates in protein synthesis are
amino acid esters, in which the carboxyl group of an
amino acid is linked to either the 2 - or the 3 -hydroxyl
group of the ribose unit at the 3 end of tRNA.
An amino acid ester of tRNA is called an aminoacyl-tRNA
or sometimes a charged tRNA.
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2.1. Amino Acids Are First
Activated by Adenylation
The activation reaction is catalyzed by specific
aminoacyl-tRNA synthetases, which are also called
activating enzymes.
The first step is the formation of an aminoacyl
adenylate from an amino acid and ATP.
This activated species is a mixed anhydride in which
the carboxyl group of the amino acid is linked to the
phosphoryl group of AMP; hence, it is also known as
aminoacyl-AMP.
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The next step is the transfer of the
aminoacyl group of aminoacyl-AMP to a
particular tRNA molecule to form
aminoacyl-tRNA.


The sum of these activation and transfer
steps is
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Post Translation

Protein structure is determined by
amino acid sequence and modifications
Modifications include
The attachment of certain sugars, lipids, or
phosphate groups
Joining different subunits of the protein to
create the quaternary structure
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Point Mutations
The change of a single nucleotide in the
DNAs template strand
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Two Types of Mutation
Substitutions
Replacing one or more base with others
Insertions or Deletions
Adding or removing one or more base
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Terima kasih,
Selamat belajar.
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