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DOI: 10.1055/s-2007-973665
© Hippokrates Verlag GmbH Stuttgart
Farnesylation of Batten Disease CLN3 Protein
Publication History
Publication Date:
13 March 2007 (online)
Abstract
The carboxyl terminal of the predicted amino acid sequence of the Batten disease CLN3 gene protein is CQLS. This motif is expected to be a site for farnesylation at the cysteine residue. In order to determine whether this is indeed farnesylated we have carried out the in-vitro prenylation of tetrapeptides CVLS, CAIL and CQLS using a farnesyl transferase preparation from bovine brain. The data shows that the CQLS is a good acceptor of a farnesyl group similar to CVLS while it is a poor acceptor of a geranylgeranyl group unlike CAIL, which is a good acceptor of a geranylgeranyl group. This suggests that the CLN3 gene product may be a farnesylated protein.
Key words
Batten disease - Neuronal ceroid-lipofuscinosis - Farnesylation