NDLI: 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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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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Two-dimensional life?

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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.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Finegold, A. A. Judd, S. R. Tamanoi, F. Gelb, M. H. Johnson, D. I. Farnsworth, C. C. Glomset, J. A.
Description	Author Affiliation: Finegold AA ( Department of Biochemistry and Molecular Biology, University of Chicago, IL 60637.);
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.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	10
Volume Number	88
Language	English
Publisher	National Academy of Sciences
Publisher Date	1991-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Alkyl And Aryl Transferases Cell Cycle Proteins Fungal Proteins Metabolism Genes, Fungal Saccharomyces Cerevisiae Proteins Saccharomyces Cerevisiae Enzymology Transferases Amino Acid Sequence Genetics Molecular Sequence Data Polyisoprenyl Phosphates Substrate Specificity Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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