Abstract
Vinculin is a well-known cytoskeletal protein and is a component of the integrin-mediated cell-matrix adhesion system. Recently, vinculin is also being reported from the nuclei from a number of organisms. However, there is no report yet on purification of nuclear vinculin from the native source of any organism. In the present study, by using western blotting, we show nuclear localization of vinculin in chicken liver. The chicken liver nuclear vinculin was purified to homogeneity and subsequently, the identity of vinculin was confirmed by peptide mass fingerprinting. Further, actin was co-immunoprecipitated with vinculin from chicken liver nuclear extract. Interestingly, the above immunoprecipitate (IP) demonstrated histone specific protease activity. Thus, the present study suggests plausible interaction of vinculin with actin and histone specific proteases in the chicken liver nuclei.
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