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A Drosophila gene that encodes a member of the protein disulfide isomerase/phospholipase C-α family
Screening of a Drosophila genomic DNA library at reduced stringency hybridization conditions using a rat PLCα cDNA probe yielded a gene which encodes a member of the protein disulfide isomerase/PLCα family. The gene has been localized to band 74C on the left arm of the third chromosome and has been...
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| Published in: | Insect biochemistry and molecular biology 1995-05, Vol.25 (5), p.647-654 |
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| Main Authors: | , , |
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| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c388t-7b33f96335182fae3c732bb5aebea7bb7a8bc3718ec1558cac41680643b5c2803 |
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| cites | cdi_FETCH-LOGICAL-c388t-7b33f96335182fae3c732bb5aebea7bb7a8bc3718ec1558cac41680643b5c2803 |
| container_end_page | 654 |
| container_issue | 5 |
| container_start_page | 647 |
| container_title | Insect biochemistry and molecular biology |
| container_volume | 25 |
| creator | McKay, Richard R. Zhu, Liqing Shortridge, Randall D. |
| description | Screening of a
Drosophila genomic DNA library at reduced stringency hybridization conditions using a rat PLCα cDNA probe yielded a gene which encodes a member of the protein disulfide isomerase/PLCα family. The gene has been localized to band 74C on the left arm of the third chromosome and has been designated
dpdi. Northern analysis shows that the
dpdi gene encodes a transcript that is 2.3 kb in length and is present throughout development as well as in both heads and bodies of adults. The deduced
dpdi protein is 496 amino acids in length and contains two domains exhibiting high similarity to thioredoxin, two regions that are similar to the hormone binding domain of human estrogen receptor, and a sequence of four amino acids (KDEL) at the C-terminus which has been described by others as being responsible for retention of proteins in the endoplasmic reticulum. Overall,
dpdi contains a higher similarity to rat protein disulfide isomerase (53% identical) than to rat PLCα (30% identical). However, it is unclear whether
dpdi functions
in vivo as a PDI or as a PLC, or both.
Drosophila with its well characterized genetics and the ability to generate mutants in a gene that has been cloned, provides an excellent system in which to resolve this issue. |
| doi_str_mv | 10.1016/0965-1748(95)00001-C |
| format | article |
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Drosophila genomic DNA library at reduced stringency hybridization conditions using a rat PLCα cDNA probe yielded a gene which encodes a member of the protein disulfide isomerase/PLCα family. The gene has been localized to band 74C on the left arm of the third chromosome and has been designated
dpdi. Northern analysis shows that the
dpdi gene encodes a transcript that is 2.3 kb in length and is present throughout development as well as in both heads and bodies of adults. The deduced
dpdi protein is 496 amino acids in length and contains two domains exhibiting high similarity to thioredoxin, two regions that are similar to the hormone binding domain of human estrogen receptor, and a sequence of four amino acids (KDEL) at the C-terminus which has been described by others as being responsible for retention of proteins in the endoplasmic reticulum. Overall,
dpdi contains a higher similarity to rat protein disulfide isomerase (53% identical) than to rat PLCα (30% identical). However, it is unclear whether
dpdi functions
in vivo as a PDI or as a PLC, or both.
Drosophila with its well characterized genetics and the ability to generate mutants in a gene that has been cloned, provides an excellent system in which to resolve this issue.</description><identifier>ISSN: 0965-1748</identifier><identifier>EISSN: 1879-0240</identifier><identifier>DOI: 10.1016/0965-1748(95)00001-C</identifier><identifier>PMID: 7787847</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Northern ; Cloning, Molecular ; Diptera ; DNA ; Drosophila ; Drosophila - enzymology ; Drosophila - genetics ; Drosophilidae ; Isomerases - genetics ; Molecular Sequence Data ; Phospholipase C ; Protein disulfide isomerase ; Protein Disulfide-Isomerases ; Rats ; Restriction Mapping ; RNA, Messenger - analysis ; Sequence Homology, Amino Acid ; Type C Phospholipases - genetics</subject><ispartof>Insect biochemistry and molecular biology, 1995-05, Vol.25 (5), p.647-654</ispartof><rights>1995</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c388t-7b33f96335182fae3c732bb5aebea7bb7a8bc3718ec1558cac41680643b5c2803</citedby><cites>FETCH-LOGICAL-c388t-7b33f96335182fae3c732bb5aebea7bb7a8bc3718ec1558cac41680643b5c2803</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7787847$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>McKay, Richard R.</creatorcontrib><creatorcontrib>Zhu, Liqing</creatorcontrib><creatorcontrib>Shortridge, Randall D.</creatorcontrib><title>A Drosophila gene that encodes a member of the protein disulfide isomerase/phospholipase C-α family</title><title>Insect biochemistry and molecular biology</title><addtitle>Insect Biochem Mol Biol</addtitle><description>Screening of a
Drosophila genomic DNA library at reduced stringency hybridization conditions using a rat PLCα cDNA probe yielded a gene which encodes a member of the protein disulfide isomerase/PLCα family. The gene has been localized to band 74C on the left arm of the third chromosome and has been designated
dpdi. Northern analysis shows that the
dpdi gene encodes a transcript that is 2.3 kb in length and is present throughout development as well as in both heads and bodies of adults. The deduced
dpdi protein is 496 amino acids in length and contains two domains exhibiting high similarity to thioredoxin, two regions that are similar to the hormone binding domain of human estrogen receptor, and a sequence of four amino acids (KDEL) at the C-terminus which has been described by others as being responsible for retention of proteins in the endoplasmic reticulum. Overall,
dpdi contains a higher similarity to rat protein disulfide isomerase (53% identical) than to rat PLCα (30% identical). However, it is unclear whether
dpdi functions
in vivo as a PDI or as a PLC, or both.
Drosophila with its well characterized genetics and the ability to generate mutants in a gene that has been cloned, provides an excellent system in which to resolve this issue.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Blotting, Northern</subject><subject>Cloning, Molecular</subject><subject>Diptera</subject><subject>DNA</subject><subject>Drosophila</subject><subject>Drosophila - enzymology</subject><subject>Drosophila - genetics</subject><subject>Drosophilidae</subject><subject>Isomerases - genetics</subject><subject>Molecular Sequence Data</subject><subject>Phospholipase C</subject><subject>Protein disulfide isomerase</subject><subject>Protein Disulfide-Isomerases</subject><subject>Rats</subject><subject>Restriction Mapping</subject><subject>RNA, Messenger - analysis</subject><subject>Sequence Homology, Amino Acid</subject><subject>Type C Phospholipases - genetics</subject><issn>0965-1748</issn><issn>1879-0240</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><recordid>eNqFkc1KxDAUhYMoOv68gUJWootqMkmadCNI_QXBja5Dkt46kXZSk47gY_kiPpMZZ3CpgUsI59yTy3cROqTkjBJanpOqFAWVXJ1U4pTkQ4t6A02oklVBppxsosmvZQftpvSaPZwLuY22pVRScTlBzSW-iiGFYeY7g19gDnicmRHD3IUGEja4h95CxKHNAuAhhhH8HDc-LbrWN4B9Cj1Ek-B8mIWUq_NDfuG6-PrErel997GPtlrTJThY33vo-eb6qb4rHh5v7-vLh8IxpcZCWsbaqmRMUDVtDTAn2dRaYcCCkdZKo6xjkipwVAjljOO0VKTkzAo3VYTtoeNVbp7ybQFp1L1PDrrOzCEskpaScSIq_q8xx1IiJc1GvjK6DClFaPUQfW_ih6ZEL7egl4j1ErGuhP7Zgq5z29E6f2F7aH6b1tizfrHSIdN49xB1cj4jh8ZHcKNugv_7g28sEpem</recordid><startdate>19950501</startdate><enddate>19950501</enddate><creator>McKay, Richard R.</creator><creator>Zhu, Liqing</creator><creator>Shortridge, Randall D.</creator><general>Elsevier Ltd</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>7SS</scope><scope>7X8</scope></search><sort><creationdate>19950501</creationdate><title>A Drosophila gene that encodes a member of the protein disulfide isomerase/phospholipase C-α family</title><author>McKay, Richard R. ; Zhu, Liqing ; Shortridge, Randall D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c388t-7b33f96335182fae3c732bb5aebea7bb7a8bc3718ec1558cac41680643b5c2803</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Blotting, Northern</topic><topic>Cloning, Molecular</topic><topic>Diptera</topic><topic>DNA</topic><topic>Drosophila</topic><topic>Drosophila - enzymology</topic><topic>Drosophila - genetics</topic><topic>Drosophilidae</topic><topic>Isomerases - genetics</topic><topic>Molecular Sequence Data</topic><topic>Phospholipase C</topic><topic>Protein disulfide isomerase</topic><topic>Protein Disulfide-Isomerases</topic><topic>Rats</topic><topic>Restriction Mapping</topic><topic>RNA, Messenger - analysis</topic><topic>Sequence Homology, Amino Acid</topic><topic>Type C Phospholipases - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>McKay, Richard R.</creatorcontrib><creatorcontrib>Zhu, Liqing</creatorcontrib><creatorcontrib>Shortridge, Randall D.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Entomology Abstracts (Full archive)</collection><collection>MEDLINE - Academic</collection><jtitle>Insect biochemistry and molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>McKay, Richard R.</au><au>Zhu, Liqing</au><au>Shortridge, Randall D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Drosophila gene that encodes a member of the protein disulfide isomerase/phospholipase C-α family</atitle><jtitle>Insect biochemistry and molecular biology</jtitle><addtitle>Insect Biochem Mol Biol</addtitle><date>1995-05-01</date><risdate>1995</risdate><volume>25</volume><issue>5</issue><spage>647</spage><epage>654</epage><pages>647-654</pages><issn>0965-1748</issn><eissn>1879-0240</eissn><abstract>Screening of a
Drosophila genomic DNA library at reduced stringency hybridization conditions using a rat PLCα cDNA probe yielded a gene which encodes a member of the protein disulfide isomerase/PLCα family. The gene has been localized to band 74C on the left arm of the third chromosome and has been designated
dpdi. Northern analysis shows that the
dpdi gene encodes a transcript that is 2.3 kb in length and is present throughout development as well as in both heads and bodies of adults. The deduced
dpdi protein is 496 amino acids in length and contains two domains exhibiting high similarity to thioredoxin, two regions that are similar to the hormone binding domain of human estrogen receptor, and a sequence of four amino acids (KDEL) at the C-terminus which has been described by others as being responsible for retention of proteins in the endoplasmic reticulum. Overall,
dpdi contains a higher similarity to rat protein disulfide isomerase (53% identical) than to rat PLCα (30% identical). However, it is unclear whether
dpdi functions
in vivo as a PDI or as a PLC, or both.
Drosophila with its well characterized genetics and the ability to generate mutants in a gene that has been cloned, provides an excellent system in which to resolve this issue.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>7787847</pmid><doi>10.1016/0965-1748(95)00001-C</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0965-1748 |
| ispartof | Insect biochemistry and molecular biology, 1995-05, Vol.25 (5), p.647-654 |
| issn | 0965-1748 1879-0240 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77340594 |
| source | ScienceDirect Journals |
| subjects | Amino Acid Sequence Animals Base Sequence Blotting, Northern Cloning, Molecular Diptera DNA Drosophila Drosophila - enzymology Drosophila - genetics Drosophilidae Isomerases - genetics Molecular Sequence Data Phospholipase C Protein disulfide isomerase Protein Disulfide-Isomerases Rats Restriction Mapping RNA, Messenger - analysis Sequence Homology, Amino Acid Type C Phospholipases - genetics |
| title | A Drosophila gene that encodes a member of the protein disulfide isomerase/phospholipase C-α family |
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