Lysine-87 is a functionally important residue in human prothymosin alpha.

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Rubtsov Y,Vartapetian A

doi

10.1016/s0014-5793(96)01171-4

subject

Has Abstract

pub_date

1996-11-18 00:00:00

pages

215-8

issue

2-3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(96)01171-4

journal_volume

397

pub_type

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