Protein prenyltransferases 英文参考文献.docVIP

Protein family review Protein prenyltransferases Sebastian Maurer-Stroh, Stefan Washietl and Frank Eisenhaber Address: Research Institute of Molecular Pathology, Dr Bohr-Gasse 7, A-1030 Vienna, Austria. Correspondence: Sebastian Maurer-Stroh. E-mail: stroh@imp.univie.ac.at Published: 1 April 2003 Genome Biology 2003, 4:212 The electronic version of this article is the complete one and can be found online at /2003/4/4/212 ? 2003 BioMed Central Ltd Summary 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 ‘Ca a X’ motif on their protein substrates; geranylgeranyltransferase II recognizes a different, 1 2 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. Gene organization and evolutionary history Gene organization to note that the genes encoding both subunits of non-CaaX prenyltransferases are much smaller (about 6-9 kilobases, kb) than those of the CaaX prenyltransferases (about 30-76 kb). The number of exons in the two types of genes are similar; the differences in gene size therefore result from dif- fering intron lengths. Protein