biosynthesis of proteins on ribosomes
DESCRIPTION
Biosynthesis of proteins on ribosomes. GENETIC CODE - sequence of mononucleotides in mRNA that specifies the sequence of amino acids in peptide chain. CODON – mRNA triplet base sequence responsible for 1 amino acid. PROPERTIES OF GENETIC CODE. - PowerPoint PPT PresentationTRANSCRIPT
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Biosynthesis of Biosynthesis of proteins on proteins on ribosomesribosomes
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GENETIC CODE - sequence of mononucleotides in mRNA that specifies the sequence of amino acids in peptide chain
CODON – mRNA triplet base sequence responsible for 1 amino acid
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PROPERTIES OF GENETIC CODE
1. Unambiguous. In any organism each codon corresponds to only one amino acid.
2. Code is degenerate. There are multiple codons for most amino acids.
3. Universal. Codons are the same for all organism.
4. Without punctuation. There are no punctuations between trinucleotides.
5. Nonoverlapping. Codons do not overlap each other.
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Structure of tRNAs
ANTICODON – triplet in tRNA that can complementary bind to codon of mRNA.
Such base pairing between codon and anticodon is responsible for the translation of genetic information from mRNA to protein.
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STAGES OF TRANSLATION
• 1. Recognition• 2. Initiation
• 3. Elongation• 4. Termination
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R1 CH
NH2
COOH + HO P
O
O
OH
P
O
O
OH
P
O
OH
O Аденозин
R1 CH
NH2
CO P
O
O
OH
Аденозин + H4P2O7O
Aminoacyladenilate
RECOGNITION
Aminoacyl-tRNA-synthetase
Aminoacyladenilate + tRNA aminoacyl-tRNA + AMP
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Activation of amino acids
Each amino acid has a specific tRNA
There is specific aminoacyl-tRNA-synthetase for each AA
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The structure of tRNA
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Initiation of Translation•The translation complex is
assembled at the beginning of the mRNA coding sequence
•Complex consists of: -Ribosomal subunits-mRNA template to be
translated-Initiator tRNA molecule-Protein initiation factors
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Initiator tRNA
•First codon translated is usually AUG
•The initiator tRNA recognizes initiation codons
-Bacteria: N-formylmethionyl-tRNA
-Eukaryotes: methionyl-tRNA
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Initiation of protein bio-synthesis Methionyl-тRNA binds to P-center
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Sites for tRNA binding in ribosomes
There are two centers: peptidyl (P) and aminoacyl (А)
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Elongation1) Positioning of the nextaminoacyl-tRNA in the A site 2) Formation of the peptide bound (enzyme – peptidyl transferase) between methionine and AA in A-centre. The residue of methionine is transferred on the amino group of another AA
3) Translocation – shift of ribosome by one codon. Methionyl-tRNA is released from P-centre. Dipeptidyl-tRNA moves from A-centre to P-centre.
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Termination of Translation
•Ribosome comes to terminal codon UGA, UAG or UAA
•No tRNA molecules recognize these codons and protein synthesis stalls
•Protein termination factors F-1, RF-2, RF-3 split off synthesized polypeptide from the last tRNA
•Ribosomal complex dissociates
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Termina-tion of Trans-lation
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POSTTRANSLATIONAL MODIFICATION
1) Preparing of proteins for different functions
2) Direction of proteins to different locations (targeting)
1. Removing of methionine (formylmethionine)
2. Formation of disulfide and other bonds (secondary, tertiary structures)
3. Proteolytic cleavage
4. Modification of amino acid residues:
- Hydroxylation
- Glycosilation
- Phosphorilation
5. Joining of prosthetic groups or cofactors
6. Formation of the quaternary structure
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Regulation of the Protein BiosynthesisThe operon model (by Jacob and Monod)
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Inhibitors of Transcription
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Antibiotics inhibiting protein
synthesis