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Enzymatic modification of proteins with a geranylgeranyl isoprenoid.

Publication ,  Journal Article
Casey, PJ; Thissen, JA; Moomaw, JF
Published in: Proc Natl Acad Sci U S A
October 1, 1991

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.

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Published In

Proc Natl Acad Sci U S A

DOI

ISSN

0027-8424

Publication Date

October 1, 1991

Volume

88

Issue

19

Start / End Page

8631 / 8635

Location

United States

Related Subject Headings

  • Transferases
  • Substrate Specificity
  • Recombinant Proteins
  • Proto-Oncogene Proteins p21(ras)
  • Protein Processing, Post-Translational
  • Peptides
  • Molecular Sequence Data
  • In Vitro Techniques
  • GTP-Binding Proteins
  • Diterpenes
 

Citation

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Casey, P. J., Thissen, J. A., & Moomaw, J. F. (1991). Enzymatic modification of proteins with a geranylgeranyl isoprenoid. Proc Natl Acad Sci U S A, 88(19), 8631–8635. https://doi.org/10.1073/pnas.88.19.8631
Casey, P. J., J. A. Thissen, and J. F. Moomaw. “Enzymatic modification of proteins with a geranylgeranyl isoprenoid.Proc Natl Acad Sci U S A 88, no. 19 (October 1, 1991): 8631–35. https://doi.org/10.1073/pnas.88.19.8631.
Casey PJ, Thissen JA, Moomaw JF. Enzymatic modification of proteins with a geranylgeranyl isoprenoid. Proc Natl Acad Sci U S A. 1991 Oct 1;88(19):8631–5.
Casey, P. J., et al. “Enzymatic modification of proteins with a geranylgeranyl isoprenoid.Proc Natl Acad Sci U S A, vol. 88, no. 19, Oct. 1991, pp. 8631–35. Pubmed, doi:10.1073/pnas.88.19.8631.
Casey PJ, Thissen JA, Moomaw JF. Enzymatic modification of proteins with a geranylgeranyl isoprenoid. Proc Natl Acad Sci U S A. 1991 Oct 1;88(19):8631–8635.
Journal cover image

Published In

Proc Natl Acad Sci U S A

DOI

ISSN

0027-8424

Publication Date

October 1, 1991

Volume

88

Issue

19

Start / End Page

8631 / 8635

Location

United States

Related Subject Headings

  • Transferases
  • Substrate Specificity
  • Recombinant Proteins
  • Proto-Oncogene Proteins p21(ras)
  • Protein Processing, Post-Translational
  • Peptides
  • Molecular Sequence Data
  • In Vitro Techniques
  • GTP-Binding Proteins
  • Diterpenes