Polyphosphate kinase 1, a conserved bacterial enzyme, in a eukaryote, Dictyostelium discoideum, with a role in cytokinesis
Polyphosphate kinase 1 (PPK1), the principal enzyme responsible for reversible synthesis of polyphosphate (poly P) from the terminal phosphate of ATP, is highly conserved in bacteria and archaea. Dictyostelium discoideum, a social slime mold, is one of a few eukaryotes known to possess a PPK1 homolo...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2007-10, Vol.104 (42), p.16486-16491 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Zhang, Haiyu Gómez-García, María R Shi, Xiaobing Rao, Narayana N Kornberg, Arthur |
| description | Polyphosphate kinase 1 (PPK1), the principal enzyme responsible for reversible synthesis of polyphosphate (poly P) from the terminal phosphate of ATP, is highly conserved in bacteria and archaea. Dictyostelium discoideum, a social slime mold, is one of a few eukaryotes known to possess a PPK1 homolog (DdPPK1). Compared with PPK1 of Escherichia coli, DdPPK1 contains the conserved residues for ATP binding and autophosphorylation, but has an N-terminal extension of 370 aa, lacking homology with any known protein. Polyphosphate or ATP promote oligomerization of the enzyme in vitro. The DdPPK1 products are heterogeneous in chain length and shorter than those of E. coli. The unique DdPPK1 N-terminal domain was shown to be necessary for its enzymatic activity, cellular localization, and physiological functions. Mutants of DdPPK1, as previously reported, are defective in development, sporulation, and predation, and as shown here, in late stages of cytokinesis and cell division. |
| doi_str_mv | 10.1073/pnas.0706847104 |
| format | Article |
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Dictyostelium discoideum, a social slime mold, is one of a few eukaryotes known to possess a PPK1 homolog (DdPPK1). Compared with PPK1 of Escherichia coli, DdPPK1 contains the conserved residues for ATP binding and autophosphorylation, but has an N-terminal extension of 370 aa, lacking homology with any known protein. Polyphosphate or ATP promote oligomerization of the enzyme in vitro. The DdPPK1 products are heterogeneous in chain length and shorter than those of E. coli. The unique DdPPK1 N-terminal domain was shown to be necessary for its enzymatic activity, cellular localization, and physiological functions. Mutants of DdPPK1, as previously reported, are defective in development, sporulation, and predation, and as shown here, in late stages of cytokinesis and cell division.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0706847104</identifier><identifier>PMID: 17940044</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Adenosine triphosphatase ; Adenosine Triphosphate - chemistry ; Amino Acid Sequence ; Animals ; Antibodies ; Archaea ; Biological Sciences ; Cell division ; Cell growth ; Cells ; Cytokinesis ; Cytokinesis - genetics ; Daughter cells ; Dictyostelium - enzymology ; Dictyostelium discoideum ; E coli ; Enzymes ; Escherichia coli ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - genetics ; Eukaryotes ; Eukaryotic cells ; Green Fluorescent Proteins - analysis ; Green Fluorescent Proteins - genetics ; Molecular Sequence Data ; Mutation ; Phosphates ; Phosphotransferases (Alcohol Group Acceptor) - chemistry ; Phosphotransferases (Alcohol Group Acceptor) - genetics ; Phosphotransferases (Phosphate Group Acceptor) - chemistry ; Phosphotransferases (Phosphate Group Acceptor) - genetics ; Phosphotransferases (Phosphate Group Acceptor) - metabolism ; Polyphosphates ; Protein Structure, Tertiary ; Proteins ; Protozoan Proteins - chemistry ; Protozoan Proteins - genetics ; Protozoan Proteins - metabolism</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2007-10, Vol.104 (42), p.16486-16491</ispartof><rights>Copyright 2007 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Oct 16, 2007</rights><rights>2007 by The National Academy of Sciences of the USA 2007</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c554t-97297f35cdfe9d9331bbc22d07bf227a8189c51c4ce447248bdb715f0e249a513</citedby><cites>FETCH-LOGICAL-c554t-97297f35cdfe9d9331bbc22d07bf227a8189c51c4ce447248bdb715f0e249a513</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/104/42.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/25450079$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/25450079$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17940044$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, Haiyu</creatorcontrib><creatorcontrib>Gómez-García, María R</creatorcontrib><creatorcontrib>Shi, Xiaobing</creatorcontrib><creatorcontrib>Rao, Narayana N</creatorcontrib><creatorcontrib>Kornberg, Arthur</creatorcontrib><title>Polyphosphate kinase 1, a conserved bacterial enzyme, in a eukaryote, Dictyostelium discoideum, with a role in cytokinesis</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Polyphosphate kinase 1 (PPK1), the principal enzyme responsible for reversible synthesis of polyphosphate (poly P) from the terminal phosphate of ATP, is highly conserved in bacteria and archaea. Dictyostelium discoideum, a social slime mold, is one of a few eukaryotes known to possess a PPK1 homolog (DdPPK1). Compared with PPK1 of Escherichia coli, DdPPK1 contains the conserved residues for ATP binding and autophosphorylation, but has an N-terminal extension of 370 aa, lacking homology with any known protein. Polyphosphate or ATP promote oligomerization of the enzyme in vitro. The DdPPK1 products are heterogeneous in chain length and shorter than those of E. coli. The unique DdPPK1 N-terminal domain was shown to be necessary for its enzymatic activity, cellular localization, and physiological functions. Mutants of DdPPK1, as previously reported, are defective in development, sporulation, and predation, and as shown here, in late stages of cytokinesis and cell division.</description><subject>Adenosine triphosphatase</subject><subject>Adenosine Triphosphate - chemistry</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Archaea</subject><subject>Biological Sciences</subject><subject>Cell division</subject><subject>Cell growth</subject><subject>Cells</subject><subject>Cytokinesis</subject><subject>Cytokinesis - genetics</subject><subject>Daughter cells</subject><subject>Dictyostelium - enzymology</subject><subject>Dictyostelium discoideum</subject><subject>E coli</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Escherichia coli Proteins - genetics</subject><subject>Eukaryotes</subject><subject>Eukaryotic cells</subject><subject>Green Fluorescent Proteins - analysis</subject><subject>Green Fluorescent Proteins - genetics</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Phosphates</subject><subject>Phosphotransferases (Alcohol Group Acceptor) - chemistry</subject><subject>Phosphotransferases (Alcohol Group Acceptor) - genetics</subject><subject>Phosphotransferases (Phosphate Group Acceptor) - chemistry</subject><subject>Phosphotransferases (Phosphate Group Acceptor) - genetics</subject><subject>Phosphotransferases (Phosphate Group Acceptor) - metabolism</subject><subject>Polyphosphates</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Protozoan Proteins - chemistry</subject><subject>Protozoan Proteins - genetics</subject><subject>Protozoan Proteins - metabolism</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1v1DAQxSMEokvhzAmIOCAh7bbjr3V8QULlU6oEEvRsOc6k620Sb22nsP3rcbSrLnDpyRrNb57nzSuK5wROCEh2uhlMPAEJy4pLAvxBMSOgyGLJFTwsZgBULipO-VHxJMY1AChRwePiiEjFATifFbfffbfdrHzcrEzC8splQSzJvDSl9UPEcINNWRubMDjTlTjcbnucl27IAI5XJmx9yvUHZ9PWx4SdG_uycdF61-DYz8tfLq0yG3yH05TdJp8_weji0-JRa7qIz_bvcXHx6ePPsy-L82-fv569P19YIXhaKEmVbJmwTYuqUYyRuraUNiDrllJpKlIpK4jlFjmXlFd1U0siWkDKlRGEHRfvdrqbse6xsTikYDq9Ca7P62tvnP63M7iVvvQ3mgLjVLAs8GYvEPz1iDHpPhvErjMD-jHqfHwQjKt7QTrlJNSk-Po_cO3HMOQrZIZwBlzJDJ3uIBt8jAHbu5UJ6Cl9PaWvD-nniZd_Oz3w-7gzUO6BafIgxzWnmix5tczI23sQ3Y5dl_B3yuyLHbuOyYc7mAouAOR0j1e7fmu8NpfBRX3xIxtkABWRFVuyP4zM2BI</recordid><startdate>20071016</startdate><enddate>20071016</enddate><creator>Zhang, Haiyu</creator><creator>Gómez-García, María R</creator><creator>Shi, Xiaobing</creator><creator>Rao, Narayana N</creator><creator>Kornberg, Arthur</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><scope>FBQ</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7T7</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20071016</creationdate><title>Polyphosphate kinase 1, a conserved bacterial enzyme, in a eukaryote, Dictyostelium discoideum, with a role in cytokinesis</title><author>Zhang, Haiyu ; Gómez-García, María R ; Shi, Xiaobing ; Rao, Narayana N ; Kornberg, Arthur</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c554t-97297f35cdfe9d9331bbc22d07bf227a8189c51c4ce447248bdb715f0e249a513</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Adenosine triphosphatase</topic><topic>Adenosine Triphosphate - chemistry</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Archaea</topic><topic>Biological Sciences</topic><topic>Cell division</topic><topic>Cell growth</topic><topic>Cells</topic><topic>Cytokinesis</topic><topic>Cytokinesis - genetics</topic><topic>Daughter cells</topic><topic>Dictyostelium - enzymology</topic><topic>Dictyostelium discoideum</topic><topic>E coli</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Escherichia coli Proteins - genetics</topic><topic>Eukaryotes</topic><topic>Eukaryotic cells</topic><topic>Green Fluorescent Proteins - analysis</topic><topic>Green Fluorescent Proteins - genetics</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Phosphates</topic><topic>Phosphotransferases (Alcohol Group Acceptor) - chemistry</topic><topic>Phosphotransferases (Alcohol Group Acceptor) - genetics</topic><topic>Phosphotransferases (Phosphate Group Acceptor) - chemistry</topic><topic>Phosphotransferases (Phosphate Group Acceptor) - genetics</topic><topic>Phosphotransferases (Phosphate Group Acceptor) - metabolism</topic><topic>Polyphosphates</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins</topic><topic>Protozoan Proteins - chemistry</topic><topic>Protozoan Proteins - genetics</topic><topic>Protozoan Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Haiyu</creatorcontrib><creatorcontrib>Gómez-García, María R</creatorcontrib><creatorcontrib>Shi, Xiaobing</creatorcontrib><creatorcontrib>Rao, Narayana N</creatorcontrib><creatorcontrib>Kornberg, Arthur</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, Haiyu</au><au>Gómez-García, María R</au><au>Shi, Xiaobing</au><au>Rao, Narayana N</au><au>Kornberg, Arthur</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Polyphosphate kinase 1, a conserved bacterial enzyme, in a eukaryote, Dictyostelium discoideum, with a role in cytokinesis</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2007-10-16</date><risdate>2007</risdate><volume>104</volume><issue>42</issue><spage>16486</spage><epage>16491</epage><pages>16486-16491</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Polyphosphate kinase 1 (PPK1), the principal enzyme responsible for reversible synthesis of polyphosphate (poly P) from the terminal phosphate of ATP, is highly conserved in bacteria and archaea. Dictyostelium discoideum, a social slime mold, is one of a few eukaryotes known to possess a PPK1 homolog (DdPPK1). Compared with PPK1 of Escherichia coli, DdPPK1 contains the conserved residues for ATP binding and autophosphorylation, but has an N-terminal extension of 370 aa, lacking homology with any known protein. Polyphosphate or ATP promote oligomerization of the enzyme in vitro. The DdPPK1 products are heterogeneous in chain length and shorter than those of E. coli. The unique DdPPK1 N-terminal domain was shown to be necessary for its enzymatic activity, cellular localization, and physiological functions. Mutants of DdPPK1, as previously reported, are defective in development, sporulation, and predation, and as shown here, in late stages of cytokinesis and cell division.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>17940044</pmid><doi>10.1073/pnas.0706847104</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adenosine triphosphatase Adenosine Triphosphate - chemistry Amino Acid Sequence Animals Antibodies Archaea Biological Sciences Cell division Cell growth Cells Cytokinesis Cytokinesis - genetics Daughter cells Dictyostelium - enzymology Dictyostelium discoideum E coli Enzymes Escherichia coli Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Eukaryotes Eukaryotic cells Green Fluorescent Proteins - analysis Green Fluorescent Proteins - genetics Molecular Sequence Data Mutation Phosphates Phosphotransferases (Alcohol Group Acceptor) - chemistry Phosphotransferases (Alcohol Group Acceptor) - genetics Phosphotransferases (Phosphate Group Acceptor) - chemistry Phosphotransferases (Phosphate Group Acceptor) - genetics Phosphotransferases (Phosphate Group Acceptor) - metabolism Polyphosphates Protein Structure, Tertiary Proteins Protozoan Proteins - chemistry Protozoan Proteins - genetics Protozoan Proteins - metabolism |
| title | Polyphosphate kinase 1, a conserved bacterial enzyme, in a eukaryote, Dictyostelium discoideum, with a role in cytokinesis |
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