Protein geranylgeranyltransferase of Saccharomyces cerevisiae is specific for Cys-Xaa-Xaa-Leu motif proteins and requires the CDC43 gene product but not the DPR1 gene product
Protein prenylation occurs by modification of proteins with one of at least two isoprenoids, the farnesyl group and the geranylgeranyl group. Protein farnesyltransferases have been identified, but no such enzyme has been identified for geranylgeranylation. We report the identification of an activity...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1991-05, Vol.88 (10), p.4448-4452 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Finegold, Alan A. Johnson, Douglas I. Farnsworth, Christopher C. Gelb, Michael H. Judd, S. Renee Glomset, John A. Tamanoi, Fuyuhiko |
| description | Protein prenylation occurs by modification of proteins with one of at least two isoprenoids, the farnesyl group and the geranylgeranyl group. Protein farnesyltransferases have been identified, but no such enzyme has been identified for geranylgeranylation. We report the identification of an activity in crude soluble yeast extracts that catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl pyrophosphate to proteins having the C-terminal sequence Cys-Ile-Ile-Leu or Cys-Val-Leu-Leu but not to a similar protein ending with Cys-Ile-Ile-Ser. This activity is dependent upon the CDC43/CAL1 gene, which is involved in budding and the control of cell polarity, but does not require the DPR1/RAM1 gene, which is known to be required for the farnesylation of Ras proteins. These results indicate that the protein geranylgeranyltransferase activity is distinct from the protein farnesyltransferase activity and that its specificity depends in part on the extreme C-terminal leucine in the protein to be prenylated. |
| doi_str_mv | 10.1073/pnas.88.10.4448 |
| format | Article |
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Renee ; Glomset, John A. ; Tamanoi, Fuyuhiko</creator><creatorcontrib>Finegold, Alan A. ; Johnson, Douglas I. ; Farnsworth, Christopher C. ; Gelb, Michael H. ; Judd, S. Renee ; Glomset, John A. ; Tamanoi, Fuyuhiko ; The University of Chicago, Chicago, IL ; Nebraska-Lincoln Univ. (USA)</creatorcontrib><description>Protein prenylation occurs by modification of proteins with one of at least two isoprenoids, the farnesyl group and the geranylgeranyl group. Protein farnesyltransferases have been identified, but no such enzyme has been identified for geranylgeranylation. We report the identification of an activity in crude soluble yeast extracts that catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl pyrophosphate to proteins having the C-terminal sequence Cys-Ile-Ile-Leu or Cys-Val-Leu-Leu but not to a similar protein ending with Cys-Ile-Ile-Ser. This activity is dependent upon the CDC43/CAL1 gene, which is involved in budding and the control of cell polarity, but does not require the DPR1/RAM1 gene, which is known to be required for the farnesylation of Ras proteins. These results indicate that the protein geranylgeranyltransferase activity is distinct from the protein farnesyltransferase activity and that its specificity depends in part on the extreme C-terminal leucine in the protein to be prenylated.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.88.10.4448</identifier><identifier>PMID: 2034682</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>actividad enzimatica ; activite enzymatique ; Alkyl and Aryl Transferases ; Amino Acid Sequence ; Amino acids ; Base Sequence ; Biochemistry ; Cell Cycle Proteins ; Diphosphates ; enzymic activity ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; genes ; Genes, Fungal ; Genetic mutation ; genetica ; genetics ; genetique ; Molecular Sequence Data ; mutacion ; mutation ; Oligonucleotides ; Plasmids ; Polyisoprenyl Phosphates - metabolism ; protein geranylgeranyltransferase ; proteinas ; proteine ; Proteins ; Pulmonary function tests ; Radioactive decay ; saccharomyces cerevisiae ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae Proteins ; Substrate Specificity ; transferasas ; transferase ; transferases ; Transferases - metabolism ; Yeasts</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1991-05, Vol.88 (10), p.4448-4452</ispartof><rights>Copyright 1991 The National Academy of Sciences of the United States of America</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c516t-19889bbcf7abc2b172f66c761076355c9e2c34aa17c341eec62334f77531ca823</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/88/10.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2357062$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2357062$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27903,27904,53769,53771,57995,58228</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2034682$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Finegold, Alan A.</creatorcontrib><creatorcontrib>Johnson, Douglas I.</creatorcontrib><creatorcontrib>Farnsworth, Christopher C.</creatorcontrib><creatorcontrib>Gelb, Michael H.</creatorcontrib><creatorcontrib>Judd, S. Renee</creatorcontrib><creatorcontrib>Glomset, John A.</creatorcontrib><creatorcontrib>Tamanoi, Fuyuhiko</creatorcontrib><creatorcontrib>The University of Chicago, Chicago, IL</creatorcontrib><creatorcontrib>Nebraska-Lincoln Univ. (USA)</creatorcontrib><title>Protein geranylgeranyltransferase of Saccharomyces cerevisiae is specific for Cys-Xaa-Xaa-Leu motif proteins and requires the CDC43 gene product but not the DPR1 gene product</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Protein prenylation occurs by modification of proteins with one of at least two isoprenoids, the farnesyl group and the geranylgeranyl group. Protein farnesyltransferases have been identified, but no such enzyme has been identified for geranylgeranylation. We report the identification of an activity in crude soluble yeast extracts that catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl pyrophosphate to proteins having the C-terminal sequence Cys-Ile-Ile-Leu or Cys-Val-Leu-Leu but not to a similar protein ending with Cys-Ile-Ile-Ser. This activity is dependent upon the CDC43/CAL1 gene, which is involved in budding and the control of cell polarity, but does not require the DPR1/RAM1 gene, which is known to be required for the farnesylation of Ras proteins. These results indicate that the protein geranylgeranyltransferase activity is distinct from the protein farnesyltransferase activity and that its specificity depends in part on the extreme C-terminal leucine in the protein to be prenylated.</description><subject>actividad enzimatica</subject><subject>activite enzymatique</subject><subject>Alkyl and Aryl Transferases</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Base Sequence</subject><subject>Biochemistry</subject><subject>Cell Cycle Proteins</subject><subject>Diphosphates</subject><subject>enzymic activity</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>genes</subject><subject>Genes, Fungal</subject><subject>Genetic mutation</subject><subject>genetica</subject><subject>genetics</subject><subject>genetique</subject><subject>Molecular Sequence Data</subject><subject>mutacion</subject><subject>mutation</subject><subject>Oligonucleotides</subject><subject>Plasmids</subject><subject>Polyisoprenyl Phosphates - metabolism</subject><subject>protein geranylgeranyltransferase</subject><subject>proteinas</subject><subject>proteine</subject><subject>Proteins</subject><subject>Pulmonary function tests</subject><subject>Radioactive decay</subject><subject>saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Substrate Specificity</subject><subject>transferasas</subject><subject>transferase</subject><subject>transferases</subject><subject>Transferases - metabolism</subject><subject>Yeasts</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUk1vEzEQXSFQCYUzF0A-wWlTe-1d21IvKC0fUiQqSiVultcZJ64269T2VuRP9TfibUJpLnCwx6P33jx7PEXxmuApwZyebHodp0LkZMoYE0-KCcGSlA2T-GkxwbjipWAVe168iPEaYyxrgY-KowpT1ohqUtxdBJ_A9WgJQffbbh9S3qPN5wjIW3SpjVnp4NdbAxEZCHDrotOAXERxA8ZZZ5D1Ac22sfyp9f2aw4DWPjmLNjuPiHS_QAFuBhdymbQCNDubMZq9exhJi8Ek1A4J9T7dw2cX38kB-rJ4ZnUX4dU-HhdXn85_zL6U82-fv84-zktTkyaVRAoh29ZYrltTtYRXtmkMb3LLGlrXRkJlKNOa8BwIgGkqSpnlvKbEaFHR4-J0V3cztGtYGOhzRzq1CW6tw1Z57dQh0ruVWvpble05z_L3e3nwNwPEpNYuGug63YMfohK4bkT-r_8SSS0ll6zJxJMd0QQfYwD7cBeC1TgJapwEJcSYj5OQFW8fP-GBv__6jL_b46PwD3pQ4MM_CcoOXZfgV8rMNzvmdUw-_HWiNcfNIyervdLL4KK6uiRSEoyFoITS302r3Y0</recordid><startdate>19910515</startdate><enddate>19910515</enddate><creator>Finegold, Alan A.</creator><creator>Johnson, Douglas I.</creator><creator>Farnsworth, Christopher C.</creator><creator>Gelb, Michael H.</creator><creator>Judd, S. Renee</creator><creator>Glomset, John A.</creator><creator>Tamanoi, Fuyuhiko</creator><general>National Academy of Sciences of the United States of America</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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19910515</creationdate><title>Protein geranylgeranyltransferase of Saccharomyces cerevisiae is specific for Cys-Xaa-Xaa-Leu motif proteins and requires the CDC43 gene product but not the DPR1 gene product</title><author>Finegold, Alan A. ; Johnson, Douglas I. ; Farnsworth, Christopher C. ; Gelb, Michael H. ; Judd, S. Renee ; Glomset, John A. ; Tamanoi, Fuyuhiko</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c516t-19889bbcf7abc2b172f66c761076355c9e2c34aa17c341eec62334f77531ca823</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>actividad enzimatica</topic><topic>activite enzymatique</topic><topic>Alkyl and Aryl Transferases</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Base Sequence</topic><topic>Biochemistry</topic><topic>Cell Cycle Proteins</topic><topic>Diphosphates</topic><topic>enzymic activity</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>genes</topic><topic>Genes, Fungal</topic><topic>Genetic mutation</topic><topic>genetica</topic><topic>genetics</topic><topic>genetique</topic><topic>Molecular Sequence Data</topic><topic>mutacion</topic><topic>mutation</topic><topic>Oligonucleotides</topic><topic>Plasmids</topic><topic>Polyisoprenyl Phosphates - metabolism</topic><topic>protein geranylgeranyltransferase</topic><topic>proteinas</topic><topic>proteine</topic><topic>Proteins</topic><topic>Pulmonary function tests</topic><topic>Radioactive decay</topic><topic>saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Substrate Specificity</topic><topic>transferasas</topic><topic>transferase</topic><topic>transferases</topic><topic>Transferases - metabolism</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Finegold, Alan A.</creatorcontrib><creatorcontrib>Johnson, Douglas I.</creatorcontrib><creatorcontrib>Farnsworth, Christopher C.</creatorcontrib><creatorcontrib>Gelb, Michael H.</creatorcontrib><creatorcontrib>Judd, S. Renee</creatorcontrib><creatorcontrib>Glomset, John A.</creatorcontrib><creatorcontrib>Tamanoi, Fuyuhiko</creatorcontrib><creatorcontrib>The University of Chicago, Chicago, IL</creatorcontrib><creatorcontrib>Nebraska-Lincoln Univ. (USA)</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</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>Finegold, Alan A.</au><au>Johnson, Douglas I.</au><au>Farnsworth, Christopher C.</au><au>Gelb, Michael H.</au><au>Judd, S. Renee</au><au>Glomset, John A.</au><au>Tamanoi, Fuyuhiko</au><aucorp>The University of Chicago, Chicago, IL</aucorp><aucorp>Nebraska-Lincoln Univ. (USA)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protein geranylgeranyltransferase of Saccharomyces cerevisiae is specific for Cys-Xaa-Xaa-Leu motif proteins and requires the CDC43 gene product but not the DPR1 gene product</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1991-05-15</date><risdate>1991</risdate><volume>88</volume><issue>10</issue><spage>4448</spage><epage>4452</epage><pages>4448-4452</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Protein prenylation occurs by modification of proteins with one of at least two isoprenoids, the farnesyl group and the geranylgeranyl group. Protein farnesyltransferases have been identified, but no such enzyme has been identified for geranylgeranylation. We report the identification of an activity in crude soluble yeast extracts that catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl pyrophosphate to proteins having the C-terminal sequence Cys-Ile-Ile-Leu or Cys-Val-Leu-Leu but not to a similar protein ending with Cys-Ile-Ile-Ser. This activity is dependent upon the CDC43/CAL1 gene, which is involved in budding and the control of cell polarity, but does not require the DPR1/RAM1 gene, which is known to be required for the farnesylation of Ras proteins. These results indicate that the protein geranylgeranyltransferase activity is distinct from the protein farnesyltransferase activity and that its specificity depends in part on the extreme C-terminal leucine in the protein to be prenylated.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>2034682</pmid><doi>10.1073/pnas.88.10.4448</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Jstor Complete Legacy; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | actividad enzimatica activite enzymatique Alkyl and Aryl Transferases Amino Acid Sequence Amino acids Base Sequence Biochemistry Cell Cycle Proteins Diphosphates enzymic activity Fungal Proteins - genetics Fungal Proteins - metabolism genes Genes, Fungal Genetic mutation genetica genetics genetique Molecular Sequence Data mutacion mutation Oligonucleotides Plasmids Polyisoprenyl Phosphates - metabolism protein geranylgeranyltransferase proteinas proteine Proteins Pulmonary function tests Radioactive decay saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae Proteins Substrate Specificity transferasas transferase transferases Transferases - metabolism Yeasts |
| title | Protein geranylgeranyltransferase of Saccharomyces cerevisiae is specific for Cys-Xaa-Xaa-Leu motif proteins and requires the CDC43 gene product but not the DPR1 gene product |
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