A two‐component signal‐transducing system is involved in competence and penicillin susceptibility in laboratory mutants of Streptococcus pneumoniae

Summary Penicillin resistance in Streptococcus pneumoniae has been attributed so far to the production of penicillin‐binding protein (PBP) variants with decreased affinities for β‐lactam antibiotics. Cefotaxime‐resistant laboratory mutants, selected after several steps on increasing concentrations o...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Molecular microbiology 1994-05, Vol.12 (3), p.505-515
Hauptverfasser: Guenzi, Eric, Gasc, Anne‐Marie, Sicard, Michel A., Hakenbeck, Regine
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 515
container_issue 3
container_start_page 505
container_title Molecular microbiology
container_volume 12
creator Guenzi, Eric
Gasc, Anne‐Marie
Sicard, Michel A.
Hakenbeck, Regine
description Summary Penicillin resistance in Streptococcus pneumoniae has been attributed so far to the production of penicillin‐binding protein (PBP) variants with decreased affinities for β‐lactam antibiotics. Cefotaxime‐resistant laboratory mutants, selected after several steps on increasing concentrations of this β‐lactam, become deficient in transformation as well. A DNA fragment conferring both cefotaxime resistance and transformation deficiency was isolated and cloned from the mutant C306. The cefotaxime resistance associated with this resistance determinant was not accompanied with apparent changes in PBP properties, and it mapped on the chromosome distinct from the known resistance determinants, genes encoding PBP2x, PBP1a or PBP2b. Determination of a 2265 bp DNA sequence of the resistance determinant revealed two open reading frames, claR and claH, whose deduced amino acid sequence identified the corresponding proteins as the response regulator and histidine kinase receptor, respectively (members of the two families of bacterial signal‐transducing proteins). Two hydrophobic peptide regions divided the histidine kinase ClaH into two putative domains: an N‐terminal extracelluiar sensor part, and an intracelluiar C‐terminal domain with the conserved His‐226 residue, the presumed phosphorylation site. The single point mutations responsible for cefotaxime‐resistance and transformation deficiency of C306 and of another two independently isolated cefotaxime‐resistant mutants were each located in the C‐terminal half of ClaH. A small extracellular protein, the competence factor, is required for induction of competence. Neither C306 nor the transformants obtained with the mutated claH gene produced competence factor, and exogenous competence factor could not complement the transformation deficiency, indicating that the signal‐transducing system cia is involved in early steps of competence regulation.
doi_str_mv 10.1111/j.1365-2958.1994.tb01038.x
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_16908734</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>16908734</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4105-1c41b29fe42aa594ed922ab81653e5b15513b8848365a1769ad29b0941430c213</originalsourceid><addsrcrecordid>eNqVUcFu1DAUtBCoLIVPQLIQ6i3BjuOszQGpqqBUasUBkLhZjvO28sqxQ-y0zY1P4Mb_8SV12Gjv-PIsz8zzaAahN5SUNJ93-5KyhheV5KKkUtZlagklTJQPT9DmCD1FGyI5KZiofjxHL2LcE0IZadgJOhGk4VWz3aA_5zjdh7-_fpvQD8GDTzjaW69dfkqj9rGbjPW3OM4xQY9txNbfBXcHXb7gRQQJvAGsfYcH8NZY5zISp2hgSLa1zqZ54TrdhlGnMM64n5L2KeKww1_TmGnBBGOmiAcPUx-81fASPdtpF-HVOk_R908fv118Lq6_XF5dnF8XpqaEFzSPtpI7qCutuayhk1WlW0EbzoC3lHPKWiFqkUPRdNtI3VWyJbKmNSOmouwUnR32DmP4OUFMqrfZuXPaQ5iioo0kYsvqTHx_IJoxxDjCTg2j7fU4K0rU0oraqyV6tUSvllbU2op6yOLX6y9T20N3lK41ZPztiutotNvl4I2NR1pNRNP8M_vhQLu3Dub_MKBubq444ewRgbSvYw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>16908734</pqid></control><display><type>article</type><title>A two‐component signal‐transducing system is involved in competence and penicillin susceptibility in laboratory mutants of Streptococcus pneumoniae</title><source>MEDLINE</source><source>Access via Wiley Online Library</source><creator>Guenzi, Eric ; Gasc, Anne‐Marie ; Sicard, Michel A. ; Hakenbeck, Regine</creator><creatorcontrib>Guenzi, Eric ; Gasc, Anne‐Marie ; Sicard, Michel A. ; Hakenbeck, Regine</creatorcontrib><description>Summary Penicillin resistance in Streptococcus pneumoniae has been attributed so far to the production of penicillin‐binding protein (PBP) variants with decreased affinities for β‐lactam antibiotics. Cefotaxime‐resistant laboratory mutants, selected after several steps on increasing concentrations of this β‐lactam, become deficient in transformation as well. A DNA fragment conferring both cefotaxime resistance and transformation deficiency was isolated and cloned from the mutant C306. The cefotaxime resistance associated with this resistance determinant was not accompanied with apparent changes in PBP properties, and it mapped on the chromosome distinct from the known resistance determinants, genes encoding PBP2x, PBP1a or PBP2b. Determination of a 2265 bp DNA sequence of the resistance determinant revealed two open reading frames, claR and claH, whose deduced amino acid sequence identified the corresponding proteins as the response regulator and histidine kinase receptor, respectively (members of the two families of bacterial signal‐transducing proteins). Two hydrophobic peptide regions divided the histidine kinase ClaH into two putative domains: an N‐terminal extracelluiar sensor part, and an intracelluiar C‐terminal domain with the conserved His‐226 residue, the presumed phosphorylation site. The single point mutations responsible for cefotaxime‐resistance and transformation deficiency of C306 and of another two independently isolated cefotaxime‐resistant mutants were each located in the C‐terminal half of ClaH. A small extracellular protein, the competence factor, is required for induction of competence. Neither C306 nor the transformants obtained with the mutated claH gene produced competence factor, and exogenous competence factor could not complement the transformation deficiency, indicating that the signal‐transducing system cia is involved in early steps of competence regulation.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1111/j.1365-2958.1994.tb01038.x</identifier><identifier>PMID: 8065267</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Amino Acid Sequence ; Antibacterial agents ; Antibiotics. Antiinfectious agents. Antiparasitic agents ; Bacterial Proteins ; Bacteriology ; Base Sequence ; Biological and medical sciences ; Cefotaxime - pharmacology ; Chromosome Mapping ; DNA Mutational Analysis ; Drug Resistance, Microbial - genetics ; Fundamental and applied biological sciences. Psychology ; Genetics ; Histidine Kinase ; Medical sciences ; Microbiology ; Molecular Sequence Data ; Mutagenesis, Insertional ; Mutation ; Penicillin Resistance - genetics ; Pharmacology. Drug treatments ; Piperacillin - pharmacology ; Protein Kinases - genetics ; Sequence Analysis, DNA ; Sequence Homology, Amino Acid ; Signal Transduction - genetics ; Streptococcus pneumoniae ; Streptococcus pneumoniae - genetics</subject><ispartof>Molecular microbiology, 1994-05, Vol.12 (3), p.505-515</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4105-1c41b29fe42aa594ed922ab81653e5b15513b8848365a1769ad29b0941430c213</citedby><cites>FETCH-LOGICAL-c4105-1c41b29fe42aa594ed922ab81653e5b15513b8848365a1769ad29b0941430c213</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1365-2958.1994.tb01038.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1365-2958.1994.tb01038.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=4086621$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8065267$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Guenzi, Eric</creatorcontrib><creatorcontrib>Gasc, Anne‐Marie</creatorcontrib><creatorcontrib>Sicard, Michel A.</creatorcontrib><creatorcontrib>Hakenbeck, Regine</creatorcontrib><title>A two‐component signal‐transducing system is involved in competence and penicillin susceptibility in laboratory mutants of Streptococcus pneumoniae</title><title>Molecular microbiology</title><addtitle>Mol Microbiol</addtitle><description>Summary Penicillin resistance in Streptococcus pneumoniae has been attributed so far to the production of penicillin‐binding protein (PBP) variants with decreased affinities for β‐lactam antibiotics. Cefotaxime‐resistant laboratory mutants, selected after several steps on increasing concentrations of this β‐lactam, become deficient in transformation as well. A DNA fragment conferring both cefotaxime resistance and transformation deficiency was isolated and cloned from the mutant C306. The cefotaxime resistance associated with this resistance determinant was not accompanied with apparent changes in PBP properties, and it mapped on the chromosome distinct from the known resistance determinants, genes encoding PBP2x, PBP1a or PBP2b. Determination of a 2265 bp DNA sequence of the resistance determinant revealed two open reading frames, claR and claH, whose deduced amino acid sequence identified the corresponding proteins as the response regulator and histidine kinase receptor, respectively (members of the two families of bacterial signal‐transducing proteins). Two hydrophobic peptide regions divided the histidine kinase ClaH into two putative domains: an N‐terminal extracelluiar sensor part, and an intracelluiar C‐terminal domain with the conserved His‐226 residue, the presumed phosphorylation site. The single point mutations responsible for cefotaxime‐resistance and transformation deficiency of C306 and of another two independently isolated cefotaxime‐resistant mutants were each located in the C‐terminal half of ClaH. A small extracellular protein, the competence factor, is required for induction of competence. Neither C306 nor the transformants obtained with the mutated claH gene produced competence factor, and exogenous competence factor could not complement the transformation deficiency, indicating that the signal‐transducing system cia is involved in early steps of competence regulation.</description><subject>Amino Acid Sequence</subject><subject>Antibacterial agents</subject><subject>Antibiotics. Antiinfectious agents. Antiparasitic agents</subject><subject>Bacterial Proteins</subject><subject>Bacteriology</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Cefotaxime - pharmacology</subject><subject>Chromosome Mapping</subject><subject>DNA Mutational Analysis</subject><subject>Drug Resistance, Microbial - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetics</subject><subject>Histidine Kinase</subject><subject>Medical sciences</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Insertional</subject><subject>Mutation</subject><subject>Penicillin Resistance - genetics</subject><subject>Pharmacology. Drug treatments</subject><subject>Piperacillin - pharmacology</subject><subject>Protein Kinases - genetics</subject><subject>Sequence Analysis, DNA</subject><subject>Sequence Homology, Amino Acid</subject><subject>Signal Transduction - genetics</subject><subject>Streptococcus pneumoniae</subject><subject>Streptococcus pneumoniae - genetics</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVUcFu1DAUtBCoLIVPQLIQ6i3BjuOszQGpqqBUasUBkLhZjvO28sqxQ-y0zY1P4Mb_8SV12Gjv-PIsz8zzaAahN5SUNJ93-5KyhheV5KKkUtZlagklTJQPT9DmCD1FGyI5KZiofjxHL2LcE0IZadgJOhGk4VWz3aA_5zjdh7-_fpvQD8GDTzjaW69dfkqj9rGbjPW3OM4xQY9txNbfBXcHXb7gRQQJvAGsfYcH8NZY5zISp2hgSLa1zqZ54TrdhlGnMM64n5L2KeKww1_TmGnBBGOmiAcPUx-81fASPdtpF-HVOk_R908fv118Lq6_XF5dnF8XpqaEFzSPtpI7qCutuayhk1WlW0EbzoC3lHPKWiFqkUPRdNtI3VWyJbKmNSOmouwUnR32DmP4OUFMqrfZuXPaQ5iioo0kYsvqTHx_IJoxxDjCTg2j7fU4K0rU0oraqyV6tUSvllbU2op6yOLX6y9T20N3lK41ZPztiutotNvl4I2NR1pNRNP8M_vhQLu3Dub_MKBubq444ewRgbSvYw</recordid><startdate>199405</startdate><enddate>199405</enddate><creator>Guenzi, Eric</creator><creator>Gasc, Anne‐Marie</creator><creator>Sicard, Michel A.</creator><creator>Hakenbeck, Regine</creator><general>Blackwell Publishing Ltd</general><general>Blackwell Science</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope></search><sort><creationdate>199405</creationdate><title>A two‐component signal‐transducing system is involved in competence and penicillin susceptibility in laboratory mutants of Streptococcus pneumoniae</title><author>Guenzi, Eric ; Gasc, Anne‐Marie ; Sicard, Michel A. ; Hakenbeck, Regine</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4105-1c41b29fe42aa594ed922ab81653e5b15513b8848365a1769ad29b0941430c213</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Antibacterial agents</topic><topic>Antibiotics. Antiinfectious agents. Antiparasitic agents</topic><topic>Bacterial Proteins</topic><topic>Bacteriology</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Cefotaxime - pharmacology</topic><topic>Chromosome Mapping</topic><topic>DNA Mutational Analysis</topic><topic>Drug Resistance, Microbial - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genetics</topic><topic>Histidine Kinase</topic><topic>Medical sciences</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Insertional</topic><topic>Mutation</topic><topic>Penicillin Resistance - genetics</topic><topic>Pharmacology. Drug treatments</topic><topic>Piperacillin - pharmacology</topic><topic>Protein Kinases - genetics</topic><topic>Sequence Analysis, DNA</topic><topic>Sequence Homology, Amino Acid</topic><topic>Signal Transduction - genetics</topic><topic>Streptococcus pneumoniae</topic><topic>Streptococcus pneumoniae - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Guenzi, Eric</creatorcontrib><creatorcontrib>Gasc, Anne‐Marie</creatorcontrib><creatorcontrib>Sicard, Michel A.</creatorcontrib><creatorcontrib>Hakenbeck, Regine</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Guenzi, Eric</au><au>Gasc, Anne‐Marie</au><au>Sicard, Michel A.</au><au>Hakenbeck, Regine</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A two‐component signal‐transducing system is involved in competence and penicillin susceptibility in laboratory mutants of Streptococcus pneumoniae</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>1994-05</date><risdate>1994</risdate><volume>12</volume><issue>3</issue><spage>505</spage><epage>515</epage><pages>505-515</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>Summary Penicillin resistance in Streptococcus pneumoniae has been attributed so far to the production of penicillin‐binding protein (PBP) variants with decreased affinities for β‐lactam antibiotics. Cefotaxime‐resistant laboratory mutants, selected after several steps on increasing concentrations of this β‐lactam, become deficient in transformation as well. A DNA fragment conferring both cefotaxime resistance and transformation deficiency was isolated and cloned from the mutant C306. The cefotaxime resistance associated with this resistance determinant was not accompanied with apparent changes in PBP properties, and it mapped on the chromosome distinct from the known resistance determinants, genes encoding PBP2x, PBP1a or PBP2b. Determination of a 2265 bp DNA sequence of the resistance determinant revealed two open reading frames, claR and claH, whose deduced amino acid sequence identified the corresponding proteins as the response regulator and histidine kinase receptor, respectively (members of the two families of bacterial signal‐transducing proteins). Two hydrophobic peptide regions divided the histidine kinase ClaH into two putative domains: an N‐terminal extracelluiar sensor part, and an intracelluiar C‐terminal domain with the conserved His‐226 residue, the presumed phosphorylation site. The single point mutations responsible for cefotaxime‐resistance and transformation deficiency of C306 and of another two independently isolated cefotaxime‐resistant mutants were each located in the C‐terminal half of ClaH. A small extracellular protein, the competence factor, is required for induction of competence. Neither C306 nor the transformants obtained with the mutated claH gene produced competence factor, and exogenous competence factor could not complement the transformation deficiency, indicating that the signal‐transducing system cia is involved in early steps of competence regulation.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>8065267</pmid><doi>10.1111/j.1365-2958.1994.tb01038.x</doi><tpages>11</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0950-382X
ispartof Molecular microbiology, 1994-05, Vol.12 (3), p.505-515
issn 0950-382X
1365-2958
language eng
recordid cdi_proquest_miscellaneous_16908734
source MEDLINE; Access via Wiley Online Library
subjects Amino Acid Sequence
Antibacterial agents
Antibiotics. Antiinfectious agents. Antiparasitic agents
Bacterial Proteins
Bacteriology
Base Sequence
Biological and medical sciences
Cefotaxime - pharmacology
Chromosome Mapping
DNA Mutational Analysis
Drug Resistance, Microbial - genetics
Fundamental and applied biological sciences. Psychology
Genetics
Histidine Kinase
Medical sciences
Microbiology
Molecular Sequence Data
Mutagenesis, Insertional
Mutation
Penicillin Resistance - genetics
Pharmacology. Drug treatments
Piperacillin - pharmacology
Protein Kinases - genetics
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Signal Transduction - genetics
Streptococcus pneumoniae
Streptococcus pneumoniae - genetics
title A two‐component signal‐transducing system is involved in competence and penicillin susceptibility in laboratory mutants of Streptococcus pneumoniae
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-25T15%3A23%3A19IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=A%20two%E2%80%90component%20signal%E2%80%90transducing%20system%20is%20involved%20in%20competence%20and%20penicillin%20susceptibility%20in%20laboratory%20mutants%20of%20Streptococcus%20pneumoniae&rft.jtitle=Molecular%20microbiology&rft.au=Guenzi,%20Eric&rft.date=1994-05&rft.volume=12&rft.issue=3&rft.spage=505&rft.epage=515&rft.pages=505-515&rft.issn=0950-382X&rft.eissn=1365-2958&rft_id=info:doi/10.1111/j.1365-2958.1994.tb01038.x&rft_dat=%3Cproquest_cross%3E16908734%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=16908734&rft_id=info:pmid/8065267&rfr_iscdi=true