Two FHA domains on an ABC transporter, Rv1747, mediate its phosphorylation by PknF, a Ser/Thr protein kinase from Mycobacterium tuberculosis
Bacterial genomics have revealed the widespread occurrence of eukaryotic-like protein kinases in prokaryotes, but little is known about their regulation, endogenous substrates, and physiological role. The present study concerns one of these enzymes, the serine/threonine protein kinase PknF from Myco...
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| Veröffentlicht in: | FEMS microbiology letters 2004-05, Vol.234 (2), p.215-223 |
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| container_title | FEMS microbiology letters |
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| creator | Molle, Virginie Soulat, Didier Jault, Jean-Michel Grangeasse, Christophe Cozzone, Alain J. Prost, Jean-François |
| description | Bacterial genomics have revealed the widespread occurrence of eukaryotic-like protein kinases in prokaryotes, but little is known about their regulation, endogenous substrates, and physiological role. The present study concerns one of these enzymes, the serine/threonine protein kinase PknF from
Mycobacterium tuberculosis. It is shown that, in addition to its autokinase activity, PknF is able to phosphorylate Rv1747, a newly described ABC transporter. This reaction appears to involve two FHA domains of Rv1747. It is suggested that recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of PknF. |
| doi_str_mv | 10.1016/j.femsle.2004.03.033 |
| format | Article |
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Mycobacterium tuberculosis. It is shown that, in addition to its autokinase activity, PknF is able to phosphorylate Rv1747, a newly described ABC transporter. This reaction appears to involve two FHA domains of Rv1747. It is suggested that recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of PknF.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1016/j.femsle.2004.03.033</identifier><identifier>PMID: 15135525</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford: Elsevier B.V</publisher><subject>ABC transporter ; Amino Acid Sequence ; Amino Acid Substitution ; ATP-Binding Cassette Transporters - chemistry ; ATP-Binding Cassette Transporters - genetics ; ATP-Binding Cassette Transporters - metabolism ; Bacterial Proteins - chemistry ; Bacterial Proteins - metabolism ; Bacteriology ; Base Sequence ; Binding Sites ; Biological and medical sciences ; DNA Primers ; FHA domain ; Fundamental and applied biological sciences. Psychology ; Genome, Bacterial ; Genotype ; Glutathione Transferase - metabolism ; Life Sciences ; Microbiology ; Microbiology and Parasitology ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mycobacterium tuberculosis ; Mycobacterium tuberculosis - enzymology ; Permeability, membrane transport, intracellular transport ; Phosphorylation ; Protein phosphorylation ; Protein-Serine-Threonine Kinases - chemistry ; Protein-Serine-Threonine Kinases - genetics ; Protein-Serine-Threonine Kinases - metabolism ; Recombinant Fusion Proteins - metabolism ; Sequence Alignment ; Sequence Homology, Amino Acid ; Ser/Thr protein kinase</subject><ispartof>FEMS microbiology letters, 2004-05, Vol.234 (2), p.215-223</ispartof><rights>2004 Federation of European Microbiological Societies</rights><rights>Copyright 2004 Federation of European Microbiological Societies</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c408t-e37bb8fd3ee32e8ab48a1955ca4aba1636363fed903644ae6236db22bddabfff3</citedby><orcidid>0000-0002-6573-3411 ; 0000-0002-5484-4589 ; 0000-0003-1743-2777</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27923,27924</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15900953$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15135525$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-02282924$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Molle, Virginie</creatorcontrib><creatorcontrib>Soulat, Didier</creatorcontrib><creatorcontrib>Jault, Jean-Michel</creatorcontrib><creatorcontrib>Grangeasse, Christophe</creatorcontrib><creatorcontrib>Cozzone, Alain J.</creatorcontrib><creatorcontrib>Prost, Jean-François</creatorcontrib><title>Two FHA domains on an ABC transporter, Rv1747, mediate its phosphorylation by PknF, a Ser/Thr protein kinase from Mycobacterium tuberculosis</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>Bacterial genomics have revealed the widespread occurrence of eukaryotic-like protein kinases in prokaryotes, but little is known about their regulation, endogenous substrates, and physiological role. The present study concerns one of these enzymes, the serine/threonine protein kinase PknF from
Mycobacterium tuberculosis. It is shown that, in addition to its autokinase activity, PknF is able to phosphorylate Rv1747, a newly described ABC transporter. This reaction appears to involve two FHA domains of Rv1747. It is suggested that recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of PknF.</description><subject>ABC transporter</subject><subject>Amino Acid Sequence</subject><subject>Amino Acid Substitution</subject><subject>ATP-Binding Cassette Transporters - chemistry</subject><subject>ATP-Binding Cassette Transporters - genetics</subject><subject>ATP-Binding Cassette Transporters - metabolism</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>DNA Primers</subject><subject>FHA domain</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genome, Bacterial</subject><subject>Genotype</subject><subject>Glutathione Transferase - metabolism</subject><subject>Life Sciences</subject><subject>Microbiology</subject><subject>Microbiology and Parasitology</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Mycobacterium tuberculosis</subject><subject>Mycobacterium tuberculosis - enzymology</subject><subject>Permeability, membrane transport, intracellular transport</subject><subject>Phosphorylation</subject><subject>Protein phosphorylation</subject><subject>Protein-Serine-Threonine Kinases - chemistry</subject><subject>Protein-Serine-Threonine Kinases - genetics</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Ser/Thr protein kinase</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkl2LEzEUhoMobnf1H4jkRkFou_mYzxuhlq0VKorW63CSOUPTnZnUJFPpf_BHm9IqkhMC4ckLeXgJecXZnDNe3O_nLfahw7lgLJszmUY-IROel9msqIvqKZkwWVYzzuryhtyGsGcJFKx4Tm54zmWei3xCfm9_ObpaL2jjerBDoG6gMNDFhyWNHoZwcD6in9JvR15m5ZT22FiISG0M9LBzIW1_6iDa9E6f6NfHYTWlQL-jv9_uPD14F9EO9NEOEJC23vX088k4DSbF2rGncdTozdi5YMML8qyFLuDL63lHfqwetsv1bPPl46flYjMzGaviDGWpddU2ElEKrEBnFfA6zw1koIEX8rxabGomiywDLIQsGi2EbhrQbdvKO_LukruDTh287cGflAOr1ouNOt8xISpRi-zIE_v2wqav_BwxRNXbYLDrYEA3BsUrxuqM5Ql8fQVHnSz9y_3rOgFvrgAEA12b9Bob_uPqlJTLxL2_cJgUHC16FYzFwSTzHk1UjbOKM3UugdqrSwnUuQSKyTRS_gFQOqVi</recordid><startdate>20040515</startdate><enddate>20040515</enddate><creator>Molle, Virginie</creator><creator>Soulat, Didier</creator><creator>Jault, Jean-Michel</creator><creator>Grangeasse, Christophe</creator><creator>Cozzone, Alain J.</creator><creator>Prost, Jean-François</creator><general>Elsevier B.V</general><general>Blackwell</general><general>Wiley-Blackwell</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QL</scope><scope>C1K</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0002-6573-3411</orcidid><orcidid>https://orcid.org/0000-0002-5484-4589</orcidid><orcidid>https://orcid.org/0000-0003-1743-2777</orcidid></search><sort><creationdate>20040515</creationdate><title>Two FHA domains on an ABC transporter, Rv1747, mediate its phosphorylation by PknF, a Ser/Thr protein kinase from Mycobacterium tuberculosis</title><author>Molle, Virginie ; Soulat, Didier ; Jault, Jean-Michel ; Grangeasse, Christophe ; Cozzone, Alain J. ; Prost, Jean-François</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c408t-e37bb8fd3ee32e8ab48a1955ca4aba1636363fed903644ae6236db22bddabfff3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>ABC transporter</topic><topic>Amino Acid Sequence</topic><topic>Amino Acid Substitution</topic><topic>ATP-Binding Cassette Transporters - chemistry</topic><topic>ATP-Binding Cassette Transporters - genetics</topic><topic>ATP-Binding Cassette Transporters - metabolism</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacteriology</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>DNA Primers</topic><topic>FHA domain</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genome, Bacterial</topic><topic>Genotype</topic><topic>Glutathione Transferase - metabolism</topic><topic>Life Sciences</topic><topic>Microbiology</topic><topic>Microbiology and Parasitology</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed</topic><topic>Mycobacterium tuberculosis</topic><topic>Mycobacterium tuberculosis - enzymology</topic><topic>Permeability, membrane transport, intracellular transport</topic><topic>Phosphorylation</topic><topic>Protein phosphorylation</topic><topic>Protein-Serine-Threonine Kinases - chemistry</topic><topic>Protein-Serine-Threonine Kinases - genetics</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>Ser/Thr protein kinase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Molle, Virginie</creatorcontrib><creatorcontrib>Soulat, Didier</creatorcontrib><creatorcontrib>Jault, Jean-Michel</creatorcontrib><creatorcontrib>Grangeasse, Christophe</creatorcontrib><creatorcontrib>Cozzone, Alain J.</creatorcontrib><creatorcontrib>Prost, Jean-François</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Molle, Virginie</au><au>Soulat, Didier</au><au>Jault, Jean-Michel</au><au>Grangeasse, Christophe</au><au>Cozzone, Alain J.</au><au>Prost, Jean-François</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Two FHA domains on an ABC transporter, Rv1747, mediate its phosphorylation by PknF, a Ser/Thr protein kinase from Mycobacterium tuberculosis</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>2004-05-15</date><risdate>2004</risdate><volume>234</volume><issue>2</issue><spage>215</spage><epage>223</epage><pages>215-223</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>Bacterial genomics have revealed the widespread occurrence of eukaryotic-like protein kinases in prokaryotes, but little is known about their regulation, endogenous substrates, and physiological role. 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Mycobacterium tuberculosis. It is shown that, in addition to its autokinase activity, PknF is able to phosphorylate Rv1747, a newly described ABC transporter. This reaction appears to involve two FHA domains of Rv1747. It is suggested that recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of PknF.</abstract><cop>Oxford</cop><pub>Elsevier B.V</pub><pmid>15135525</pmid><doi>10.1016/j.femsle.2004.03.033</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0002-6573-3411</orcidid><orcidid>https://orcid.org/0000-0002-5484-4589</orcidid><orcidid>https://orcid.org/0000-0003-1743-2777</orcidid></addata></record> |
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| identifier | ISSN: 0378-1097 |
| ispartof | FEMS microbiology letters, 2004-05, Vol.234 (2), p.215-223 |
| issn | 0378-1097 1574-6968 |
| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Oxford University Press Journals All Titles (1996-Current); Alma/SFX Local Collection |
| subjects | ABC transporter Amino Acid Sequence Amino Acid Substitution ATP-Binding Cassette Transporters - chemistry ATP-Binding Cassette Transporters - genetics ATP-Binding Cassette Transporters - metabolism Bacterial Proteins - chemistry Bacterial Proteins - metabolism Bacteriology Base Sequence Binding Sites Biological and medical sciences DNA Primers FHA domain Fundamental and applied biological sciences. Psychology Genome, Bacterial Genotype Glutathione Transferase - metabolism Life Sciences Microbiology Microbiology and Parasitology Molecular Sequence Data Mutagenesis, Site-Directed Mycobacterium tuberculosis Mycobacterium tuberculosis - enzymology Permeability, membrane transport, intracellular transport Phosphorylation Protein phosphorylation Protein-Serine-Threonine Kinases - chemistry Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism Recombinant Fusion Proteins - metabolism Sequence Alignment Sequence Homology, Amino Acid Ser/Thr protein kinase |
| title | Two FHA domains on an ABC transporter, Rv1747, mediate its phosphorylation by PknF, a Ser/Thr protein kinase from Mycobacterium tuberculosis |
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