Lysine-87 is a functionally important residue in human prothymosin alphaстатья
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Дата последнего поиска статьи во внешних источниках: 31 октября 2014 г.
Аннотация:Human prothymosin alpha mutants were generated with the aid of random mutagenesis and screened for their ability to inhibit yeast Saccharomyces cerevisiae cell growth. Conversion of Lys-87 to Glu resulted in an inactivated prothymosin alpha mutant, which lost the ability of the wild-type protein to block yeast cell growth. We propose that prothymosin alpha may possess a bipartite rather than monopartite nuclear localization signal, which includes Lys-87, and that the above mutation destroys one part of the nuclear localization signal, thus preventing efficient nuclear uptake of prothymosin alpha.