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Protein prenyltransferases.

Maurer-Stroh S, Washietl S, Eisenhaber F - Genome Biol. (2003)

Bottom Line: 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.The effects of these inhibitors are complicated, however, by the overlapping substrate specificities of geranylgeranyltransferase I and farnesyltransferase.

View Article: PubMed Central - HTML - PubMed

Affiliation: Research Institute of Molecular Pathology, Dr Bohr-Gasse 7, A-1030 Vienna, Austria. stroh@imp.univie.ac.at

ABSTRACT

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 '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.

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Gene structures and chromosomal locations of human protein prenyltransferase subunit genes. The chromosome diagrams and the locations of the genes on the cytogenetic map are according to the NCBI MapViewer [67]. The sizes of the genes are indicated but are not drawn to scale. (a) Genes encoding CaaX protein prenyltransferases are relatively long; (b) genes encoding non-CaaX protein prenyltransferases are much shorter.
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Figure 1: Gene structures and chromosomal locations of human protein prenyltransferase subunit genes. The chromosome diagrams and the locations of the genes on the cytogenetic map are according to the NCBI MapViewer [67]. The sizes of the genes are indicated but are not drawn to scale. (a) Genes encoding CaaX protein prenyltransferases are relatively long; (b) genes encoding non-CaaX protein prenyltransferases are much shorter.

Mentions: The genomic organization of the human genes that encode protein prenyltransferases is shown in Figure 1. It is interesting 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 differing intron lengths.


Protein prenyltransferases.

Maurer-Stroh S, Washietl S, Eisenhaber F - Genome Biol. (2003)

Gene structures and chromosomal locations of human protein prenyltransferase subunit genes. The chromosome diagrams and the locations of the genes on the cytogenetic map are according to the NCBI MapViewer [67]. The sizes of the genes are indicated but are not drawn to scale. (a) Genes encoding CaaX protein prenyltransferases are relatively long; (b) genes encoding non-CaaX protein prenyltransferases are much shorter.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC154572&req=5

Figure 1: Gene structures and chromosomal locations of human protein prenyltransferase subunit genes. The chromosome diagrams and the locations of the genes on the cytogenetic map are according to the NCBI MapViewer [67]. The sizes of the genes are indicated but are not drawn to scale. (a) Genes encoding CaaX protein prenyltransferases are relatively long; (b) genes encoding non-CaaX protein prenyltransferases are much shorter.
Mentions: The genomic organization of the human genes that encode protein prenyltransferases is shown in Figure 1. It is interesting 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 differing intron lengths.

Bottom Line: 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.The effects of these inhibitors are complicated, however, by the overlapping substrate specificities of geranylgeranyltransferase I and farnesyltransferase.

View Article: PubMed Central - HTML - PubMed

Affiliation: Research Institute of Molecular Pathology, Dr Bohr-Gasse 7, A-1030 Vienna, Austria. stroh@imp.univie.ac.at

ABSTRACT

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 '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.

Show MeSH