Gene Cloning and Characterization of CDP-diacylglycerol Synthase from Rat Brain
A cDNA encoded a 462-amino acid protein, which showed CDP-diacylglycerol synthase (CDS) activity was cloned for the first time as the vertebrate enzyme molecule from rat brain cDNA library. The deduced molecular mass of this rat CDS was 53 kDa, and putative primary structure included several possibl...
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| Veröffentlicht in: | The Journal of biological chemistry 1997-04, Vol.272 (14), p.9503-9509 |
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| creator | Saito, S Goto, K Tonosaki, A Kondo, H |
| description | A cDNA encoded a 462-amino acid protein, which showed CDP-diacylglycerol synthase (CDS) activity was cloned for the first
time as the vertebrate enzyme molecule from rat brain cDNA library. The deduced molecular mass of this rat CDS was 53 kDa,
and putative primary structure included several possible membrane- spanning regions. At the amino acid sequence level, rat
CDS shared 55.5%, 31.7%, and 20.9% identity with already known Drosophila , Saccharomyces cerevisiae , and Escherichia coli CDS, respectively. This rat CDS preferred 1-stearoyl-2-arachidonoyl phosphatidic acid as a substrate, and its activity was
strongly inhibited by phosphatidylglycerol 4,5-bisphosphate. By immunoblotting analysis of COS cells overexpressed with the
epitope-tagged for rat CDS, a 60-kDa band was detected. By epitope-tag immunocytochemistry, the CDS protein was mainly localized
in close association with the membrane of the endoplasmic reticulum of the transfected cells. The intense mRNA expression
of CDS was localized in the cerebellar Purkinje cells, the pineal body, and the inner segment of photoreceptor cells. Additionally,
very intense expression was detected in postmitotic spermatocytes and spermatids. |
| doi_str_mv | 10.1074/jbc.272.14.9503 |
| format | Article |
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time as the vertebrate enzyme molecule from rat brain cDNA library. The deduced molecular mass of this rat CDS was 53 kDa,
and putative primary structure included several possible membrane- spanning regions. At the amino acid sequence level, rat
CDS shared 55.5%, 31.7%, and 20.9% identity with already known Drosophila , Saccharomyces cerevisiae , and Escherichia coli CDS, respectively. This rat CDS preferred 1-stearoyl-2-arachidonoyl phosphatidic acid as a substrate, and its activity was
strongly inhibited by phosphatidylglycerol 4,5-bisphosphate. By immunoblotting analysis of COS cells overexpressed with the
epitope-tagged for rat CDS, a 60-kDa band was detected. By epitope-tag immunocytochemistry, the CDS protein was mainly localized
in close association with the membrane of the endoplasmic reticulum of the transfected cells. The intense mRNA expression
of CDS was localized in the cerebellar Purkinje cells, the pineal body, and the inner segment of photoreceptor cells. Additionally,
very intense expression was detected in postmitotic spermatocytes and spermatids.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.272.14.9503</identifier><identifier>PMID: 9083091</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Brain - enzymology ; COS Cells ; Diacylglycerol Cholinephosphotransferase - chemistry ; Diacylglycerol Cholinephosphotransferase - genetics ; In Situ Hybridization ; Male ; Molecular Sequence Data ; Phosphatidylinositol 4,5-Diphosphate - metabolism ; Rats ; Rats, Wistar ; Retina - enzymology ; RNA, Messenger - metabolism ; Testis - enzymology</subject><ispartof>The Journal of biological chemistry, 1997-04, Vol.272 (14), p.9503-9509</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c458t-e3d34b1211ef224c96ef2b57ebd435fc76712555e2278299752da8a81e2d25ef3</citedby><cites>FETCH-LOGICAL-c458t-e3d34b1211ef224c96ef2b57ebd435fc76712555e2278299752da8a81e2d25ef3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9083091$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Saito, S</creatorcontrib><creatorcontrib>Goto, K</creatorcontrib><creatorcontrib>Tonosaki, A</creatorcontrib><creatorcontrib>Kondo, H</creatorcontrib><title>Gene Cloning and Characterization of CDP-diacylglycerol Synthase from Rat Brain</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>A cDNA encoded a 462-amino acid protein, which showed CDP-diacylglycerol synthase (CDS) activity was cloned for the first
time as the vertebrate enzyme molecule from rat brain cDNA library. The deduced molecular mass of this rat CDS was 53 kDa,
and putative primary structure included several possible membrane- spanning regions. At the amino acid sequence level, rat
CDS shared 55.5%, 31.7%, and 20.9% identity with already known Drosophila , Saccharomyces cerevisiae , and Escherichia coli CDS, respectively. This rat CDS preferred 1-stearoyl-2-arachidonoyl phosphatidic acid as a substrate, and its activity was
strongly inhibited by phosphatidylglycerol 4,5-bisphosphate. By immunoblotting analysis of COS cells overexpressed with the
epitope-tagged for rat CDS, a 60-kDa band was detected. By epitope-tag immunocytochemistry, the CDS protein was mainly localized
in close association with the membrane of the endoplasmic reticulum of the transfected cells. The intense mRNA expression
of CDS was localized in the cerebellar Purkinje cells, the pineal body, and the inner segment of photoreceptor cells. Additionally,
very intense expression was detected in postmitotic spermatocytes and spermatids.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Brain - enzymology</subject><subject>COS Cells</subject><subject>Diacylglycerol Cholinephosphotransferase - chemistry</subject><subject>Diacylglycerol Cholinephosphotransferase - genetics</subject><subject>In Situ Hybridization</subject><subject>Male</subject><subject>Molecular Sequence Data</subject><subject>Phosphatidylinositol 4,5-Diphosphate - metabolism</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Retina - enzymology</subject><subject>RNA, Messenger - metabolism</subject><subject>Testis - enzymology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMFr2zAUxsXoaNNu550KgsJuTvRkKbKOm7umhUDH1sJuQpafYxXbyiSHkv31dUkY9NR3-Q7f732HHyFfgM2BKbF4qtycKz4HMdeS5R_IDFiRZ7mEPydkxhiHTHNZnJHzlJ7YdELDKTnVE8Q0zMj9CgekZRcGP2yoHWpatjZaN2L0_-zow0BDQ8vrn1ntrdt3m27vMIaO_t4PY2sT0iaGnv6yI_0erR8-kY-N7RJ-PuYFebz58VDeZuv71V35bZ05IYsxw7zORQUcABvOhdPLKSupsKpFLhunlgq4lBI5VwXXWkle28IWgLzmEpv8gnw97G5j-LvDNJreJ4ddZwcMu2RUoXkuVPEuCEvGFUg1gYsD6GJIKWJjttH3Nu4NMPPq2kyuzeTagDCvrqePy-P0ruqx_s8f5U791aFv_aZ99hFN5YNrsX-z8gIZTITJ</recordid><startdate>19970404</startdate><enddate>19970404</enddate><creator>Saito, S</creator><creator>Goto, K</creator><creator>Tonosaki, A</creator><creator>Kondo, H</creator><general>American Society for Biochemistry and Molecular Biology</general><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>7TK</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19970404</creationdate><title>Gene Cloning and Characterization of CDP-diacylglycerol Synthase from Rat Brain</title><author>Saito, S ; Goto, K ; Tonosaki, A ; Kondo, H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c458t-e3d34b1211ef224c96ef2b57ebd435fc76712555e2278299752da8a81e2d25ef3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Brain - enzymology</topic><topic>COS Cells</topic><topic>Diacylglycerol Cholinephosphotransferase - chemistry</topic><topic>Diacylglycerol Cholinephosphotransferase - genetics</topic><topic>In Situ Hybridization</topic><topic>Male</topic><topic>Molecular Sequence Data</topic><topic>Phosphatidylinositol 4,5-Diphosphate - metabolism</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Retina - enzymology</topic><topic>RNA, Messenger - metabolism</topic><topic>Testis - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Saito, S</creatorcontrib><creatorcontrib>Goto, K</creatorcontrib><creatorcontrib>Tonosaki, A</creatorcontrib><creatorcontrib>Kondo, H</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Saito, S</au><au>Goto, K</au><au>Tonosaki, A</au><au>Kondo, H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Gene Cloning and Characterization of CDP-diacylglycerol Synthase from Rat Brain</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1997-04-04</date><risdate>1997</risdate><volume>272</volume><issue>14</issue><spage>9503</spage><epage>9509</epage><pages>9503-9509</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>A cDNA encoded a 462-amino acid protein, which showed CDP-diacylglycerol synthase (CDS) activity was cloned for the first
time as the vertebrate enzyme molecule from rat brain cDNA library. The deduced molecular mass of this rat CDS was 53 kDa,
and putative primary structure included several possible membrane- spanning regions. At the amino acid sequence level, rat
CDS shared 55.5%, 31.7%, and 20.9% identity with already known Drosophila , Saccharomyces cerevisiae , and Escherichia coli CDS, respectively. This rat CDS preferred 1-stearoyl-2-arachidonoyl phosphatidic acid as a substrate, and its activity was
strongly inhibited by phosphatidylglycerol 4,5-bisphosphate. By immunoblotting analysis of COS cells overexpressed with the
epitope-tagged for rat CDS, a 60-kDa band was detected. By epitope-tag immunocytochemistry, the CDS protein was mainly localized
in close association with the membrane of the endoplasmic reticulum of the transfected cells. The intense mRNA expression
of CDS was localized in the cerebellar Purkinje cells, the pineal body, and the inner segment of photoreceptor cells. Additionally,
very intense expression was detected in postmitotic spermatocytes and spermatids.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>9083091</pmid><doi>10.1074/jbc.272.14.9503</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1997-04, Vol.272 (14), p.9503-9509 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78923478 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Base Sequence Brain - enzymology COS Cells Diacylglycerol Cholinephosphotransferase - chemistry Diacylglycerol Cholinephosphotransferase - genetics In Situ Hybridization Male Molecular Sequence Data Phosphatidylinositol 4,5-Diphosphate - metabolism Rats Rats, Wistar Retina - enzymology RNA, Messenger - metabolism Testis - enzymology |
| title | Gene Cloning and Characterization of CDP-diacylglycerol Synthase from Rat Brain |
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