Lysine‐87 is a functionally important residue in human prothymosin α

FEBS Letters

Rubtsov, Yuri¹  Vartapetian, Andrey¹ 

[1] Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119899 Moscow, Russian Federation

关键词: Prothymosin α;    PCR-based mutagenesis;    Cell growth inhibition;    Nuclear localization signal;    Saccharomyces cerevisiae;    NLS;    nuclear localization signal;    PCR;    polymerase chain reaction;    ProTα;    prothymosin α;   

DOI  :  10.1016/S0014-5793(96)01171-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Human prothymosin a 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 α mutant, which lost the ability of the wild-type protein to block yeast cell growth. We propose that prothymosin α 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 α.

【 授权许可】

Unknown