A gene (prsA) of Bacillus subtilis involved in a novel, late stage of protein export
Summary A gene locus of Bacillus subtilis identified by mutations (prs) conferring a defect in protein secretion was cloned from a lambdaGEM‐11 expression library. The sites of three closely linked prs mutations (prs‐3, prs‐29 and prs‐40) were found to reside in a 5.3kb DNA fragment, which also comp...
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| Veröffentlicht in: | Molecular microbiology 1991-05, Vol.5 (5), p.1273-1283 |
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| container_title | Molecular microbiology |
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| creator | Kontinen, V. P. Saris, P. Sarvas, M. |
| description | Summary
A gene locus of Bacillus subtilis identified by mutations (prs) conferring a defect in protein secretion was cloned from a lambdaGEM‐11 expression library. The sites of three closely linked prs mutations (prs‐3, prs‐29 and prs‐40) were found to reside in a 5.3kb DNA fragment, which also complemented the secretion defect in prs‐3 and prs‐29 mutants. Partial sequencing of the fragment showed that these three mutations affect one distinct gene (prs A) encoding a putative protein of 292 amino acids (33 kDa). Sequence analysis Indicated the PrsA protein to be a lipoprotein located outside the cytoplasmic membrane. Thirty percent identity was shown to the PrtM protein of Lactococcus lactis, which is involved in the maturation of an exported proteinase. The phenotypes of prsA mutants and the structural similarity of PrsA with PrtM suggest that PrsA may have a novel function at a late phase in protein export. |
| doi_str_mv | 10.1111/j.1365-2958.1991.tb01901.x |
| format | Article |
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A gene locus of Bacillus subtilis identified by mutations (prs) conferring a defect in protein secretion was cloned from a lambdaGEM‐11 expression library. The sites of three closely linked prs mutations (prs‐3, prs‐29 and prs‐40) were found to reside in a 5.3kb DNA fragment, which also complemented the secretion defect in prs‐3 and prs‐29 mutants. Partial sequencing of the fragment showed that these three mutations affect one distinct gene (prs A) encoding a putative protein of 292 amino acids (33 kDa). Sequence analysis Indicated the PrsA protein to be a lipoprotein located outside the cytoplasmic membrane. Thirty percent identity was shown to the PrtM protein of Lactococcus lactis, which is involved in the maturation of an exported proteinase. The phenotypes of prsA mutants and the structural similarity of PrsA with PrtM suggest that PrsA may have a novel function at a late phase in protein export.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1111/j.1365-2958.1991.tb01901.x</identifier><identifier>PMID: 1956302</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>alpha-Amylases - genetics ; alpha-Amylases - metabolism ; Amino Acid Sequence ; Bacillus subtilis - genetics ; Bacillus subtilis - physiology ; Bacterial Proteins - metabolism ; Bacteriology ; Base Sequence ; Biological and medical sciences ; Biological Transport ; Fundamental and applied biological sciences. Psychology ; Genes, Bacterial ; Genetic Complementation Test ; Lipoproteins - genetics ; Lipoproteins - metabolism ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Microbiology ; Molecular Sequence Data ; Open Reading Frames ; Permeability, membrane transport, intracellular transport ; Phosphoenolpyruvate Sugar Phosphotransferase System - genetics ; Phosphoenolpyruvate Sugar Phosphotransferase System - metabolism ; Protein Processing, Post-Translational ; Protein Sorting Signals - genetics ; Recombinant Fusion Proteins - metabolism ; Sequence Homology, Nucleic Acid</subject><ispartof>Molecular microbiology, 1991-05, Vol.5 (5), p.1273-1283</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4313-a935d2f979e112910964312e34b60cae3ce6f8b22b189a56091c1e4eb8036f513</citedby><cites>FETCH-LOGICAL-c4313-a935d2f979e112910964312e34b60cae3ce6f8b22b189a56091c1e4eb8036f513</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.1365-2958.1991.tb01901.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1365-2958.1991.tb01901.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27923,27924,45573,45574</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19758105$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1956302$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kontinen, V. P.</creatorcontrib><creatorcontrib>Saris, P.</creatorcontrib><creatorcontrib>Sarvas, M.</creatorcontrib><title>A gene (prsA) of Bacillus subtilis involved in a novel, late stage of protein export</title><title>Molecular microbiology</title><addtitle>Mol Microbiol</addtitle><description>Summary
A gene locus of Bacillus subtilis identified by mutations (prs) conferring a defect in protein secretion was cloned from a lambdaGEM‐11 expression library. The sites of three closely linked prs mutations (prs‐3, prs‐29 and prs‐40) were found to reside in a 5.3kb DNA fragment, which also complemented the secretion defect in prs‐3 and prs‐29 mutants. Partial sequencing of the fragment showed that these three mutations affect one distinct gene (prs A) encoding a putative protein of 292 amino acids (33 kDa). Sequence analysis Indicated the PrsA protein to be a lipoprotein located outside the cytoplasmic membrane. Thirty percent identity was shown to the PrtM protein of Lactococcus lactis, which is involved in the maturation of an exported proteinase. The phenotypes of prsA mutants and the structural similarity of PrsA with PrtM suggest that PrsA may have a novel function at a late phase in protein export.</description><subject>alpha-Amylases - genetics</subject><subject>alpha-Amylases - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Bacillus subtilis - genetics</subject><subject>Bacillus subtilis - physiology</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Biological Transport</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes, Bacterial</subject><subject>Genetic Complementation Test</subject><subject>Lipoproteins - genetics</subject><subject>Lipoproteins - metabolism</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Open Reading Frames</subject><subject>Permeability, membrane transport, intracellular transport</subject><subject>Phosphoenolpyruvate Sugar Phosphotransferase System - genetics</subject><subject>Phosphoenolpyruvate Sugar Phosphotransferase System - metabolism</subject><subject>Protein Processing, Post-Translational</subject><subject>Protein Sorting Signals - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Sequence Homology, Nucleic Acid</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkF1r2zAUhsXYSLNuP6EgCisr1N45UuRYvSlpWbtAwm4y6J2QlePgoNipZafpv59Nwta7Ut1I6H3OBw9j5wgxdufHOkaZqEholcaoNcZNBqgB4_0HNvwXfWRD0AoimYrHE_Y5hDUASkjkgA1Qq0SCGLLFhK-oJP59W4fJJa9yfmtd4X0beGizpvBF4EW5q_yOlt2DW15WO_JX3NuGeGjsivqibV011MW031Z184V9yq0P9PV4n7I_9z8Xd7-i2e-H6d1kFrmRRBlZLdVS5HqsCVFoBJ10_4LkKEvAWZKOkjzNhMgw1VYloNEhjShLQSa5QnnKLg59u_FPLYXGbIrgyHtbUtUGMxYKUGn1JthDKCV04PUBdHUVQk252dbFxtYvBsH07s3a9IJNL9j07s3Rvdl3xWfHKW22oeX_0oPsLv92zG1w1ue1LV0RXmFjlSL0294cuOfC08s7NjDz-RTFWMq_r3ae-g</recordid><startdate>199105</startdate><enddate>199105</enddate><creator>Kontinen, V. P.</creator><creator>Saris, P.</creator><creator>Sarvas, M.</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>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>199105</creationdate><title>A gene (prsA) of Bacillus subtilis involved in a novel, late stage of protein export</title><author>Kontinen, V. P. ; Saris, P. ; Sarvas, M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4313-a935d2f979e112910964312e34b60cae3ce6f8b22b189a56091c1e4eb8036f513</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>alpha-Amylases - genetics</topic><topic>alpha-Amylases - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Bacillus subtilis - genetics</topic><topic>Bacillus subtilis - physiology</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacteriology</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Biological Transport</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes, Bacterial</topic><topic>Genetic Complementation Test</topic><topic>Lipoproteins - genetics</topic><topic>Lipoproteins - metabolism</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Open Reading Frames</topic><topic>Permeability, membrane transport, intracellular transport</topic><topic>Phosphoenolpyruvate Sugar Phosphotransferase System - genetics</topic><topic>Phosphoenolpyruvate Sugar Phosphotransferase System - metabolism</topic><topic>Protein Processing, Post-Translational</topic><topic>Protein Sorting Signals - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Sequence Homology, Nucleic Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kontinen, V. P.</creatorcontrib><creatorcontrib>Saris, P.</creatorcontrib><creatorcontrib>Sarvas, M.</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>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kontinen, V. P.</au><au>Saris, P.</au><au>Sarvas, M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A gene (prsA) of Bacillus subtilis involved in a novel, late stage of protein export</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>1991-05</date><risdate>1991</risdate><volume>5</volume><issue>5</issue><spage>1273</spage><epage>1283</epage><pages>1273-1283</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>Summary
A gene locus of Bacillus subtilis identified by mutations (prs) conferring a defect in protein secretion was cloned from a lambdaGEM‐11 expression library. The sites of three closely linked prs mutations (prs‐3, prs‐29 and prs‐40) were found to reside in a 5.3kb DNA fragment, which also complemented the secretion defect in prs‐3 and prs‐29 mutants. Partial sequencing of the fragment showed that these three mutations affect one distinct gene (prs A) encoding a putative protein of 292 amino acids (33 kDa). Sequence analysis Indicated the PrsA protein to be a lipoprotein located outside the cytoplasmic membrane. Thirty percent identity was shown to the PrtM protein of Lactococcus lactis, which is involved in the maturation of an exported proteinase. The phenotypes of prsA mutants and the structural similarity of PrsA with PrtM suggest that PrsA may have a novel function at a late phase in protein export.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>1956302</pmid><doi>10.1111/j.1365-2958.1991.tb01901.x</doi><tpages>11</tpages></addata></record> |
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| ispartof | Molecular microbiology, 1991-05, Vol.5 (5), p.1273-1283 |
| issn | 0950-382X 1365-2958 |
| language | eng |
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| source | MEDLINE; Wiley Online Library All Journals |
| subjects | alpha-Amylases - genetics alpha-Amylases - metabolism Amino Acid Sequence Bacillus subtilis - genetics Bacillus subtilis - physiology Bacterial Proteins - metabolism Bacteriology Base Sequence Biological and medical sciences Biological Transport Fundamental and applied biological sciences. Psychology Genes, Bacterial Genetic Complementation Test Lipoproteins - genetics Lipoproteins - metabolism Membrane Proteins - genetics Membrane Proteins - metabolism Microbiology Molecular Sequence Data Open Reading Frames Permeability, membrane transport, intracellular transport Phosphoenolpyruvate Sugar Phosphotransferase System - genetics Phosphoenolpyruvate Sugar Phosphotransferase System - metabolism Protein Processing, Post-Translational Protein Sorting Signals - genetics Recombinant Fusion Proteins - metabolism Sequence Homology, Nucleic Acid |
| title | A gene (prsA) of Bacillus subtilis involved in a novel, late stage of protein export |
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