A Proteolytic Transmembrane Signaling Pathway and Resistance to β-Lactams in Staphylococci
β-Lactamase and penicillin-binding protein 2a mediate staphylococcal resistance to β-lactam antibiotics, which are otherwise highly clinically effective. Production of these inducible proteins is regulated by a signal-transducing integral membrane protein and a transcriptional repressor. The signal...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2001-03, Vol.291 (5510), p.1962-1965 |
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| container_end_page | 1965 |
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| container_issue | 5510 |
| container_start_page | 1962 |
| container_title | Science (American Association for the Advancement of Science) |
| container_volume | 291 |
| creator | Zhang, H. Z. Hackbarth, C. J. Chansky, K. M. Chambers, H. F. |
| description | β-Lactamase and penicillin-binding protein 2a mediate staphylococcal resistance to β-lactam antibiotics, which are otherwise highly clinically effective. Production of these inducible proteins is regulated by a signal-transducing integral membrane protein and a transcriptional repressor. The signal transducer is a fusion protein with penicillin-binding and zinc metalloprotease domains. The signal for protein expression is transmitted by site-specific proteolytic cleavage of both the transducer, which autoactivates, and the repressor, which is inactivated, unblocking gene transcription. Compounds that disrupt this regulatory pathway could restore the activity of β-lactam antibiotics against drug-resistant strains of Staphylococci. |
| doi_str_mv | 10.1126/science.1055144 |
| format | Article |
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Z. ; Hackbarth, C. J. ; Chansky, K. M. ; Chambers, H. F.</creator><creatorcontrib>Zhang, H. Z. ; Hackbarth, C. J. ; Chansky, K. M. ; Chambers, H. F.</creatorcontrib><description>β-Lactamase and penicillin-binding protein 2a mediate staphylococcal resistance to β-lactam antibiotics, which are otherwise highly clinically effective. Production of these inducible proteins is regulated by a signal-transducing integral membrane protein and a transcriptional repressor. The signal transducer is a fusion protein with penicillin-binding and zinc metalloprotease domains. The signal for protein expression is transmitted by site-specific proteolytic cleavage of both the transducer, which autoactivates, and the repressor, which is inactivated, unblocking gene transcription. Compounds that disrupt this regulatory pathway could restore the activity of β-lactam antibiotics against drug-resistant strains of Staphylococci.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1055144</identifier><identifier>PMID: 11239156</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>Amino Acid Motifs ; Amino Acid Sequence ; Anti-Bacterial Agents - metabolism ; Anti-Bacterial Agents - pharmacology ; Antibiotics ; Bacterial Proteins - chemistry ; Bacterial Proteins - metabolism ; Bacteriology ; Beta lactam antibiotics ; Beta lactamases ; beta-Lactam Resistance ; beta-Lactamases - biosynthesis ; beta-Lactams ; Biological and medical sciences ; Carrier Proteins - chemistry ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Catalysis ; Cell lines ; Cell Membrane - metabolism ; Cloning, Molecular ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - metabolism ; Fundamental and applied biological sciences. Psychology ; General practice ; Genes ; Genes, Regulator ; Genetic mutation ; Genetics ; Literary Devices ; Logical Thinking ; Membranes ; Metalloendopeptidases - chemistry ; Metalloendopeptidases - metabolism ; Microbiology ; Mutagenesis, Site-Directed ; Penicillin ; Penicillin-Binding Proteins ; Plasmids ; Protein Structure, Tertiary ; Proteins ; Recombinant Fusion Proteins - metabolism ; Repressor Proteins - chemistry ; Repressor Proteins - genetics ; Repressor Proteins - metabolism ; Ribosomes ; RNA ; Signal Transduction ; Staphylococcal infections ; Staphylococcus ; Staphylococcus aureus - drug effects ; Staphylococcus aureus - genetics ; Staphylococcus aureus - metabolism ; Structure-activity relationships ; Transformation, Bacterial ; Zinc</subject><ispartof>Science (American Association for the Advancement of Science), 2001-03, Vol.291 (5510), p.1962-1965</ispartof><rights>Copyright 2001 American Association for the Advancement of Science</rights><rights>2001 INIST-CNRS</rights><rights>COPYRIGHT 2001 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science Mar 9, 2001</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c670t-b854b5d191bb435443ec8ca697da3e1af17855924395c738ff99b1b48240ec113</citedby><cites>FETCH-LOGICAL-c670t-b854b5d191bb435443ec8ca697da3e1af17855924395c738ff99b1b48240ec113</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3082453$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3082453$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,803,2884,2885,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=917098$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11239156$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, H. Z.</creatorcontrib><creatorcontrib>Hackbarth, C. J.</creatorcontrib><creatorcontrib>Chansky, K. M.</creatorcontrib><creatorcontrib>Chambers, H. F.</creatorcontrib><title>A Proteolytic Transmembrane Signaling Pathway and Resistance to β-Lactams in Staphylococci</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>β-Lactamase and penicillin-binding protein 2a mediate staphylococcal resistance to β-lactam antibiotics, which are otherwise highly clinically effective. Production of these inducible proteins is regulated by a signal-transducing integral membrane protein and a transcriptional repressor. The signal transducer is a fusion protein with penicillin-binding and zinc metalloprotease domains. The signal for protein expression is transmitted by site-specific proteolytic cleavage of both the transducer, which autoactivates, and the repressor, which is inactivated, unblocking gene transcription. Compounds that disrupt this regulatory pathway could restore the activity of β-lactam antibiotics against drug-resistant strains of Staphylococci.</description><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>Anti-Bacterial Agents - metabolism</subject><subject>Anti-Bacterial Agents - pharmacology</subject><subject>Antibiotics</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>Beta lactam antibiotics</subject><subject>Beta lactamases</subject><subject>beta-Lactam Resistance</subject><subject>beta-Lactamases - biosynthesis</subject><subject>beta-Lactams</subject><subject>Biological and medical sciences</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Catalysis</subject><subject>Cell lines</subject><subject>Cell Membrane - metabolism</subject><subject>Cloning, Molecular</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Fundamental and applied biological sciences. 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The signal for protein expression is transmitted by site-specific proteolytic cleavage of both the transducer, which autoactivates, and the repressor, which is inactivated, unblocking gene transcription. Compounds that disrupt this regulatory pathway could restore the activity of β-lactam antibiotics against drug-resistant strains of Staphylococci.</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>11239156</pmid><doi>10.1126/science.1055144</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 2001-03, Vol.291 (5510), p.1962-1965 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_743074138 |
| source | MEDLINE; JSTOR Archive Collection A-Z Listing; American Association for the Advancement of Science |
| subjects | Amino Acid Motifs Amino Acid Sequence Anti-Bacterial Agents - metabolism Anti-Bacterial Agents - pharmacology Antibiotics Bacterial Proteins - chemistry Bacterial Proteins - metabolism Bacteriology Beta lactam antibiotics Beta lactamases beta-Lactam Resistance beta-Lactamases - biosynthesis beta-Lactams Biological and medical sciences Carrier Proteins - chemistry Carrier Proteins - genetics Carrier Proteins - metabolism Catalysis Cell lines Cell Membrane - metabolism Cloning, Molecular DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism Fundamental and applied biological sciences. Psychology General practice Genes Genes, Regulator Genetic mutation Genetics Literary Devices Logical Thinking Membranes Metalloendopeptidases - chemistry Metalloendopeptidases - metabolism Microbiology Mutagenesis, Site-Directed Penicillin Penicillin-Binding Proteins Plasmids Protein Structure, Tertiary Proteins Recombinant Fusion Proteins - metabolism Repressor Proteins - chemistry Repressor Proteins - genetics Repressor Proteins - metabolism Ribosomes RNA Signal Transduction Staphylococcal infections Staphylococcus Staphylococcus aureus - drug effects Staphylococcus aureus - genetics Staphylococcus aureus - metabolism Structure-activity relationships Transformation, Bacterial Zinc |
| title | A Proteolytic Transmembrane Signaling Pathway and Resistance to β-Lactams in Staphylococci |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-22T03%3A17%3A46IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=A%20Proteolytic%20Transmembrane%20Signaling%20Pathway%20and%20Resistance%20to%20%CE%B2-Lactams%20in%20Staphylococci&rft.jtitle=Science%20(American%20Association%20for%20the%20Advancement%20of%20Science)&rft.au=Zhang,%20H.%20Z.&rft.date=2001-03-09&rft.volume=291&rft.issue=5510&rft.spage=1962&rft.epage=1965&rft.pages=1962-1965&rft.issn=0036-8075&rft.eissn=1095-9203&rft.coden=SCIEAS&rft_id=info:doi/10.1126/science.1055144&rft_dat=%3Cgale_proqu%3EA72275614%3C/gale_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=213581607&rft_id=info:pmid/11239156&rft_galeid=A72275614&rft_jstor_id=3082453&rfr_iscdi=true |