Email updates

Keep up to date with the latest news and content from Genome Biology and BioMed Central.

Protein family review

Protein prenyltransferases

Sebastian Maurer-Stroh*, Stefan Washietl and Frank Eisenhaber

Author Affiliations

Research Institute of Molecular Pathology, Dr Bohr-Gasse 7, A-1030 Vienna, Austria

For all author emails, please log on.

Genome Biology 2003, 4:212  doi:10.1186/gb-2003-4-4-212

Published: 1 April 2003

Abstract

Three different protein prenyltransferases (farnesyltransferase and geranylgeranyltransferases I and II) catalyze the attachment of prenyl lipid anchors 15 or 20 carbons long to the carboxyl termini of a variety of eukaryotic proteins. Farnesyltransferase and geranylgeranyltransferase I both recognize a 'Ca1a2X' motif on their protein substrates; geranylgeranyltransferase II recognizes a different, non-CaaX motif. Each enzyme has two subunits. The genes encoding CaaX protein prenyltransferases are considerably longer than those encoding non-CaaX subunits, as a result of longer introns. Alternative splice forms are predicted to occur, but the extent to which each splice form is translated and the functions of the different resulting isoforms remain to be established. Farnesyltransferase-inhibitor drugs have been developed as anti-cancer agents and may also be able to treat several other diseases. The effects of these inhibitors are complicated, however, by the overlapping substrate specificities of geranylgeranyltransferase I and farnesyltransferase.