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Protein kinase activity in Helicobacter pylori
Abstract Based on the predictive analysis of the cellular protein content from the complete genome sequence of Helicobacter pylori, discrepant results were previously reported concerning the occurrence of a protein kinase in this bacterium. To solve this ambiguity, we have directly assayed cellular...
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Published in: | FEMS microbiology letters 1999-07, Vol.176 (2), p.327-332 |
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creator | Grangeasse, Christophe Pichon, Bruno Bollen, Alex Godfroid, Edmond |
description | Abstract
Based on the predictive analysis of the cellular protein content from the complete genome sequence of Helicobacter pylori, discrepant results were previously reported concerning the occurrence of a protein kinase in this bacterium. To solve this ambiguity, we have directly assayed cellular extracts for their capacity of phosphorylating endogenous proteins. At least eight different proteins, ranging from 24 to 200 kDa, were found to be phosphorylated to a varying extent. Individual measurement of their phosphoamino acid composition showed that they all were modified at serine residues. These data indicate that H. pylori does contain a protein-serine kinase activity. |
doi_str_mv | 10.1111/j.1574-6968.1999.tb13679.x |
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Based on the predictive analysis of the cellular protein content from the complete genome sequence of Helicobacter pylori, discrepant results were previously reported concerning the occurrence of a protein kinase in this bacterium. To solve this ambiguity, we have directly assayed cellular extracts for their capacity of phosphorylating endogenous proteins. At least eight different proteins, ranging from 24 to 200 kDa, were found to be phosphorylated to a varying extent. Individual measurement of their phosphoamino acid composition showed that they all were modified at serine residues. These data indicate that H. pylori does contain a protein-serine kinase activity.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.1999.tb13679.x</identifier><identifier>PMID: 10427715</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Adenosine Triphosphate - metabolism ; Bacterial protein phosphorylation ; Bacterial Proteins - metabolism ; Bacteriology ; Biological and medical sciences ; Fundamental and applied biological sciences. Psychology ; Genomes ; Helicobacter pylori ; Helicobacter pylori - enzymology ; Kinases ; Metabolism. Enzymes ; Microbiology ; Nucleotide sequence ; Phosphorylation ; Protein kinase ; Protein Kinases - analysis ; Protein-serine kinase ; Proteins</subject><ispartof>FEMS microbiology letters, 1999-07, Vol.176 (2), p.327-332</ispartof><rights>1999 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved. 1999</rights><rights>1999 INIST-CNRS</rights><rights>1999 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4397-f753209d179729b7de47ba6a20e4cbf8707118d7c6cd465541cbd5c80d0f36063</citedby><cites>FETCH-LOGICAL-c4397-f753209d179729b7de47ba6a20e4cbf8707118d7c6cd465541cbd5c80d0f36063</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1876810$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10427715$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Grangeasse, Christophe</creatorcontrib><creatorcontrib>Pichon, Bruno</creatorcontrib><creatorcontrib>Bollen, Alex</creatorcontrib><creatorcontrib>Godfroid, Edmond</creatorcontrib><title>Protein kinase activity in Helicobacter pylori</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>Abstract
Based on the predictive analysis of the cellular protein content from the complete genome sequence of Helicobacter pylori, discrepant results were previously reported concerning the occurrence of a protein kinase in this bacterium. To solve this ambiguity, we have directly assayed cellular extracts for their capacity of phosphorylating endogenous proteins. At least eight different proteins, ranging from 24 to 200 kDa, were found to be phosphorylated to a varying extent. Individual measurement of their phosphoamino acid composition showed that they all were modified at serine residues. These data indicate that H. pylori does contain a protein-serine kinase activity.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Bacterial protein phosphorylation</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genomes</subject><subject>Helicobacter pylori</subject><subject>Helicobacter pylori - enzymology</subject><subject>Kinases</subject><subject>Metabolism. Enzymes</subject><subject>Microbiology</subject><subject>Nucleotide sequence</subject><subject>Phosphorylation</subject><subject>Protein kinase</subject><subject>Protein Kinases - analysis</subject><subject>Protein-serine kinase</subject><subject>Proteins</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><recordid>eNqVkM1q3DAUhUVoyEymeYUwtCU7O7q2pSt1UQih-YEJ6aJdC1mWQROPPZXsJvP2kfGQlJIuoo3E1XeOjg4hn4CmENf5OgWGRcIlFylIKdO-hJyjTJ8OyPzl6gOZ0xxFAlTijByHsKaUFhnlR2QG8YAIbE7SH77rrWuXD67VwS616d0f1--WcXRjG2e6Mo6sX253TefdR3JY6ybYk_2-IL-uvv-8vElW99e3lxerxBS5xKRGlmdUVoASM1liZQssNdcZtYUpa4EUAUSFhpuq4IwVYMqKGUErWuec8nxBzibfre9-Dzb0auOCsU2jW9sNQXEpM1owGsHP_4DrbvBtzKayHAAZCgGR-jpRxncheFurrXcb7XcKqBo7VWs1FqfG4tTYqdp3qp6i-HT_xFBubPWXdCoxAl_2gA5GN7XXrXHhlRPIBYxRv03Yo2vs7h0J1NXdKs8wGrDJoBu2_5Enb33gGeL2oWs</recordid><startdate>199907</startdate><enddate>199907</enddate><creator>Grangeasse, Christophe</creator><creator>Pichon, Bruno</creator><creator>Bollen, Alex</creator><creator>Godfroid, Edmond</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><general>Oxford University Press</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>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>199907</creationdate><title>Protein kinase activity in Helicobacter pylori</title><author>Grangeasse, Christophe ; Pichon, Bruno ; Bollen, Alex ; Godfroid, Edmond</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4397-f753209d179729b7de47ba6a20e4cbf8707118d7c6cd465541cbd5c80d0f36063</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Bacterial protein phosphorylation</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genomes</topic><topic>Helicobacter pylori</topic><topic>Helicobacter pylori - enzymology</topic><topic>Kinases</topic><topic>Metabolism. 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Based on the predictive analysis of the cellular protein content from the complete genome sequence of Helicobacter pylori, discrepant results were previously reported concerning the occurrence of a protein kinase in this bacterium. To solve this ambiguity, we have directly assayed cellular extracts for their capacity of phosphorylating endogenous proteins. At least eight different proteins, ranging from 24 to 200 kDa, were found to be phosphorylated to a varying extent. Individual measurement of their phosphoamino acid composition showed that they all were modified at serine residues. These data indicate that H. pylori does contain a protein-serine kinase activity.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>10427715</pmid><doi>10.1111/j.1574-6968.1999.tb13679.x</doi><tpages>6</tpages></addata></record> |
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subjects | Adenosine Triphosphate - metabolism Bacterial protein phosphorylation Bacterial Proteins - metabolism Bacteriology Biological and medical sciences Fundamental and applied biological sciences. Psychology Genomes Helicobacter pylori Helicobacter pylori - enzymology Kinases Metabolism. Enzymes Microbiology Nucleotide sequence Phosphorylation Protein kinase Protein Kinases - analysis Protein-serine kinase Proteins |
title | Protein kinase activity in Helicobacter pylori |
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