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Peptidyl transferase inhibition by the nascent leader peptide of an inducible cat gene.

Identifieur interne : 004513 ( Main/Exploration ); précédent : 004512; suivant : 004514

Peptidyl transferase inhibition by the nascent leader peptide of an inducible cat gene.

Auteurs : Z. Gu ; E J Rogers ; P S Lovett

Source :

RBID : pubmed:7690023

Descripteurs français

English descriptors

Abstract

The site of ribosome stalling in the leader of cat transcripts is critical to induction of downstream translation. Site-specific stalling requires translation of the first five leader codons and the presence of chloramphenicol, a sequence-independent inhibitor of ribosome elongation. We demonstrate in this report that a synthetic peptide (the 5-mer) corresponding to the N-terminal five codons of the cat-86 leader inhibits peptidyl transferase in vitro. The N-terminal 2-, 3-, and 4-mers and the reverse 5-mer (reverse amino acid sequence of the 5-mer) are virtually without effect on peptidyl transferase. A missense mutation in the cat-86 leader that abolishes induction in vivo corresponds to an amino acid replacement in the 5-mer that completely relieves peptidyl transferase inhibition. In contrast, a missense mutation that does not interfere with in vivo induction corresponds to an amino acid replacement in the 5-mer that does not significantly alter peptidyl transferase inhibition. Our results suggest that peptidyl transferase inhibition by the nascent cat-86 5-mer peptide may be the primary determinant of the site of ribosome stalling in the leader. A model based on this concept can explain the site specificity of ribosome stalling as well as the response of induction to very low levels of the antibiotic inducer.

DOI: 10.1128/jb.175.17.5309-5313.1993
PubMed: 7690023


Affiliations:

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Le document en format XML

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<nlm:affiliation>Department of Biological Sciences, University of Maryland Baltimore County, Catonsville 21228.</nlm:affiliation>
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<term>Amino Acid Sequence</term>
<term>Bacillus subtilis (enzymology)</term>
<term>Bacillus subtilis (genetics)</term>
<term>Base Sequence</term>
<term>Chloramphenicol (pharmacology)</term>
<term>Chloramphenicol O-Acetyltransferase (genetics)</term>
<term>Chloramphenicol O-Acetyltransferase (metabolism)</term>
<term>Drug Resistance, Microbial (genetics)</term>
<term>Enzyme Induction</term>
<term>Erythromycin (pharmacology)</term>
<term>Kinetics</term>
<term>Lincomycin (pharmacology)</term>
<term>Molecular Sequence Data</term>
<term>Peptidyl Transferases (antagonists & inhibitors)</term>
<term>Peptidyl Transferases (drug effects)</term>
<term>Protein Sorting Signals (genetics)</term>
<term>Protein Sorting Signals (metabolism)</term>
<term>RNA, Bacterial</term>
<term>Ribosomes (metabolism)</term>
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<term>ARN bactérien</term>
<term>Bacillus subtilis (enzymologie)</term>
<term>Bacillus subtilis (génétique)</term>
<term>Chloramphenicol O-acetyltransferase (génétique)</term>
<term>Chloramphenicol O-acetyltransferase (métabolisme)</term>
<term>Chloramphénicol (pharmacologie)</term>
<term>Cinétique</term>
<term>Données de séquences moléculaires</term>
<term>Induction enzymatique</term>
<term>Lincomycine (pharmacologie)</term>
<term>Peptidyl transferases ()</term>
<term>Peptidyl transferases (antagonistes et inhibiteurs)</term>
<term>Ribosomes (métabolisme)</term>
<term>Résistance microbienne aux médicaments (génétique)</term>
<term>Signaux de triage des protéines (génétique)</term>
<term>Signaux de triage des protéines (métabolisme)</term>
<term>Séquence d'acides aminés</term>
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<term>Peptidyl Transferases</term>
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<term>Chloramphenicol O-Acetyltransferase</term>
<term>Protein Sorting Signals</term>
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<term>Chloramphenicol</term>
<term>Erythromycin</term>
<term>Lincomycin</term>
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<term>Peptidyl transferases</term>
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<term>Chloramphenicol O-acetyltransferase</term>
<term>Résistance microbienne aux médicaments</term>
<term>Signaux de triage des protéines</term>
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<term>Ribosomes</term>
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<term>Données de séquences moléculaires</term>
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<term>Séquence d'acides aminés</term>
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<div type="abstract" xml:lang="en">The site of ribosome stalling in the leader of cat transcripts is critical to induction of downstream translation. Site-specific stalling requires translation of the first five leader codons and the presence of chloramphenicol, a sequence-independent inhibitor of ribosome elongation. We demonstrate in this report that a synthetic peptide (the 5-mer) corresponding to the N-terminal five codons of the cat-86 leader inhibits peptidyl transferase in vitro. The N-terminal 2-, 3-, and 4-mers and the reverse 5-mer (reverse amino acid sequence of the 5-mer) are virtually without effect on peptidyl transferase. A missense mutation in the cat-86 leader that abolishes induction in vivo corresponds to an amino acid replacement in the 5-mer that completely relieves peptidyl transferase inhibition. In contrast, a missense mutation that does not interfere with in vivo induction corresponds to an amino acid replacement in the 5-mer that does not significantly alter peptidyl transferase inhibition. Our results suggest that peptidyl transferase inhibition by the nascent cat-86 5-mer peptide may be the primary determinant of the site of ribosome stalling in the leader. A model based on this concept can explain the site specificity of ribosome stalling as well as the response of induction to very low levels of the antibiotic inducer.</div>
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