Genetic Evidence for the Expression of ATP- and GTP-specific Succinyl-CoA Synthetases in Multicellular Eucaryotes
Highly ATP- and GTP-specific isoforms of succinyl-CoA synthetase in pigeon incorporate the same α-subunit, but different β-subunits (Johnson, J. D., Muhonen, W. W., and Lambeth, D. O. (1998) J. Biol. Chem. 273, 27573–27579). The sequences of the mature subunits were determined by methods based on re...
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| Veröffentlicht in: | The Journal of biological chemistry 1998-10, Vol.273 (42), p.27580-27586 |
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| creator | Johnson, James D. Mehus, James G. Tews, Kristin Milavetz, Barry I. Lambeth, David O. |
| description | Highly ATP- and GTP-specific isoforms of succinyl-CoA synthetase in pigeon incorporate the same α-subunit, but different β-subunits (Johnson, J. D., Muhonen, W. W., and Lambeth, D. O. (1998) J. Biol. Chem. 273, 27573–27579). The sequences of the mature subunits were determined by methods based on reverse transcription-polymerase chain reaction. The 306-residue mature α-subunit in pigeon shows >88% identity to its homologues in pig and rat. The sequences of the mature ATP- and GTP-specific β-subunits (A-β and G-β, respectively) in pigeon are 54% identical. These sequences were used to identify expressed sequence tags for human and mouse that were highly homologous to G-β and A-β, respectively. The sequences for mature A-β and G-β in mouse and human were completed and verified by polymerase chain reaction. The sequence of A-β in pig was also obtained. The mammalian A-β sequences show >89% identity to each other; the G-β sequences are similarly related. However, pairwise comparisons of the A-β and G-β sequences revealed |
| doi_str_mv | 10.1074/jbc.273.42.27580 |
| format | Article |
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D., Muhonen, W. W., and Lambeth, D. O. (1998) J. Biol. Chem. 273, 27573–27579). The sequences of the mature subunits were determined by methods based on reverse transcription-polymerase chain reaction. The 306-residue mature α-subunit in pigeon shows >88% identity to its homologues in pig and rat. The sequences of the mature ATP- and GTP-specific β-subunits (A-β and G-β, respectively) in pigeon are 54% identical. These sequences were used to identify expressed sequence tags for human and mouse that were highly homologous to G-β and A-β, respectively. The sequences for mature A-β and G-β in mouse and human were completed and verified by polymerase chain reaction. The sequence of A-β in pig was also obtained. The mammalian A-β sequences show >89% identity to each other; the G-β sequences are similarly related. However, pairwise comparisons of the A-β and G-β sequences revealed <53% identity. Alignment with two sequences of the β-subunit in Caenorhabditis elegans suggests that the A-β and G-β genes arose by duplication early in the evolution of multicellular eucaryotes. The expression of A-β is strong in numerous mouse and human tissues, which suggests that ATP-specific succinyl-CoA synthetase also plays an important role in species throughout the animal kingdom.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.273.42.27580</identifier><identifier>PMID: 9765291</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Cloning, Molecular ; Columbidae ; Eukaryotic Cells - enzymology ; Evolution, Molecular ; Expressed Sequence Tags ; Humans ; Mice ; Molecular Sequence Data ; Phylogeny ; Protein Conformation ; Sequence Analysis, DNA ; Sequence Homology, Amino Acid ; Species Specificity ; Succinate-CoA Ligases - classification ; Succinate-CoA Ligases - genetics ; Swine ; Tissue Distribution</subject><ispartof>The Journal of biological chemistry, 1998-10, Vol.273 (42), p.27580-27586</ispartof><rights>1998 © 1998 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c513t-5a37fda8336abda067b6f794abcbd4550ad8dc6d703807720b6e309797dc79703</citedby><cites>FETCH-LOGICAL-c513t-5a37fda8336abda067b6f794abcbd4550ad8dc6d703807720b6e309797dc79703</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782,27907,27908</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9765291$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Johnson, James D.</creatorcontrib><creatorcontrib>Mehus, James G.</creatorcontrib><creatorcontrib>Tews, Kristin</creatorcontrib><creatorcontrib>Milavetz, Barry I.</creatorcontrib><creatorcontrib>Lambeth, David O.</creatorcontrib><title>Genetic Evidence for the Expression of ATP- and GTP-specific Succinyl-CoA Synthetases in Multicellular Eucaryotes</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Highly ATP- and GTP-specific isoforms of succinyl-CoA synthetase in pigeon incorporate the same α-subunit, but different β-subunits (Johnson, J. D., Muhonen, W. W., and Lambeth, D. O. (1998) J. Biol. Chem. 273, 27573–27579). The sequences of the mature subunits were determined by methods based on reverse transcription-polymerase chain reaction. The 306-residue mature α-subunit in pigeon shows >88% identity to its homologues in pig and rat. The sequences of the mature ATP- and GTP-specific β-subunits (A-β and G-β, respectively) in pigeon are 54% identical. These sequences were used to identify expressed sequence tags for human and mouse that were highly homologous to G-β and A-β, respectively. The sequences for mature A-β and G-β in mouse and human were completed and verified by polymerase chain reaction. The sequence of A-β in pig was also obtained. The mammalian A-β sequences show >89% identity to each other; the G-β sequences are similarly related. However, pairwise comparisons of the A-β and G-β sequences revealed <53% identity. Alignment with two sequences of the β-subunit in Caenorhabditis elegans suggests that the A-β and G-β genes arose by duplication early in the evolution of multicellular eucaryotes. The expression of A-β is strong in numerous mouse and human tissues, which suggests that ATP-specific succinyl-CoA synthetase also plays an important role in species throughout the animal kingdom.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Cloning, Molecular</subject><subject>Columbidae</subject><subject>Eukaryotic Cells - enzymology</subject><subject>Evolution, Molecular</subject><subject>Expressed Sequence Tags</subject><subject>Humans</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Phylogeny</subject><subject>Protein Conformation</subject><subject>Sequence Analysis, DNA</subject><subject>Sequence Homology, Amino Acid</subject><subject>Species Specificity</subject><subject>Succinate-CoA Ligases - classification</subject><subject>Succinate-CoA Ligases - genetics</subject><subject>Swine</subject><subject>Tissue Distribution</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kc9r2zAUx0VZ6dIf910GOozenD5ZlmXvFkKWDVpaaAu9CVl6XlQcK5Xsbvnvqyyhh0F10BO87_fLl48I-cJgykAWV8-NmeaST4s8DVHBEZkwqHjGBXv6RCYAOcvqXFSfyWmMz5BOUbMTclLLUuQ1m5CXJfY4OEMXr85ib5C2PtBhhXTxdxMwRud76ls6e7jLqO4tXaZH3KBxbTLdj8a4fttlcz-j99s--QYdMVLX05uxS7nYdWOnA12MRoetHzCek-NWdxEvDvOMPP5YPMx_Zte3y1_z2XVmBONDJjSXrdUV56VurIZSNmUr60I3prGFEKBtZU1pJfAKpMyhKZFDLWtpTbqAn5HLfe4m-JcR46DWLu766B79GBWTUAvOdkLYC03wMQZs1Sa4dWqrGKgdZZUoq0RZFbn6RzlZvh6yx2aN9t1wwJr23_b7lfu9-uMCqsZ5s8L1_zHf9zJMHF4dBhWN232CTRYzKOvdxx3eAEwcmBk</recordid><startdate>19981016</startdate><enddate>19981016</enddate><creator>Johnson, James D.</creator><creator>Mehus, James G.</creator><creator>Tews, Kristin</creator><creator>Milavetz, Barry I.</creator><creator>Lambeth, David O.</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>7TM</scope></search><sort><creationdate>19981016</creationdate><title>Genetic Evidence for the Expression of ATP- and GTP-specific Succinyl-CoA Synthetases in Multicellular Eucaryotes</title><author>Johnson, James D. ; Mehus, James G. ; Tews, Kristin ; Milavetz, Barry I. ; Lambeth, David O.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c513t-5a37fda8336abda067b6f794abcbd4550ad8dc6d703807720b6e309797dc79703</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Cloning, Molecular</topic><topic>Columbidae</topic><topic>Eukaryotic Cells - enzymology</topic><topic>Evolution, Molecular</topic><topic>Expressed Sequence Tags</topic><topic>Humans</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Phylogeny</topic><topic>Protein Conformation</topic><topic>Sequence Analysis, DNA</topic><topic>Sequence Homology, Amino Acid</topic><topic>Species Specificity</topic><topic>Succinate-CoA Ligases - classification</topic><topic>Succinate-CoA Ligases - genetics</topic><topic>Swine</topic><topic>Tissue Distribution</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Johnson, James D.</creatorcontrib><creatorcontrib>Mehus, James G.</creatorcontrib><creatorcontrib>Tews, Kristin</creatorcontrib><creatorcontrib>Milavetz, Barry I.</creatorcontrib><creatorcontrib>Lambeth, David O.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Johnson, James D.</au><au>Mehus, James G.</au><au>Tews, Kristin</au><au>Milavetz, Barry I.</au><au>Lambeth, David O.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Genetic Evidence for the Expression of ATP- and GTP-specific Succinyl-CoA Synthetases in Multicellular Eucaryotes</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1998-10-16</date><risdate>1998</risdate><volume>273</volume><issue>42</issue><spage>27580</spage><epage>27586</epage><pages>27580-27586</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Highly ATP- and GTP-specific isoforms of succinyl-CoA synthetase in pigeon incorporate the same α-subunit, but different β-subunits (Johnson, J. D., Muhonen, W. W., and Lambeth, D. O. (1998) J. Biol. Chem. 273, 27573–27579). The sequences of the mature subunits were determined by methods based on reverse transcription-polymerase chain reaction. The 306-residue mature α-subunit in pigeon shows >88% identity to its homologues in pig and rat. The sequences of the mature ATP- and GTP-specific β-subunits (A-β and G-β, respectively) in pigeon are 54% identical. These sequences were used to identify expressed sequence tags for human and mouse that were highly homologous to G-β and A-β, respectively. The sequences for mature A-β and G-β in mouse and human were completed and verified by polymerase chain reaction. The sequence of A-β in pig was also obtained. The mammalian A-β sequences show >89% identity to each other; the G-β sequences are similarly related. However, pairwise comparisons of the A-β and G-β sequences revealed <53% identity. Alignment with two sequences of the β-subunit in Caenorhabditis elegans suggests that the A-β and G-β genes arose by duplication early in the evolution of multicellular eucaryotes. The expression of A-β is strong in numerous mouse and human tissues, which suggests that ATP-specific succinyl-CoA synthetase also plays an important role in species throughout the animal kingdom.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>9765291</pmid><doi>10.1074/jbc.273.42.27580</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Cloning, Molecular Columbidae Eukaryotic Cells - enzymology Evolution, Molecular Expressed Sequence Tags Humans Mice Molecular Sequence Data Phylogeny Protein Conformation Sequence Analysis, DNA Sequence Homology, Amino Acid Species Specificity Succinate-CoA Ligases - classification Succinate-CoA Ligases - genetics Swine Tissue Distribution |
| title | Genetic Evidence for the Expression of ATP- and GTP-specific Succinyl-CoA Synthetases in Multicellular Eucaryotes |
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