Premium
Mutational analysis of human prothymosin α reveals a bipartite nuclear localization signal
Author(s) -
Rubtsov Yuri P.,
Zolotukhin Andrei S.,
Vorobjev Ivan A.,
Chichkova Nina V.,
Pavlov Nickolay A.,
Karger Elena M.,
Evstafieva Alexandra G.,
Felber Barbara K.,
Vartapetian Andrey B.
Publication year - 1997
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(97)00824-7
Subject(s) - nuclear localization sequence , saccharomyces cerevisiae , nuclear protein , nuclear transport , mutant , biology , cell nucleus , microbiology and biotechnology , subcellular localization , mutation , yeast , biochemistry , cytoplasm , gene , transcription factor
Mutants of human prothymosin α with impaired ability to inhibit yeast Saccharomyces cerevisiae . cerevisiae cell growth were characterized. Two types of prothymosin α‐inactivating mutations were observed. Mutations that belong to the first type compromised the nuclear entry of prothymosin α by affecting its nuclear localization signal. Analysis of subcellular distribution of GFP‐prothymosin α fusions revealed a bipartite nuclear localization signal that is both necessary and sufficient for nuclear import of the protein in human cells. Mutations of the second type abrogated the inhibitory action of prothymosin α through an unknown mechanism, without influencing the nuclear import of the protein.