title: 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.
authors.affiliation: Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russian Federation.
authors.forename: Y
authors.initials: Y
authors.lastname: Rubtsov
authors.forename: A
authors.initials: A
authors.lastname: Vartapetian
mesh_terms: D000595:Amino Acid Sequence; D002467:Cell Nucleus / Q000378:metabolism; D006801:Humans; D008239:Lysine / Q000737:chemistry*; D008969:Molecular Sequence Data; D016296:Mutagenesis; D010957:Plasmids; D017354:Point Mutation; D011498:Protein Precursors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000254:growth & development; D013947:Thymosin / Q000031:analogs & derivatives* / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D014170:Transformation, Genetic
chemical_list: D011498:Protein Precursors; C040782:prothymosin alpha; D013947:Thymosin; D008239:Lysine