Premium
Lysine‐87 is a functionally important residue in human prothymosin α
Author(s) -
Rubtsov Yuri,
Vartapetian Andrey
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01171-4
Subject(s) - nuclear localization sequence , saccharomyces cerevisiae , mutant , yeast , mutagenesis , chemistry , microbiology and biotechnology , nuclear transport , nuclear protein , cell growth , biochemistry , mutation , biology , cell nucleus , transcription factor , cytoplasm , gene
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.