RGD Reference Report - Expression cloning of a novel farnesylated protein, RDJ2, encoding a DnaJ protein homologue. - Rat Genome Database

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Expression cloning of a novel farnesylated protein, RDJ2, encoding a DnaJ protein homologue.

Authors: Andres, DA  Shao, H  Crick, DC  Finlin, BS 
Citation: Andres DA, etal., Arch Biochem Biophys 1997 Oct 1;346(1):113-24.
RGD ID: 70722
Pubmed: PMID:9328291   (View Abstract at PubMed)
DOI: DOI:10.1006/abbi.1997.0296   (Journal Full-text)

The CAAX farnesyltransferase is a heterodimeric enzyme that attaches a farnesyl group to a single cysteine in cellular proteins which terminate in the sequence CAAX, where C is cysteine, A is an aliphatic amino acid, and X is most often methionine or serine. Substrates include the p21ras proteins, nuclear lamins, and a series of retinal proteins. To date, a limited number of substrates for the farnesyltransferase have been identified, predominantly by demonstration of the attachment of a farnesyl group to previously identified cDNA clones which encode proteins containing an appropriate carboxyl-terminal tetrapeptide. We describe here the use of a cDNA fusion protein expression library, together with enzymatic in vitro [3H]farnesyl radiolabeling, as a means of identifying novel farnesylated proteins. One candidate cDNA was fully cloned and found to be a homologue of the Escherichia coli heat shock gene dnaJ. The predicted amino acid sequence of this protein was found to terminate with the tetrapeptide Cys-Ala-His-Gln, which conforms to the consensus sequence for recognition by farnesyltransferase, and was shown to undergo in vivo farnesylation. This farnesylated protein, designated RDJ2 (rat DnaJ homologue 2), is a novel and ubiquitously expressed DnaJ homologue and is the newest member of the subfamily of DnaJ-related proteins which are posttranslationally modified by protein farnesylation.

Objects referenced in this article
Gene Dnaja2 DnaJ heat shock protein family (Hsp40) member A2 Rattus norvegicus

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