Lactococcus lactis YfiA is necessary and sufficient for ribosome dimerization
Summary Dimerization and inactivation of ribosomes in Escherichia coli is a two‐step process that involves the binding of ribosome modulation factor (RMF) and hibernation promotion factor (HPF). Lactococcus lactis MG1363 expresses a protein, YfiALl, which associates with ribosomes in the stationary...
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| Veröffentlicht in: | Molecular microbiology 2014-01, Vol.91 (2), p.394-407 |
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| creator | Puri, Pranav Eckhardt, Thomas H. Franken, Linda E. Fusetti, Fabrizia Stuart, Marc C. A. Boekema, Egbert J. Kuipers, Oscar P. Kok, Jan Poolman, Bert |
| description | Summary
Dimerization and inactivation of ribosomes in Escherichia coli is a two‐step process that involves the binding of ribosome modulation factor (RMF) and hibernation promotion factor (HPF). Lactococcus lactis MG1363 expresses a protein, YfiALl, which associates with ribosomes in the stationary phase of growth and is responsible for dimerization of ribosomes. We show that full‐length YfiALl is necessary and sufficient for ribosome dimerization in L. lactis but also functions heterologously in vitro with E. coli ribosomes. Deletion of the yfiA gene has no effect on the growth rate but diminishes the survival of L. lactis under energy‐starving conditions. The N‐terminal domain of YfiALl is homologous to HPF from E. coli, whereas the C‐terminal domain has no counterpart in E. coli. By assembling ribosome dimers in vitro, we could dissect the roles of the N‐ and C‐terminal domains of YfiALl. It is concluded that the dimerization and inactivation of ribosomes in L. lactis and E. coli differ in several cellular and molecular aspects. In addition, two‐dimensional maps of dimeric ribosomes from L. lactis obtained by single particle electron microscopy show a marked structural difference in monomer association in comparison to the ribosome dimers in E. coli. |
| doi_str_mv | 10.1111/mmi.12468 |
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Dimerization and inactivation of ribosomes in Escherichia coli is a two‐step process that involves the binding of ribosome modulation factor (RMF) and hibernation promotion factor (HPF). Lactococcus lactis MG1363 expresses a protein, YfiALl, which associates with ribosomes in the stationary phase of growth and is responsible for dimerization of ribosomes. We show that full‐length YfiALl is necessary and sufficient for ribosome dimerization in L. lactis but also functions heterologously in vitro with E. coli ribosomes. Deletion of the yfiA gene has no effect on the growth rate but diminishes the survival of L. lactis under energy‐starving conditions. The N‐terminal domain of YfiALl is homologous to HPF from E. coli, whereas the C‐terminal domain has no counterpart in E. coli. By assembling ribosome dimers in vitro, we could dissect the roles of the N‐ and C‐terminal domains of YfiALl. It is concluded that the dimerization and inactivation of ribosomes in L. lactis and E. coli differ in several cellular and molecular aspects. In addition, two‐dimensional maps of dimeric ribosomes from L. lactis obtained by single particle electron microscopy show a marked structural difference in monomer association in comparison to the ribosome dimers in E. coli.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1111/mmi.12468</identifier><identifier>PMID: 24279750</identifier><language>eng</language><publisher>England: Blackwell Publishing Ltd</publisher><subject>Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Comparative analysis ; Dimerization ; E coli ; Escherichia coli - genetics ; Escherichia coli - growth & development ; Escherichia coli - metabolism ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - metabolism ; Gene Deletion ; Lactococcus lactis - genetics ; Lactococcus lactis - growth & development ; Lactococcus lactis - metabolism ; Lactococcus lactis - ultrastructure ; Microscopy, Electron ; Models, Molecular ; Molecules ; Proteins ; Ribosomal Proteins - genetics ; Ribosomal Proteins - metabolism ; Ribosomes - chemistry ; Ribosomes - metabolism ; Ribosomes - ultrastructure ; Sequence Homology, Amino Acid</subject><ispartof>Molecular microbiology, 2014-01, Vol.91 (2), p.394-407</ispartof><rights>2013 John Wiley & Sons Ltd</rights><rights>2013 John Wiley & Sons Ltd.</rights><rights>Copyright Blackwell Publishing Ltd. Jan 2014</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fmmi.12468$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fmmi.12468$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,1432,27915,27916,45565,45566,46400,46824</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24279750$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Puri, Pranav</creatorcontrib><creatorcontrib>Eckhardt, Thomas H.</creatorcontrib><creatorcontrib>Franken, Linda E.</creatorcontrib><creatorcontrib>Fusetti, Fabrizia</creatorcontrib><creatorcontrib>Stuart, Marc C. A.</creatorcontrib><creatorcontrib>Boekema, Egbert J.</creatorcontrib><creatorcontrib>Kuipers, Oscar P.</creatorcontrib><creatorcontrib>Kok, Jan</creatorcontrib><creatorcontrib>Poolman, Bert</creatorcontrib><title>Lactococcus lactis YfiA is necessary and sufficient for ribosome dimerization</title><title>Molecular microbiology</title><addtitle>Mol Microbiol</addtitle><description>Summary
Dimerization and inactivation of ribosomes in Escherichia coli is a two‐step process that involves the binding of ribosome modulation factor (RMF) and hibernation promotion factor (HPF). Lactococcus lactis MG1363 expresses a protein, YfiALl, which associates with ribosomes in the stationary phase of growth and is responsible for dimerization of ribosomes. We show that full‐length YfiALl is necessary and sufficient for ribosome dimerization in L. lactis but also functions heterologously in vitro with E. coli ribosomes. Deletion of the yfiA gene has no effect on the growth rate but diminishes the survival of L. lactis under energy‐starving conditions. The N‐terminal domain of YfiALl is homologous to HPF from E. coli, whereas the C‐terminal domain has no counterpart in E. coli. By assembling ribosome dimers in vitro, we could dissect the roles of the N‐ and C‐terminal domains of YfiALl. It is concluded that the dimerization and inactivation of ribosomes in L. lactis and E. coli differ in several cellular and molecular aspects. In addition, two‐dimensional maps of dimeric ribosomes from L. lactis obtained by single particle electron microscopy show a marked structural difference in monomer association in comparison to the ribosome dimers in E. coli.</description><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Comparative analysis</subject><subject>Dimerization</subject><subject>E coli</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - growth & development</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Gene Deletion</subject><subject>Lactococcus lactis - genetics</subject><subject>Lactococcus lactis - growth & development</subject><subject>Lactococcus lactis - metabolism</subject><subject>Lactococcus lactis - ultrastructure</subject><subject>Microscopy, Electron</subject><subject>Models, Molecular</subject><subject>Molecules</subject><subject>Proteins</subject><subject>Ribosomal Proteins - genetics</subject><subject>Ribosomal Proteins - metabolism</subject><subject>Ribosomes - chemistry</subject><subject>Ribosomes - metabolism</subject><subject>Ribosomes - ultrastructure</subject><subject>Sequence Homology, Amino Acid</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkctKw0AUhgdRbK0ufAEJuHGTdi6Z27IUL4WWbhR0FSaTGZiSZGomQerKjS_qkzi21YVnc344Hz_nnB-ASwTHKNakrt0Y4YyJIzBEhNEUSyqOwRBKClMi8PMAnIWwhhARyMgpGOAMc8kpHILVQunOa691H5Iqahe-Pj5frJsmLiSN0SYE1W4T1ZRJ6K112pmmS6xvk9YVPvjaJKWrTeveVed8cw5OrKqCuTj0EXi6u32cPaSL1f18Nl2kayKgSBFGymQF1ZhYCjmRRSkoZ1QThDXDiNnScsIsh0IrzZmRypZMa1HAklkIyQjc7H03rX_tTejy2gVtqko1xvchR5mEPDoIGdHrf-ja920Tt4sUFxAxSVmkrg5UX9SmzDetq-Ph-e-rIjDZA2-uMtu_OYL5TwZ5zCDfZZAvl_OdIN8Co3ly</recordid><startdate>201401</startdate><enddate>201401</enddate><creator>Puri, Pranav</creator><creator>Eckhardt, Thomas H.</creator><creator>Franken, Linda E.</creator><creator>Fusetti, Fabrizia</creator><creator>Stuart, Marc C. A.</creator><creator>Boekema, Egbert J.</creator><creator>Kuipers, Oscar P.</creator><creator>Kok, Jan</creator><creator>Poolman, Bert</creator><general>Blackwell Publishing Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</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><scope>7X8</scope></search><sort><creationdate>201401</creationdate><title>Lactococcus lactis YfiA is necessary and sufficient for ribosome dimerization</title><author>Puri, Pranav ; Eckhardt, Thomas H. ; Franken, Linda E. ; Fusetti, Fabrizia ; Stuart, Marc C. A. ; Boekema, Egbert J. ; Kuipers, Oscar P. ; Kok, Jan ; Poolman, Bert</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-j3808-121ae4b5c23f50739bd85765c312c6216fdf736f708cac76e9afd6cc8b0d6f003</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Comparative analysis</topic><topic>Dimerization</topic><topic>E coli</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - growth & development</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Gene Deletion</topic><topic>Lactococcus lactis - genetics</topic><topic>Lactococcus lactis - growth & development</topic><topic>Lactococcus lactis - metabolism</topic><topic>Lactococcus lactis - ultrastructure</topic><topic>Microscopy, Electron</topic><topic>Models, Molecular</topic><topic>Molecules</topic><topic>Proteins</topic><topic>Ribosomal Proteins - genetics</topic><topic>Ribosomal Proteins - metabolism</topic><topic>Ribosomes - chemistry</topic><topic>Ribosomes - metabolism</topic><topic>Ribosomes - ultrastructure</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Puri, Pranav</creatorcontrib><creatorcontrib>Eckhardt, Thomas H.</creatorcontrib><creatorcontrib>Franken, Linda E.</creatorcontrib><creatorcontrib>Fusetti, Fabrizia</creatorcontrib><creatorcontrib>Stuart, Marc C. A.</creatorcontrib><creatorcontrib>Boekema, Egbert J.</creatorcontrib><creatorcontrib>Kuipers, Oscar P.</creatorcontrib><creatorcontrib>Kok, Jan</creatorcontrib><creatorcontrib>Poolman, Bert</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</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><collection>MEDLINE - Academic</collection><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Puri, Pranav</au><au>Eckhardt, Thomas H.</au><au>Franken, Linda E.</au><au>Fusetti, Fabrizia</au><au>Stuart, Marc C. A.</au><au>Boekema, Egbert J.</au><au>Kuipers, Oscar P.</au><au>Kok, Jan</au><au>Poolman, Bert</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Lactococcus lactis YfiA is necessary and sufficient for ribosome dimerization</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>2014-01</date><risdate>2014</risdate><volume>91</volume><issue>2</issue><spage>394</spage><epage>407</epage><pages>394-407</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>Summary
Dimerization and inactivation of ribosomes in Escherichia coli is a two‐step process that involves the binding of ribosome modulation factor (RMF) and hibernation promotion factor (HPF). Lactococcus lactis MG1363 expresses a protein, YfiALl, which associates with ribosomes in the stationary phase of growth and is responsible for dimerization of ribosomes. We show that full‐length YfiALl is necessary and sufficient for ribosome dimerization in L. lactis but also functions heterologously in vitro with E. coli ribosomes. Deletion of the yfiA gene has no effect on the growth rate but diminishes the survival of L. lactis under energy‐starving conditions. The N‐terminal domain of YfiALl is homologous to HPF from E. coli, whereas the C‐terminal domain has no counterpart in E. coli. By assembling ribosome dimers in vitro, we could dissect the roles of the N‐ and C‐terminal domains of YfiALl. It is concluded that the dimerization and inactivation of ribosomes in L. lactis and E. coli differ in several cellular and molecular aspects. In addition, two‐dimensional maps of dimeric ribosomes from L. lactis obtained by single particle electron microscopy show a marked structural difference in monomer association in comparison to the ribosome dimers in E. coli.</abstract><cop>England</cop><pub>Blackwell Publishing Ltd</pub><pmid>24279750</pmid><doi>10.1111/mmi.12468</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Bacterial Proteins - genetics Bacterial Proteins - metabolism Comparative analysis Dimerization E coli Escherichia coli - genetics Escherichia coli - growth & development Escherichia coli - metabolism Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Gene Deletion Lactococcus lactis - genetics Lactococcus lactis - growth & development Lactococcus lactis - metabolism Lactococcus lactis - ultrastructure Microscopy, Electron Models, Molecular Molecules Proteins Ribosomal Proteins - genetics Ribosomal Proteins - metabolism Ribosomes - chemistry Ribosomes - metabolism Ribosomes - ultrastructure Sequence Homology, Amino Acid |
| title | Lactococcus lactis YfiA is necessary and sufficient for ribosome dimerization |
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