Instability of bacteriophage Mu transposase and the role of host Hfl protein
Summary The activity of the transposase of bacteriophage Mu is unstable, requiring the protein to be synthesized throughout the lytic cycle (Pato and Reich, 1982). Using Western blot analysis, we analysed the stability of the transposase protein during the lytic cycle and found that it, too, is unst...
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| Veröffentlicht in: | Molecular microbiology 1990-11, Vol.4 (11), p.1891-1897 |
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| container_end_page | 1897 |
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| container_issue | 11 |
| container_start_page | 1891 |
| container_title | Molecular microbiology |
| container_volume | 4 |
| creator | Gama, M.‐J. Toussaint, A. Pato, M. L. |
| description | Summary
The activity of the transposase of bacteriophage Mu is unstable, requiring the protein to be synthesized throughout the lytic cycle (Pato and Reich, 1982). Using Western blot analysis, we analysed the stability of the transposase protein during the lytic cycle and found that it, too, is unstable. The instability of the protein is observed both in the presence and the absence of Mu ONA replication, and is independent of other Mu‐encoded proteins and the transposase binding sites at the Mu genome ends. Stability of the protein is enhanced in host strains mutated at the hfl locus; however, stability of the transposase activity is not enhanced in these strains, suggesting that functional inactivation of the protein is not simply a result of its proteolysis. |
| doi_str_mv | 10.1111/j.1365-2958.1990.tb02038.x |
| format | Article |
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The activity of the transposase of bacteriophage Mu is unstable, requiring the protein to be synthesized throughout the lytic cycle (Pato and Reich, 1982). Using Western blot analysis, we analysed the stability of the transposase protein during the lytic cycle and found that it, too, is unstable. The instability of the protein is observed both in the presence and the absence of Mu ONA replication, and is independent of other Mu‐encoded proteins and the transposase binding sites at the Mu genome ends. Stability of the protein is enhanced in host strains mutated at the hfl locus; however, stability of the transposase activity is not enhanced in these strains, suggesting that functional inactivation of the protein is not simply a result of its proteolysis.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1111/j.1365-2958.1990.tb02038.x</identifier><identifier>PMID: 1964485</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Bacteriophage mu - enzymology ; Bacteriophage mu - genetics ; Biological and medical sciences ; DNA Replication ; Enzyme Stability ; Escherichia coli - enzymology ; Escherichia coli - genetics ; Fundamental and applied biological sciences. Psychology ; Genes, Viral ; Microbiology ; Mutation ; Nucleotidyltransferases - metabolism ; Plasmids ; Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains ; Transposases ; Viral Proteins - metabolism ; Virology</subject><ispartof>Molecular microbiology, 1990-11, Vol.4 (11), p.1891-1897</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4311-f5b2eb088867a37c151da1674055eaf6c0024a062de50c81339137a73b6d5b633</citedby><cites>FETCH-LOGICAL-c4311-f5b2eb088867a37c151da1674055eaf6c0024a062de50c81339137a73b6d5b633</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.1365-2958.1990.tb02038.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1365-2958.1990.tb02038.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19473052$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1964485$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gama, M.‐J.</creatorcontrib><creatorcontrib>Toussaint, A.</creatorcontrib><creatorcontrib>Pato, M. L.</creatorcontrib><title>Instability of bacteriophage Mu transposase and the role of host Hfl protein</title><title>Molecular microbiology</title><addtitle>Mol Microbiol</addtitle><description>Summary
The activity of the transposase of bacteriophage Mu is unstable, requiring the protein to be synthesized throughout the lytic cycle (Pato and Reich, 1982). Using Western blot analysis, we analysed the stability of the transposase protein during the lytic cycle and found that it, too, is unstable. The instability of the protein is observed both in the presence and the absence of Mu ONA replication, and is independent of other Mu‐encoded proteins and the transposase binding sites at the Mu genome ends. Stability of the protein is enhanced in host strains mutated at the hfl locus; however, stability of the transposase activity is not enhanced in these strains, suggesting that functional inactivation of the protein is not simply a result of its proteolysis.</description><subject>Bacteriophage mu - enzymology</subject><subject>Bacteriophage mu - genetics</subject><subject>Biological and medical sciences</subject><subject>DNA Replication</subject><subject>Enzyme Stability</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes, Viral</subject><subject>Microbiology</subject><subject>Mutation</subject><subject>Nucleotidyltransferases - metabolism</subject><subject>Plasmids</subject><subject>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</subject><subject>Transposases</subject><subject>Viral Proteins - metabolism</subject><subject>Virology</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkMtKxDAUhoMoOl4eQQiC7lrPSZo0dSMiXgZmcKPgLqRp6nTotGOTQeftbZlB3Ylncxb_dy58hJwhxNjX5TxGLkXEMqFizDKIQw4MuIo_d8joO9olI8gERFyx1wNy6P0cADlIvk_2MZNJosSITMaNDyav6iqsaVvS3Njguqpdzsybo9MVDZ1p_LL1xjtqmoKGmaNdW7sBnrU-0MeypsuuDa5qjsleaWrvTrb9iLzc3z3fPkaTp4fx7c0ksglHjEqRM5eDUkqmhqcWBRYGZZqAEM6U0gKwxIBkhRNgFXKeIU9NynNZiFxyfkQuNnv7u-8r54NeVN66ujaNa1deK2CZQpH8CaJQLBFC9ODVBrRd633nSr3sqoXp1hpBD871XA9i9SBWD8711rn-7IdPt1dW-cIVP6MbyX1-vs2Nt6Yue6O28r-wJOUgWM9db7iPqnbrf3ygp9Mxql7SFwt-nUI</recordid><startdate>199011</startdate><enddate>199011</enddate><creator>Gama, M.‐J.</creator><creator>Toussaint, A.</creator><creator>Pato, M. L.</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>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>199011</creationdate><title>Instability of bacteriophage Mu transposase and the role of host Hfl protein</title><author>Gama, M.‐J. ; Toussaint, A. ; Pato, M. L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4311-f5b2eb088867a37c151da1674055eaf6c0024a062de50c81339137a73b6d5b633</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Bacteriophage mu - enzymology</topic><topic>Bacteriophage mu - genetics</topic><topic>Biological and medical sciences</topic><topic>DNA Replication</topic><topic>Enzyme Stability</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes, Viral</topic><topic>Microbiology</topic><topic>Mutation</topic><topic>Nucleotidyltransferases - metabolism</topic><topic>Plasmids</topic><topic>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</topic><topic>Transposases</topic><topic>Viral Proteins - metabolism</topic><topic>Virology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gama, M.‐J.</creatorcontrib><creatorcontrib>Toussaint, A.</creatorcontrib><creatorcontrib>Pato, M. L.</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>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gama, M.‐J.</au><au>Toussaint, A.</au><au>Pato, M. L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Instability of bacteriophage Mu transposase and the role of host Hfl protein</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>1990-11</date><risdate>1990</risdate><volume>4</volume><issue>11</issue><spage>1891</spage><epage>1897</epage><pages>1891-1897</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>Summary
The activity of the transposase of bacteriophage Mu is unstable, requiring the protein to be synthesized throughout the lytic cycle (Pato and Reich, 1982). Using Western blot analysis, we analysed the stability of the transposase protein during the lytic cycle and found that it, too, is unstable. The instability of the protein is observed both in the presence and the absence of Mu ONA replication, and is independent of other Mu‐encoded proteins and the transposase binding sites at the Mu genome ends. Stability of the protein is enhanced in host strains mutated at the hfl locus; however, stability of the transposase activity is not enhanced in these strains, suggesting that functional inactivation of the protein is not simply a result of its proteolysis.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>1964485</pmid><doi>10.1111/j.1365-2958.1990.tb02038.x</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0950-382X |
| ispartof | Molecular microbiology, 1990-11, Vol.4 (11), p.1891-1897 |
| issn | 0950-382X 1365-2958 |
| language | eng |
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| source | MEDLINE; Access via Wiley Online Library |
| subjects | Bacteriophage mu - enzymology Bacteriophage mu - genetics Biological and medical sciences DNA Replication Enzyme Stability Escherichia coli - enzymology Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Genes, Viral Microbiology Mutation Nucleotidyltransferases - metabolism Plasmids Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains Transposases Viral Proteins - metabolism Virology |
| title | Instability of bacteriophage Mu transposase and the role of host Hfl protein |
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