The Bacillus subtilis spore coat protein interaction network
Summary Bacterial spores are surrounded by a morphologically complex, mechanically flexible protein coat, which protects the spore from toxic molecules. The interactions among the over 50 proteins that make up the coat remain poorly understood. We have used cell biological and protein biochemical ap...
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| Veröffentlicht in: | Molecular microbiology 2006-01, Vol.59 (2), p.487-502 |
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| container_title | Molecular microbiology |
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| creator | Kim, Hosan Hahn, Marlene Grabowski, Paul McPherson, Derrell C. Otte, Michele M. Wang, Rong Ferguson, Caitlin C. Eichenberger, Patrick Driks, Adam |
| description | Summary
Bacterial spores are surrounded by a morphologically complex, mechanically flexible protein coat, which protects the spore from toxic molecules. The interactions among the over 50 proteins that make up the coat remain poorly understood. We have used cell biological and protein biochemical approaches to identify novel coat proteins in Bacillus subtilis and describe the network of their interactions, in order to understand coat assembly and the molecular basis of its protective functions and mechanical properties. Our analysis characterizes the interactions between 32 coat proteins. This detailed view reveals a complex interaction network. A key feature of the network is the importance of a small subset of proteins that direct the assembly of most of the coat. From an analysis of the network topology, we propose a model in which low‐affinity interactions are abundant in the coat and account, to a significant degree, for the coat's mechanical properties as well as structural variation between spores. |
| doi_str_mv | 10.1111/j.1365-2958.2005.04968.x |
| format | Article |
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Bacterial spores are surrounded by a morphologically complex, mechanically flexible protein coat, which protects the spore from toxic molecules. The interactions among the over 50 proteins that make up the coat remain poorly understood. We have used cell biological and protein biochemical approaches to identify novel coat proteins in Bacillus subtilis and describe the network of their interactions, in order to understand coat assembly and the molecular basis of its protective functions and mechanical properties. Our analysis characterizes the interactions between 32 coat proteins. This detailed view reveals a complex interaction network. A key feature of the network is the importance of a small subset of proteins that direct the assembly of most of the coat. From an analysis of the network topology, we propose a model in which low‐affinity interactions are abundant in the coat and account, to a significant degree, for the coat's mechanical properties as well as structural variation between spores.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1111/j.1365-2958.2005.04968.x</identifier><identifier>PMID: 16390444</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science Ltd</publisher><subject>Antibiotics ; Bacillus subtilis ; Bacillus subtilis - genetics ; Bacillus subtilis - metabolism ; Bacillus subtilis - physiology ; Bacterial proteins ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Bacterial Proteins - physiology ; Biological and medical sciences ; Cells ; Electrophoresis, Polyacrylamide Gel ; Fundamental and applied biological sciences. Psychology ; Gene Deletion ; Microbiology ; Protein Binding ; Spores, Bacterial</subject><ispartof>Molecular microbiology, 2006-01, Vol.59 (2), p.487-502</ispartof><rights>2006 INIST-CNRS</rights><rights>Copyright Blackwell Publishing Jan 2006</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5718-64d945d2b02f99e14eb4a665c9119303eadbc15605f4f0fa2997e59607d0c3523</citedby><cites>FETCH-LOGICAL-c5718-64d945d2b02f99e14eb4a665c9119303eadbc15605f4f0fa2997e59607d0c3523</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.1365-2958.2005.04968.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1365-2958.2005.04968.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,1427,27903,27904,45553,45554,46388,46812</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17478229$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16390444$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kim, Hosan</creatorcontrib><creatorcontrib>Hahn, Marlene</creatorcontrib><creatorcontrib>Grabowski, Paul</creatorcontrib><creatorcontrib>McPherson, Derrell C.</creatorcontrib><creatorcontrib>Otte, Michele M.</creatorcontrib><creatorcontrib>Wang, Rong</creatorcontrib><creatorcontrib>Ferguson, Caitlin C.</creatorcontrib><creatorcontrib>Eichenberger, Patrick</creatorcontrib><creatorcontrib>Driks, Adam</creatorcontrib><title>The Bacillus subtilis spore coat protein interaction network</title><title>Molecular microbiology</title><addtitle>Mol Microbiol</addtitle><description>Summary
Bacterial spores are surrounded by a morphologically complex, mechanically flexible protein coat, which protects the spore from toxic molecules. The interactions among the over 50 proteins that make up the coat remain poorly understood. We have used cell biological and protein biochemical approaches to identify novel coat proteins in Bacillus subtilis and describe the network of their interactions, in order to understand coat assembly and the molecular basis of its protective functions and mechanical properties. Our analysis characterizes the interactions between 32 coat proteins. This detailed view reveals a complex interaction network. A key feature of the network is the importance of a small subset of proteins that direct the assembly of most of the coat. From an analysis of the network topology, we propose a model in which low‐affinity interactions are abundant in the coat and account, to a significant degree, for the coat's mechanical properties as well as structural variation between spores.</description><subject>Antibiotics</subject><subject>Bacillus subtilis</subject><subject>Bacillus subtilis - genetics</subject><subject>Bacillus subtilis - metabolism</subject><subject>Bacillus subtilis - physiology</subject><subject>Bacterial proteins</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacterial Proteins - physiology</subject><subject>Biological and medical sciences</subject><subject>Cells</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Deletion</subject><subject>Microbiology</subject><subject>Protein Binding</subject><subject>Spores, Bacterial</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkF1LwzAUhoMoOqd_QYqgd60nn21AL3T4MdjwRsG7kKYpZnbtTFqm_97WDQWvzE0OnOe8vDwIRRgS3L-LRYKp4DGRPEsIAE-ASZElHzto9LPYRSOQHGKakZcDdBjCAgBTEHQfHWBBJTDGRujy6dVGN9q4qupCFLq8dZXrh1XjbWQa3UYr37TW1ZGrW-u1aV1TR7Vt141_O0J7pa6CPd7-Y_R8d_s0eYhnj_fTyfUsNjzFWSxYIRkvSA6klNJiZnOmheBGYiwpUKuL3GAugJeshFITKVPLpYC0AEM5oWN0vsntu7x3NrRq6YKxVaVr23RB4ZQxmmHag6d_wEXT-brvprAUnDFMh7RsAxnfhOBtqVbeLbX_VBjUoFct1GBRDRbVoFd961Uf_enJNr_Ll7b4Pdz67IGzLaCD0VXpdW1c-OVSlmaEyJ672nBrV9nPfxdQ8_l0mOgXmZOUTg</recordid><startdate>200601</startdate><enddate>200601</enddate><creator>Kim, Hosan</creator><creator>Hahn, Marlene</creator><creator>Grabowski, Paul</creator><creator>McPherson, Derrell C.</creator><creator>Otte, Michele M.</creator><creator>Wang, Rong</creator><creator>Ferguson, Caitlin C.</creator><creator>Eichenberger, Patrick</creator><creator>Driks, Adam</creator><general>Blackwell Science Ltd</general><general>Blackwell Science</general><general>Blackwell Publishing Ltd</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>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>200601</creationdate><title>The Bacillus subtilis spore coat protein interaction network</title><author>Kim, Hosan ; Hahn, Marlene ; Grabowski, Paul ; McPherson, Derrell C. ; Otte, Michele M. ; Wang, Rong ; Ferguson, Caitlin C. ; Eichenberger, Patrick ; Driks, Adam</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5718-64d945d2b02f99e14eb4a665c9119303eadbc15605f4f0fa2997e59607d0c3523</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Antibiotics</topic><topic>Bacillus subtilis</topic><topic>Bacillus subtilis - genetics</topic><topic>Bacillus subtilis - metabolism</topic><topic>Bacillus subtilis - physiology</topic><topic>Bacterial proteins</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacterial Proteins - physiology</topic><topic>Biological and medical sciences</topic><topic>Cells</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Deletion</topic><topic>Microbiology</topic><topic>Protein Binding</topic><topic>Spores, Bacterial</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kim, Hosan</creatorcontrib><creatorcontrib>Hahn, Marlene</creatorcontrib><creatorcontrib>Grabowski, Paul</creatorcontrib><creatorcontrib>McPherson, Derrell C.</creatorcontrib><creatorcontrib>Otte, Michele M.</creatorcontrib><creatorcontrib>Wang, Rong</creatorcontrib><creatorcontrib>Ferguson, Caitlin C.</creatorcontrib><creatorcontrib>Eichenberger, Patrick</creatorcontrib><creatorcontrib>Driks, Adam</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>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kim, Hosan</au><au>Hahn, Marlene</au><au>Grabowski, Paul</au><au>McPherson, Derrell C.</au><au>Otte, Michele M.</au><au>Wang, Rong</au><au>Ferguson, Caitlin C.</au><au>Eichenberger, Patrick</au><au>Driks, Adam</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Bacillus subtilis spore coat protein interaction network</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>2006-01</date><risdate>2006</risdate><volume>59</volume><issue>2</issue><spage>487</spage><epage>502</epage><pages>487-502</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>Summary
Bacterial spores are surrounded by a morphologically complex, mechanically flexible protein coat, which protects the spore from toxic molecules. The interactions among the over 50 proteins that make up the coat remain poorly understood. We have used cell biological and protein biochemical approaches to identify novel coat proteins in Bacillus subtilis and describe the network of their interactions, in order to understand coat assembly and the molecular basis of its protective functions and mechanical properties. Our analysis characterizes the interactions between 32 coat proteins. This detailed view reveals a complex interaction network. A key feature of the network is the importance of a small subset of proteins that direct the assembly of most of the coat. From an analysis of the network topology, we propose a model in which low‐affinity interactions are abundant in the coat and account, to a significant degree, for the coat's mechanical properties as well as structural variation between spores.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>16390444</pmid><doi>10.1111/j.1365-2958.2005.04968.x</doi><tpages>16</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Molecular microbiology, 2006-01, Vol.59 (2), p.487-502 |
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| subjects | Antibiotics Bacillus subtilis Bacillus subtilis - genetics Bacillus subtilis - metabolism Bacillus subtilis - physiology Bacterial proteins Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacterial Proteins - physiology Biological and medical sciences Cells Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology Gene Deletion Microbiology Protein Binding Spores, Bacterial |
| title | The Bacillus subtilis spore coat protein interaction network |
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