Enzymatic modification of proteins with a geranylgeranyl isoprenoid.
Journal Article (Journal Article)
The prenylation of several proteins involved in oncogenesis and signal transduction plays an essential role in regulating their biological activities. Two distinct isoprenoids are known to be involved in this modification, the 15-carbon farnesyl and 20-carbon geranylgeranyl groups. Thus far, identified farnesylated proteins contain methionine or serine at the COOH terminus, while those modified by geranylgeranyl end in leucine. This report describes the characterization of an enzyme activity that transfers the geranylgeranyl group to candidate proteins. The enzyme, termed a "protein geranylgeranyltransferase," exhibits a marked preference for substrate proteins that contain leucine at the COOH terminus. In fact, the enzyme will efficiently modify a normally farnesylated protein, Ha-ras, if its COOH-terminal amino acid is switched from serine to leucine. Additional studies characterize this enzyme and suggest that it is responsible for the geranylgeranyl modification of a number of GTP-binding proteins (or their subunits) that contain a consensus prenylation sequence ending in leucine.
Full Text
Duke Authors
Cited Authors
- Casey, PJ; Thissen, JA; Moomaw, JF
Published Date
- October 1, 1991
Published In
Volume / Issue
- 88 / 19
Start / End Page
- 8631 - 8635
PubMed ID
- 1924324
Pubmed Central ID
- PMC52563
International Standard Serial Number (ISSN)
- 0027-8424
Digital Object Identifier (DOI)
- 10.1073/pnas.88.19.8631
Language
- eng
Conference Location
- United States