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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Veröffentlicht in:The FEBS journal 2012-03, Vol.279 (6), p.1080-1092
Hauptverfasser: Kumar, Ritesh, Sabareesh, Varatharajan, Mukhopadhyay, Asish K., Rao, Desirazu N.
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Mukhopadhyay, Asish K.
Rao, Desirazu N.
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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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. 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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. 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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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