Proteolytic processing of Escherichia coli twin-arginine signal peptides by LepB
The twin-arginine translocation (Tat) apparatus is a protein targeting system found in the cytoplasmic membranes of many prokaryotes. Substrate proteins of the Tat pathway are synthesised with signal peptides bearing SRRxFLK ‘twin-arginine' amino acid motifs. All Tat signal peptides have a comm...
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| Veröffentlicht in: | Archives of microbiology 2009-12, Vol.191 (12), p.919-925 |
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| creator | Lüke, Iris Handford, Jennifer I Palmer, Tracy Sargent, Frank |
| description | The twin-arginine translocation (Tat) apparatus is a protein targeting system found in the cytoplasmic membranes of many prokaryotes. Substrate proteins of the Tat pathway are synthesised with signal peptides bearing SRRxFLK ‘twin-arginine' amino acid motifs. All Tat signal peptides have a common tripartite structure comprising a polar N-terminal region, followed by a hydrophobic region of variable length and a polar C-terminal region. In Escherichia coli, Tat signal peptides are proteolytically cleaved after translocation. The signal peptide C-terminal regions contain conserved AxA motifs, which are possible recognition sequences for leader peptidase I (LepB). In this work, the role of LepB in Tat signal peptide processing was addressed directly. Deliberate repression of lepB expression prevented processing of all Tat substrates tested, including SufI, AmiC, and a TorA-23K reporter protein. In addition, electron microscopy revealed gross defects in cell architecture and membrane integrity following depletion of cellular LepB protein levels. |
| doi_str_mv | 10.1007/s00203-009-0516-5 |
| format | Article |
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Substrate proteins of the Tat pathway are synthesised with signal peptides bearing SRRxFLK ‘twin-arginine' amino acid motifs. All Tat signal peptides have a common tripartite structure comprising a polar N-terminal region, followed by a hydrophobic region of variable length and a polar C-terminal region. In Escherichia coli, Tat signal peptides are proteolytically cleaved after translocation. The signal peptide C-terminal regions contain conserved AxA motifs, which are possible recognition sequences for leader peptidase I (LepB). In this work, the role of LepB in Tat signal peptide processing was addressed directly. Deliberate repression of lepB expression prevented processing of all Tat substrates tested, including SufI, AmiC, and a TorA-23K reporter protein. In addition, electron microscopy revealed gross defects in cell architecture and membrane integrity following depletion of cellular LepB protein levels.</description><identifier>ISSN: 0302-8933</identifier><identifier>EISSN: 1432-072X</identifier><identifier>DOI: 10.1007/s00203-009-0516-5</identifier><identifier>PMID: 19809807</identifier><identifier>CODEN: AMICCW</identifier><language>eng</language><publisher>Berlin/Heidelberg: Berlin/Heidelberg : Springer-Verlag</publisher><subject>Amino acids ; Antibiotics ; Bacteriology ; Biochemistry ; Biological and medical sciences ; Biomedical and Life Sciences ; Biotechnology ; Cell Biology ; Cloning ; E coli ; Ecology ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Escherichia coli Proteins - genetics ; Escherichia coli Proteins - metabolism ; Fundamental and applied biological sciences. Psychology ; Gene Deletion ; Gene Expression Regulation, Bacterial - physiology ; Glucose ; Life Sciences ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Membranes ; Microbial Ecology ; Microbiology ; Microscopy ; Miscellaneous ; Peptides ; Plasmids ; Proteins ; Serine Endopeptidases - genetics ; Serine Endopeptidases - metabolism ; Short Communication ; Translocation</subject><ispartof>Archives of microbiology, 2009-12, Vol.191 (12), p.919-925</ispartof><rights>Springer-Verlag 2009</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c490t-1ad451c60b72ae50e305471a18971d96b8714c7fd316bd9d1ee5e6f49d75c3fd3</citedby><cites>FETCH-LOGICAL-c490t-1ad451c60b72ae50e305471a18971d96b8714c7fd316bd9d1ee5e6f49d75c3fd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00203-009-0516-5$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00203-009-0516-5$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=22167439$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19809807$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lüke, Iris</creatorcontrib><creatorcontrib>Handford, Jennifer I</creatorcontrib><creatorcontrib>Palmer, Tracy</creatorcontrib><creatorcontrib>Sargent, Frank</creatorcontrib><title>Proteolytic processing of Escherichia coli twin-arginine signal peptides by LepB</title><title>Archives of microbiology</title><addtitle>Arch Microbiol</addtitle><addtitle>Arch Microbiol</addtitle><description>The twin-arginine translocation (Tat) apparatus is a protein targeting system found in the cytoplasmic membranes of many prokaryotes. Substrate proteins of the Tat pathway are synthesised with signal peptides bearing SRRxFLK ‘twin-arginine' amino acid motifs. All Tat signal peptides have a common tripartite structure comprising a polar N-terminal region, followed by a hydrophobic region of variable length and a polar C-terminal region. In Escherichia coli, Tat signal peptides are proteolytically cleaved after translocation. The signal peptide C-terminal regions contain conserved AxA motifs, which are possible recognition sequences for leader peptidase I (LepB). In this work, the role of LepB in Tat signal peptide processing was addressed directly. Deliberate repression of lepB expression prevented processing of all Tat substrates tested, including SufI, AmiC, and a TorA-23K reporter protein. In addition, electron microscopy revealed gross defects in cell architecture and membrane integrity following depletion of cellular LepB protein levels.</description><subject>Amino acids</subject><subject>Antibiotics</subject><subject>Bacteriology</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Cell Biology</subject><subject>Cloning</subject><subject>E coli</subject><subject>Ecology</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins - genetics</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Deletion</subject><subject>Gene Expression Regulation, Bacterial - physiology</subject><subject>Glucose</subject><subject>Life Sciences</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Membranes</subject><subject>Microbial Ecology</subject><subject>Microbiology</subject><subject>Microscopy</subject><subject>Miscellaneous</subject><subject>Peptides</subject><subject>Plasmids</subject><subject>Proteins</subject><subject>Serine Endopeptidases - genetics</subject><subject>Serine Endopeptidases - metabolism</subject><subject>Short Communication</subject><subject>Translocation</subject><issn>0302-8933</issn><issn>1432-072X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNp9kE9r3DAQxUVoSbZpP0AuiSj0qHZGkiXr2IT0Dyw00AZ6E7IsOwqO7Uheyn77KnhJcyoMCEa_9-bxCDlD-IgA-lMG4CAYgGFQoWLVEdmgFJyB5r9fkQ0I4Kw2QpyQNznfAyCv6_qYnKCpoYzekJubNC1hGvZL9HROkw85x7GnU0evs78LKfq76KifhkiXP3FkLvVxjGOgOfajG-gc5iW2IdNmT7dhvnxLXnduyOHd4T0lt1-uf119Y9sfX79ffd4yLw0sDF0rK_QKGs1dqCAIqKRGh7XR2BrV1Bql110rUDWtaTGEKqhOmlZXXpT1KXm_-pbQj7uQF3s_7VJJlC0aI0BqrgqEK-TTlHMKnZ1TfHBpbxHsU4V2rdCWCu1ThbYqmvOD8a55CO0_xaGzAnw4AC57N3TJjT7mZ45zVFoKUzi-crl8jX1ILxL-5_rFKurcZF2fivHtTw4oADUokEr8BUBpkZw</recordid><startdate>20091201</startdate><enddate>20091201</enddate><creator>Lüke, Iris</creator><creator>Handford, Jennifer I</creator><creator>Palmer, Tracy</creator><creator>Sargent, Frank</creator><general>Berlin/Heidelberg : Springer-Verlag</general><general>Springer-Verlag</general><general>Springer</general><general>Springer Nature B.V</general><scope>FBQ</scope><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>3V.</scope><scope>7QL</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope></search><sort><creationdate>20091201</creationdate><title>Proteolytic processing of Escherichia coli twin-arginine signal peptides by LepB</title><author>Lüke, Iris ; Handford, Jennifer I ; Palmer, Tracy ; Sargent, Frank</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c490t-1ad451c60b72ae50e305471a18971d96b8714c7fd316bd9d1ee5e6f49d75c3fd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Amino acids</topic><topic>Antibiotics</topic><topic>Bacteriology</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnology</topic><topic>Cell Biology</topic><topic>Cloning</topic><topic>E coli</topic><topic>Ecology</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli Proteins - genetics</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Deletion</topic><topic>Gene Expression Regulation, Bacterial - physiology</topic><topic>Glucose</topic><topic>Life Sciences</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Membranes</topic><topic>Microbial Ecology</topic><topic>Microbiology</topic><topic>Microscopy</topic><topic>Miscellaneous</topic><topic>Peptides</topic><topic>Plasmids</topic><topic>Proteins</topic><topic>Serine Endopeptidases - genetics</topic><topic>Serine Endopeptidases - metabolism</topic><topic>Short Communication</topic><topic>Translocation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lüke, Iris</creatorcontrib><creatorcontrib>Handford, Jennifer I</creatorcontrib><creatorcontrib>Palmer, Tracy</creatorcontrib><creatorcontrib>Sargent, Frank</creatorcontrib><collection>AGRIS</collection><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>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><jtitle>Archives of microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lüke, Iris</au><au>Handford, Jennifer I</au><au>Palmer, Tracy</au><au>Sargent, Frank</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proteolytic processing of Escherichia coli twin-arginine signal peptides by LepB</atitle><jtitle>Archives of microbiology</jtitle><stitle>Arch Microbiol</stitle><addtitle>Arch Microbiol</addtitle><date>2009-12-01</date><risdate>2009</risdate><volume>191</volume><issue>12</issue><spage>919</spage><epage>925</epage><pages>919-925</pages><issn>0302-8933</issn><eissn>1432-072X</eissn><coden>AMICCW</coden><abstract>The twin-arginine translocation (Tat) apparatus is a protein targeting system found in the cytoplasmic membranes of many prokaryotes. 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| ispartof | Archives of microbiology, 2009-12, Vol.191 (12), p.919-925 |
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| subjects | Amino acids Antibiotics Bacteriology Biochemistry Biological and medical sciences Biomedical and Life Sciences Biotechnology Cell Biology Cloning E coli Ecology Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Fundamental and applied biological sciences. Psychology Gene Deletion Gene Expression Regulation, Bacterial - physiology Glucose Life Sciences Membrane Proteins - genetics Membrane Proteins - metabolism Membranes Microbial Ecology Microbiology Microscopy Miscellaneous Peptides Plasmids Proteins Serine Endopeptidases - genetics Serine Endopeptidases - metabolism Short Communication Translocation |
| title | Proteolytic processing of Escherichia coli twin-arginine signal peptides by LepB |
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