Peptidyl transferase inhibition by the nascent leader peptide of an inducible cat gene.
Identifieur interne : 002770 ( PubMed/Checkpoint ); précédent : 002769; suivant : 002771Peptidyl transferase inhibition by the nascent leader peptide of an inducible cat gene.
Auteurs : Z. Gu ; E J Rogers ; P S LovettSource :
- Journal of bacteriology [ 0021-9193 ] ; 1993.
Descripteurs français
- KwdFr :
- ARN bactérien, Bacillus subtilis (enzymologie), Bacillus subtilis (génétique), Chloramphenicol O-acetyltransferase (génétique), Chloramphenicol O-acetyltransferase (métabolisme), Chloramphénicol (pharmacologie), Cinétique, Données de séquences moléculaires, Induction enzymatique, Lincomycine (pharmacologie), Peptidyl transferases (), Peptidyl transferases (antagonistes et inhibiteurs), Ribosomes (métabolisme), Résistance microbienne aux médicaments (génétique), Signaux de triage des protéines (génétique), Signaux de triage des protéines (métabolisme), Séquence d'acides aminés, Séquence nucléotidique, Érythromycine (pharmacologie).
- MESH :
- antagonistes et inhibiteurs : Peptidyl transferases.
- enzymologie : Bacillus subtilis.
- génétique : Bacillus subtilis, Chloramphenicol O-acetyltransferase, Résistance microbienne aux médicaments, Signaux de triage des protéines.
- métabolisme : Chloramphenicol O-acetyltransferase, Ribosomes, Signaux de triage des protéines.
- pharmacologie : Chloramphénicol, Lincomycine, Érythromycine.
- ARN bactérien, Cinétique, Données de séquences moléculaires, Induction enzymatique, Peptidyl transferases, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence, Bacillus subtilis (enzymology), Bacillus subtilis (genetics), Base Sequence, Chloramphenicol (pharmacology), Chloramphenicol O-Acetyltransferase (genetics), Chloramphenicol O-Acetyltransferase (metabolism), Drug Resistance, Microbial (genetics), Enzyme Induction, Erythromycin (pharmacology), Kinetics, Lincomycin (pharmacology), Molecular Sequence Data, Peptidyl Transferases (antagonists & inhibitors), Peptidyl Transferases (drug effects), Protein Sorting Signals (genetics), Protein Sorting Signals (metabolism), RNA, Bacterial, Ribosomes (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Peptidyl Transferases.
- chemical , drug effects : Peptidyl Transferases.
- chemical , genetics : Chloramphenicol O-Acetyltransferase, Protein Sorting Signals.
- chemical , metabolism : Chloramphenicol O-Acetyltransferase, Protein Sorting Signals.
- chemical , pharmacology : Chloramphenicol, Erythromycin, Lincomycin.
- enzymology : Bacillus subtilis.
- genetics : Bacillus subtilis, Drug Resistance, Microbial.
- metabolism : Ribosomes.
- Amino Acid Sequence, Base Sequence, Enzyme Induction, Kinetics, Molecular Sequence Data, RNA, Bacterial.
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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Gu</name><affiliation><nlm:affiliation>Department of Biological Sciences, University of Maryland Baltimore County, Catonsville 21228.</nlm:affiliation><wicri:noCountry code="subField">Catonsville 21228</wicri:noCountry></affiliation></author><author><name sortKey="Rogers, E J" sort="Rogers, E J" uniqKey="Rogers E" first="E J" last="Rogers">E J Rogers</name></author><author><name sortKey="Lovett, P S" sort="Lovett, P S" uniqKey="Lovett P" first="P S" last="Lovett">P S Lovett</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1993">1993</date><idno type="RBID">pubmed:7690023</idno><idno type="pmid">7690023</idno><idno type="doi">10.1128/jb.175.17.5309-5313.1993</idno><idno type="wicri:Area/PubMed/Corpus">002912</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002912</idno><idno type="wicri:Area/PubMed/Curation">002912</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002912</idno><idno type="wicri:Area/PubMed/Checkpoint">002770</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002770</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Peptidyl transferase inhibition by the nascent leader peptide of an inducible cat gene.</title><author><name sortKey="Gu, Z" sort="Gu, Z" uniqKey="Gu Z" first="Z" last="Gu">Z. Gu</name><affiliation><nlm:affiliation>Department of Biological Sciences, University of Maryland Baltimore County, Catonsville 21228.</nlm:affiliation><wicri:noCountry code="subField">Catonsville 21228</wicri:noCountry></affiliation></author><author><name sortKey="Rogers, E J" sort="Rogers, E J" uniqKey="Rogers E" first="E J" last="Rogers">E J Rogers</name></author><author><name sortKey="Lovett, P S" sort="Lovett, P S" uniqKey="Lovett P" first="P S" last="Lovett">P S Lovett</name></author></analytic><series><title level="j">Journal of bacteriology</title><idno type="ISSN">0021-9193</idno><imprint><date when="1993" type="published">1993</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><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 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scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Ribosomes</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Chloramphenicol O-acetyltransferase</term><term>Ribosomes</term><term>Signaux de triage des protéines</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Chloramphénicol</term><term>Lincomycine</term><term>Érythromycine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Base Sequence</term><term>Enzyme Induction</term><term>Kinetics</term><term>Molecular Sequence Data</term><term>RNA, Bacterial</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>ARN bactérien</term><term>Cinétique</term><term>Données de séquences moléculaires</term><term>Induction enzymatique</term><term>Peptidyl transferases</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><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></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">7690023</PMID><DateCompleted><Year>1993</Year><Month>10</Month><Day>01</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>08</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9193</ISSN><JournalIssue CitedMedium="Print"><Volume>175</Volume><Issue>17</Issue><PubDate><Year>1993</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Journal of bacteriology</Title><ISOAbbreviation>J. Bacteriol.</ISOAbbreviation></Journal><ArticleTitle>Peptidyl transferase inhibition by the nascent leader peptide of an inducible cat gene.</ArticleTitle><Pagination><MedlinePgn>5309-13</MedlinePgn></Pagination><Abstract><AbstractText>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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Gu</LastName><ForeName>Z</ForeName><Initials>Z</Initials><AffiliationInfo><Affiliation>Department of Biological Sciences, University of Maryland Baltimore County, Catonsville 21228.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rogers</LastName><ForeName>E J</ForeName><Initials>EJ</Initials></Author><Author ValidYN="Y"><LastName>Lovett</LastName><ForeName>P S</ForeName><Initials>PS</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>GM-42925</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Bacteriol</MedlineTA><NlmUniqueID>2985120R</NlmUniqueID><ISSNLinking>0021-9193</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D021382">Protein Sorting Signals</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012329">RNA, Bacterial</NameOfSubstance></Chemical><Chemical><RegistryNumber>63937KV33D</RegistryNumber><NameOfSubstance UI="D004917">Erythromycin</NameOfSubstance></Chemical><Chemical><RegistryNumber>66974FR9Q1</RegistryNumber><NameOfSubstance UI="D002701">Chloramphenicol</NameOfSubstance></Chemical><Chemical><RegistryNumber>BOD072YW0F</RegistryNumber><NameOfSubstance UI="D008034">Lincomycin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.3.1.28</RegistryNumber><NameOfSubstance UI="D015500">Chloramphenicol O-Acetyltransferase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.3.2.12</RegistryNumber><NameOfSubstance UI="D010458">Peptidyl Transferases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><GeneSymbolList><GeneSymbol>cat</GeneSymbol></GeneSymbolList><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001412" MajorTopicYN="N">Bacillus subtilis</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002701" MajorTopicYN="N">Chloramphenicol</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015500" MajorTopicYN="N">Chloramphenicol O-Acetyltransferase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004352" MajorTopicYN="N">Drug Resistance, Microbial</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004790" MajorTopicYN="N">Enzyme Induction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004917" MajorTopicYN="N">Erythromycin</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008034" MajorTopicYN="N">Lincomycin</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010458" MajorTopicYN="N">Peptidyl Transferases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D021382" MajorTopicYN="N">Protein Sorting Signals</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012329" MajorTopicYN="N">RNA, Bacterial</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012270" MajorTopicYN="N">Ribosomes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1993</Year><Month>9</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1993</Year><Month>9</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1993</Year><Month>9</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">7690023</ArticleId><ArticleId IdType="pmc">PMC206583</ArticleId><ArticleId IdType="doi">10.1128/jb.175.17.5309-5313.1993</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>J Mol Biol. 1965 Nov;14(1):63-70</Citation><ArticleIdList><ArticleId IdType="pubmed">5327658</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Microbiol. 1993 Jun;8(6):1063-9</Citation><ArticleIdList><ArticleId 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Gu</name><name sortKey="Lovett, P S" sort="Lovett, P S" uniqKey="Lovett P" first="P S" last="Lovett">P S Lovett</name><name sortKey="Rogers, E J" sort="Rogers, E J" uniqKey="Rogers E" first="E J" last="Rogers">E J Rogers</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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