Mutations in hpyAVIBM, C5 cytosine DNA methyltransferase from Helicobacter pylori result in relaxed specificity
The genome of Helicobacter pylori is rich in restriction–modification (RM) systems. Approximately 4% of the genome codes for components of RM systems. hpyAVIBM, which codes for a phase‐variable C5 cytosine methyltransferase (MTase) from H. pylori, lacks a cognate restriction enzyme. Over‐expression...
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description | The genome of Helicobacter pylori is rich in restriction–modification (RM) systems. Approximately 4% of the genome codes for components of RM systems. hpyAVIBM, which codes for a phase‐variable C5 cytosine methyltransferase (MTase) from H. pylori, lacks a cognate restriction enzyme. Over‐expression of M.HpyAVIB in Escherichia coli enhances the rate of mutations. However, when the catalytically inactive F9N or C82W mutants of M.HpyAVIB were expressed in E. coli, mutations were not observed. The M.HpyAVIB gene itself was mutated to give rise to different variants of the MTase. M.HpyAVIB variants were purified and differences in kinetic properties and specificity were observed. Intriguingly, purified MTase variants showed relaxed substrate specificity. Homologues of hpyAVIBM homologues amplified and sequenced from different clinical isolates showed similar variations in sequence. Thus, hpyAVIBM presents an interesting example of allelic variations in H. pylori where changes in the nucleotide sequence result in proteins with new properties.
HpyAVIBM codes for a C5– cytosine MTase from H. pylori. It was observed that expression of M.HpyAVIB in E. coli enhanced the mutation rate. hpyAVIBM itself was mutated to give rise to different variants. Purified MTase variants showed relaxed substrate specificity. Thus, hpyAVIBM presents an interesting example of allelic variations in H. pylori where changes in the nucleotide sequence result in proteins with new properties. |
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HpyAVIBM codes for a C5– cytosine MTase from H. pylori. It was observed that expression of M.HpyAVIB in E. coli enhanced the mutation rate. hpyAVIBM itself was mutated to give rise to different variants. Purified MTase variants showed relaxed substrate specificity. Thus, hpyAVIBM presents an interesting example of allelic variations in H. pylori where changes in the nucleotide sequence result in proteins with new properties.</description><identifier>ISSN: 1742-464X</identifier><identifier>EISSN: 1742-4658</identifier><identifier>DOI: 10.1111/j.1742-4658.2012.08502.x</identifier><identifier>PMID: 22269034</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Base Sequence ; Cytosine - metabolism ; DNA Methylation ; DNA methyltransferase ; DNA, Bacterial - chemistry ; DNA, Bacterial - metabolism ; DNA-Cytosine Methylases - chemistry ; DNA-Cytosine Methylases - genetics ; DNA-Cytosine Methylases - metabolism ; EcoDam ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Helicobacter pylori - enzymology ; Helicobacter pylori - genetics ; Helicobacter pylori - metabolism ; Helicobacter pylori ; mismatch repair pathway ; Molecular Sequence Data ; Mutation ; mutations ; Substrate Specificity</subject><ispartof>The FEBS journal, 2012-03, Vol.279 (6), p.1080-1092</ispartof><rights>2012 The Authors Journal compilation © 2012 FEBS</rights><rights>2012 The Authors Journal compilation © 2012 FEBS.</rights><lds50>peer_reviewed</lds50><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%2Fj.1742-4658.2012.08502.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1742-4658.2012.08502.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,1433,27924,27925,45574,45575,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22269034$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kumar, Ritesh</creatorcontrib><creatorcontrib>Sabareesh, Varatharajan</creatorcontrib><creatorcontrib>Mukhopadhyay, Asish K.</creatorcontrib><creatorcontrib>Rao, Desirazu N.</creatorcontrib><title>Mutations in hpyAVIBM, C5 cytosine DNA methyltransferase from Helicobacter pylori result in relaxed specificity</title><title>The FEBS journal</title><addtitle>FEBS J</addtitle><description>The genome of Helicobacter pylori is rich in restriction–modification (RM) systems. Approximately 4% of the genome codes for components of RM systems. hpyAVIBM, which codes for a phase‐variable C5 cytosine methyltransferase (MTase) from H. pylori, lacks a cognate restriction enzyme. Over‐expression of M.HpyAVIB in Escherichia coli enhances the rate of mutations. However, when the catalytically inactive F9N or C82W mutants of M.HpyAVIB were expressed in E. coli, mutations were not observed. The M.HpyAVIB gene itself was mutated to give rise to different variants of the MTase. M.HpyAVIB variants were purified and differences in kinetic properties and specificity were observed. Intriguingly, purified MTase variants showed relaxed substrate specificity. Homologues of hpyAVIBM homologues amplified and sequenced from different clinical isolates showed similar variations in sequence. Thus, hpyAVIBM presents an interesting example of allelic variations in H. pylori where changes in the nucleotide sequence result in proteins with new properties.
HpyAVIBM codes for a C5– cytosine MTase from H. pylori. It was observed that expression of M.HpyAVIB in E. coli enhanced the mutation rate. hpyAVIBM itself was mutated to give rise to different variants. Purified MTase variants showed relaxed substrate specificity. Thus, hpyAVIBM presents an interesting example of allelic variations in H. pylori where changes in the nucleotide sequence result in proteins with new properties.</description><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Base Sequence</subject><subject>Cytosine - metabolism</subject><subject>DNA Methylation</subject><subject>DNA methyltransferase</subject><subject>DNA, Bacterial - chemistry</subject><subject>DNA, Bacterial - metabolism</subject><subject>DNA-Cytosine Methylases - chemistry</subject><subject>DNA-Cytosine Methylases - genetics</subject><subject>DNA-Cytosine Methylases - metabolism</subject><subject>EcoDam</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Helicobacter pylori - enzymology</subject><subject>Helicobacter pylori - genetics</subject><subject>Helicobacter pylori - metabolism</subject><subject>Helicobacter pylori</subject><subject>mismatch repair pathway</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>mutations</subject><subject>Substrate Specificity</subject><issn>1742-464X</issn><issn>1742-4658</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kblOxDAYhC0E4n4F5JKCDT6TuEFallPiKDhEZzmOI7xyDmxHbDok3pQnYcOxf_OPNJ-mmAEAYpTg5R3PE5wxMmEpzxOCMElQzhFJFmtge2WsrzR72QI7IcwRopwJsQm2CCGpQJRtg7fbPqpo2yZA28DXbpg-X5_eHsEZh3qIbbCNgWd3U1ib-Dq46FUTKuNVMLDybQ2vjLO6LZSOxn99fHaDa72F3oTexTHQG6cWpoShM9pWVts47IGNSrlg9v_-Lni6OH-cXU1u7i-vZ9ObSYdFSiYVUwXmvEgzUdAy44IRjphSOcmrUolCU6TzUtOMZKhSimuuqWKYFTlFqWaa7oLD39zOt2-9CVHWNmjjnGpM2weJyTKKMsHEEj34Q_uiNqXsvK2VH-R_TUvg5Bd4t84MKx8jOc4h53JsWo6ty3EO-TOHXMiL89OHUdJvpNWADg</recordid><startdate>201203</startdate><enddate>201203</enddate><creator>Kumar, Ritesh</creator><creator>Sabareesh, Varatharajan</creator><creator>Mukhopadhyay, Asish K.</creator><creator>Rao, Desirazu N.</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>7X8</scope></search><sort><creationdate>201203</creationdate><title>Mutations in hpyAVIBM, C5 cytosine DNA methyltransferase from Helicobacter pylori result in relaxed specificity</title><author>Kumar, Ritesh ; Sabareesh, Varatharajan ; Mukhopadhyay, Asish K. ; Rao, Desirazu N.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p1962-f4ab155b679b3d75942504aa828fda9bc30c8dc37270faa5c5c3a414b8306c4c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Base Sequence</topic><topic>Cytosine - metabolism</topic><topic>DNA Methylation</topic><topic>DNA methyltransferase</topic><topic>DNA, Bacterial - chemistry</topic><topic>DNA, Bacterial - metabolism</topic><topic>DNA-Cytosine Methylases - chemistry</topic><topic>DNA-Cytosine Methylases - genetics</topic><topic>DNA-Cytosine Methylases - metabolism</topic><topic>EcoDam</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Helicobacter pylori - enzymology</topic><topic>Helicobacter pylori - genetics</topic><topic>Helicobacter pylori - metabolism</topic><topic>Helicobacter pylori</topic><topic>mismatch repair pathway</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>mutations</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kumar, Ritesh</creatorcontrib><creatorcontrib>Sabareesh, Varatharajan</creatorcontrib><creatorcontrib>Mukhopadhyay, Asish K.</creatorcontrib><creatorcontrib>Rao, Desirazu N.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>The FEBS journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kumar, Ritesh</au><au>Sabareesh, Varatharajan</au><au>Mukhopadhyay, Asish K.</au><au>Rao, Desirazu N.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mutations in hpyAVIBM, C5 cytosine DNA methyltransferase from Helicobacter pylori result in relaxed specificity</atitle><jtitle>The FEBS journal</jtitle><addtitle>FEBS J</addtitle><date>2012-03</date><risdate>2012</risdate><volume>279</volume><issue>6</issue><spage>1080</spage><epage>1092</epage><pages>1080-1092</pages><issn>1742-464X</issn><eissn>1742-4658</eissn><abstract>The genome of Helicobacter pylori is rich in restriction–modification (RM) systems. Approximately 4% of the genome codes for components of RM systems. hpyAVIBM, which codes for a phase‐variable C5 cytosine methyltransferase (MTase) from H. pylori, lacks a cognate restriction enzyme. Over‐expression of M.HpyAVIB in Escherichia coli enhances the rate of mutations. However, when the catalytically inactive F9N or C82W mutants of M.HpyAVIB were expressed in E. coli, mutations were not observed. The M.HpyAVIB gene itself was mutated to give rise to different variants of the MTase. M.HpyAVIB variants were purified and differences in kinetic properties and specificity were observed. Intriguingly, purified MTase variants showed relaxed substrate specificity. Homologues of hpyAVIBM homologues amplified and sequenced from different clinical isolates showed similar variations in sequence. Thus, hpyAVIBM presents an interesting example of allelic variations in H. pylori where changes in the nucleotide sequence result in proteins with new properties.
HpyAVIBM codes for a C5– cytosine MTase from H. pylori. It was observed that expression of M.HpyAVIB in E. coli enhanced the mutation rate. hpyAVIBM itself was mutated to give rise to different variants. Purified MTase variants showed relaxed substrate specificity. Thus, hpyAVIBM presents an interesting example of allelic variations in H. pylori where changes in the nucleotide sequence result in proteins with new properties.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>22269034</pmid><doi>10.1111/j.1742-4658.2012.08502.x</doi><tpages>13</tpages></addata></record> |
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subjects | Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Base Sequence Cytosine - metabolism DNA Methylation DNA methyltransferase DNA, Bacterial - chemistry DNA, Bacterial - metabolism DNA-Cytosine Methylases - chemistry DNA-Cytosine Methylases - genetics DNA-Cytosine Methylases - metabolism EcoDam Escherichia coli - genetics Escherichia coli - metabolism Helicobacter pylori - enzymology Helicobacter pylori - genetics Helicobacter pylori - metabolism Helicobacter pylori mismatch repair pathway Molecular Sequence Data Mutation mutations Substrate Specificity |
title | Mutations in hpyAVIBM, C5 cytosine DNA methyltransferase from Helicobacter pylori result in relaxed specificity |
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