The adenylyl-cyclase-associated protein, CAP, was originally identified in yeasts as a protein that functions in both signal transduction and cytoskeletal organization. This paper reports the identification of a cDNA and genomic DNA that encodes a CAP homologue from the mushroom . The gene contains eight introns and an ORF encoding a 518 amino acid protein. The CAP is 35.5% and 40.9% identical at the amino acid level with CAP and CAP, respectively. The C-terminal domain shows greater homology (39-46% identity) with yeast CAPs than does the N-terminal domain (27-35% identity). Southern blotting and Northern blotting results suggest that is a single-copy gene and uniformly expressed. Expression of the CAP in both and cerevisiae complemented defects associated with the loss of the C-terminal domain function of the endogenous CAP. By using a yeast two-hybrid assay, an interaction was demonstrated between the CAP and actin. This result and the functional complementation test indicate that CAP from has a conserved C-terminal domain function.

Keyword(s): actin , adenylyl cyclase , cAMP and Ras

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