Identification and characterization of a lower plant Ypt/Rab guanosine dissociation inhibitor (GDI)
The cDNA encoding a Ypt/Rab guanosine dissociation inhibitor (Ypt-GDI) was isolated from the multicellular green alga Volvox carteri, representing the first complete plant gdi gene described. The gdiV1 gene occurs as a single copy in the algal genome, indicating that its product regulates all YptV p...
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Veröffentlicht in: | FEBS letters 1996-11, Vol.396 (2), p.298-304 |
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description | The cDNA encoding a Ypt/Rab guanosine dissociation inhibitor (Ypt-GDI) was isolated from the multicellular green alga
Volvox carteri, representing the first complete plant
gdi gene described. The
gdiV1 gene occurs as a single copy in the algal genome, indicating that its product regulates all YptV proteins from
Volvox. The derived GDI protein (GDIV1p) shows high similarity to animal and fungal GDIs. A specific antibody developed against GDIV1p detected the protein throughout the whole
Volvox life-cycle. GDIV1p was localized in the cytoplasm and in the algal flagellum. This is in line with earlier findings of a dual localization of Ypt proteins both in the cell body and in the motility organelle, and indicates a novel role of the GDI/Ypt system, possibly in intraflagellar transport. |
doi_str_mv | 10.1016/0014-5793(96)01068-X |
format | Article |
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Volvox carteri, representing the first complete plant
gdi gene described. The
gdiV1 gene occurs as a single copy in the algal genome, indicating that its product regulates all YptV proteins from
Volvox. The derived GDI protein (GDIV1p) shows high similarity to animal and fungal GDIs. A specific antibody developed against GDIV1p detected the protein throughout the whole
Volvox life-cycle. GDIV1p was localized in the cytoplasm and in the algal flagellum. This is in line with earlier findings of a dual localization of Ypt proteins both in the cell body and in the motility organelle, and indicates a novel role of the GDI/Ypt system, possibly in intraflagellar transport.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(96)01068-X</identifier><identifier>PMID: 8915007</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Algal Proteins ; Amino Acid Sequence ; Animals ; Chlamydomonas ; Chlamydomonas reinhardtii - chemistry ; Chlamydomonas reinhardtii - genetics ; Chlorophyta - chemistry ; Chlorophyta - genetics ; Cytosol - chemistry ; DNA, Complementary - genetics ; Flagella - chemistry ; Flagellum ; Genes ; Green alga ; GTP-Binding Proteins - analysis ; GTP-Binding Proteins - chemistry ; GTP-Binding Proteins - genetics ; Guanine Nucleotide Dissociation Inhibitors ; Humans ; Molecular Sequence Data ; Sequence Homology, Amino Acid ; Transport ; Volvox ; Ypt/Rab protein</subject><ispartof>FEBS letters, 1996-11, Vol.396 (2), p.298-304</ispartof><rights>1996</rights><rights>FEBS Letters 396 (1996) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c466X-7d2faaf99dce26f1c4bf2b4b2da42ece93c9303a9845c9d0b3e143c25d0a13ac3</citedby><cites>FETCH-LOGICAL-c466X-7d2faaf99dce26f1c4bf2b4b2da42ece93c9303a9845c9d0b3e143c25d0a13ac3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2F0014-5793%2896%2901068-X$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(96)01068-X$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,1417,3550,27924,27925,45574,45575,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8915007$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Beyser, Kurt</creatorcontrib><creatorcontrib>Fabry, Stefan</creatorcontrib><title>Identification and characterization of a lower plant Ypt/Rab guanosine dissociation inhibitor (GDI)</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>The cDNA encoding a Ypt/Rab guanosine dissociation inhibitor (Ypt-GDI) was isolated from the multicellular green alga
Volvox carteri, representing the first complete plant
gdi gene described. The
gdiV1 gene occurs as a single copy in the algal genome, indicating that its product regulates all YptV proteins from
Volvox. The derived GDI protein (GDIV1p) shows high similarity to animal and fungal GDIs. A specific antibody developed against GDIV1p detected the protein throughout the whole
Volvox life-cycle. GDIV1p was localized in the cytoplasm and in the algal flagellum. This is in line with earlier findings of a dual localization of Ypt proteins both in the cell body and in the motility organelle, and indicates a novel role of the GDI/Ypt system, possibly in intraflagellar transport.</description><subject>Algal Proteins</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Chlamydomonas</subject><subject>Chlamydomonas reinhardtii - chemistry</subject><subject>Chlamydomonas reinhardtii - genetics</subject><subject>Chlorophyta - chemistry</subject><subject>Chlorophyta - genetics</subject><subject>Cytosol - chemistry</subject><subject>DNA, Complementary - genetics</subject><subject>Flagella - chemistry</subject><subject>Flagellum</subject><subject>Genes</subject><subject>Green alga</subject><subject>GTP-Binding Proteins - analysis</subject><subject>GTP-Binding Proteins - chemistry</subject><subject>GTP-Binding Proteins - genetics</subject><subject>Guanine Nucleotide Dissociation Inhibitors</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Sequence Homology, Amino Acid</subject><subject>Transport</subject><subject>Volvox</subject><subject>Ypt/Rab protein</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkM1rFEEQxRtR4hr9DxT6JMlhTH_NR18Ejdm4EBBEYT01PdU1pmR2eu2eNcS_3hlnyVE8NfXeq9fFj7GXUryRQlYXQkhTlLXVZ7Y6F1JUTbF9xFayqXWhTdU8ZquHyFP2LOcfYpobaU_YSWNlKUS9YrAJOIzUEfiR4sD9EDjc-uRhxES_FzF23PM-3mHi-94PI_-2Hy8--5Z_P_ghZhqQB8o5Ai15Gm6ppTEmfnb9YXP-nD3pfJ_xxfE9ZV_XV18uPxY3n643l-9uCjBVtS3qoDrvO2sDoKo6CabtVGtaFbxRCGg1WC20t40pwQbRapRGgyqD8FJ70Kfs9dK7T_HnAfPodpQB--lkjIfs6qZUpRL1FDRLEFLMOWHn9ol2Pt07KdzM1s3g3AzO2WmY2brttPbq2H9odxgelo4wJ3-9-HfU4_1_dbr11Xs1G7Nuq7_q_NHbpQgnWr8Ik8tAOAAGSgijC5H-fekfiYWdug</recordid><startdate>19961104</startdate><enddate>19961104</enddate><creator>Beyser, Kurt</creator><creator>Fabry, Stefan</creator><general>Elsevier B.V</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>7X8</scope></search><sort><creationdate>19961104</creationdate><title>Identification and characterization of a lower plant Ypt/Rab guanosine dissociation inhibitor (GDI)</title><author>Beyser, Kurt ; Fabry, Stefan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c466X-7d2faaf99dce26f1c4bf2b4b2da42ece93c9303a9845c9d0b3e143c25d0a13ac3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Algal Proteins</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Chlamydomonas</topic><topic>Chlamydomonas reinhardtii - chemistry</topic><topic>Chlamydomonas reinhardtii - genetics</topic><topic>Chlorophyta - chemistry</topic><topic>Chlorophyta - genetics</topic><topic>Cytosol - chemistry</topic><topic>DNA, Complementary - genetics</topic><topic>Flagella - chemistry</topic><topic>Flagellum</topic><topic>Genes</topic><topic>Green alga</topic><topic>GTP-Binding Proteins - analysis</topic><topic>GTP-Binding Proteins - chemistry</topic><topic>GTP-Binding Proteins - genetics</topic><topic>Guanine Nucleotide Dissociation Inhibitors</topic><topic>Humans</topic><topic>Molecular Sequence Data</topic><topic>Sequence Homology, Amino Acid</topic><topic>Transport</topic><topic>Volvox</topic><topic>Ypt/Rab protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Beyser, Kurt</creatorcontrib><creatorcontrib>Fabry, Stefan</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>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Beyser, Kurt</au><au>Fabry, Stefan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification and characterization of a lower plant Ypt/Rab guanosine dissociation inhibitor (GDI)</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1996-11-04</date><risdate>1996</risdate><volume>396</volume><issue>2</issue><spage>298</spage><epage>304</epage><pages>298-304</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The cDNA encoding a Ypt/Rab guanosine dissociation inhibitor (Ypt-GDI) was isolated from the multicellular green alga
Volvox carteri, representing the first complete plant
gdi gene described. The
gdiV1 gene occurs as a single copy in the algal genome, indicating that its product regulates all YptV proteins from
Volvox. The derived GDI protein (GDIV1p) shows high similarity to animal and fungal GDIs. A specific antibody developed against GDIV1p detected the protein throughout the whole
Volvox life-cycle. GDIV1p was localized in the cytoplasm and in the algal flagellum. This is in line with earlier findings of a dual localization of Ypt proteins both in the cell body and in the motility organelle, and indicates a novel role of the GDI/Ypt system, possibly in intraflagellar transport.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>8915007</pmid><doi>10.1016/0014-5793(96)01068-X</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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source | Wiley Online Library - AutoHoldings Journals; MEDLINE; Elsevier ScienceDirect Journals Complete; Alma/SFX Local Collection; EZB Electronic Journals Library |
subjects | Algal Proteins Amino Acid Sequence Animals Chlamydomonas Chlamydomonas reinhardtii - chemistry Chlamydomonas reinhardtii - genetics Chlorophyta - chemistry Chlorophyta - genetics Cytosol - chemistry DNA, Complementary - genetics Flagella - chemistry Flagellum Genes Green alga GTP-Binding Proteins - analysis GTP-Binding Proteins - chemistry GTP-Binding Proteins - genetics Guanine Nucleotide Dissociation Inhibitors Humans Molecular Sequence Data Sequence Homology, Amino Acid Transport Volvox Ypt/Rab protein |
title | Identification and characterization of a lower plant Ypt/Rab guanosine dissociation inhibitor (GDI) |
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