title: Multiple tRNA attachment sites in prothymosin alpha.
abstract: A covalent complex formed by bacterial tRNAs and prothymosin alpha, an abundant acidic nuclear protein involved in proliferation of mammalian cells, upon production of the recombinant rat protein in Escherichia coli cells was studied. Several tRNA attachment sites were identified in the prothymosin alpha molecule using a combination of deletion analysis of prothymosin alpha and site-specific fragmentation of the protein moiety of the prothymosin alpha-tRNA complex. The electrophoretic mobilities of the tRNA-linked prothymosin alpha and its derivatives are consistent with one tRNA molecule attached to one prothymosin alpha molecule, thus suggesting that alternative tRNA linking to one of several available attachment sites occurs. The possible effect of tRNA attachment on the nuclear uptake of prothymosin alpha is discussed.
authors.affiliation: Belozersky Institute of Physico-Chemical Biology and Center of Molecular Medicine, Moscow State University, Russia.
authors.forename: D E
authors.initials: DE
authors.lastname: Lukashev
authors.forename: N V
authors.initials: NV
authors.lastname: Chichkova
authors.forename: A B
authors.initials: AB
authors.lastname: Vartapetian
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D004926:Escherichia coli / Q000378:metabolism; D008954:Models, Biological; D008969:Molecular Sequence Data; D016296:Mutagenesis; D011485:Protein Binding; D011498:Protein Precursors / Q000737:chemistry / Q000378:metabolism*; D012343:RNA, Transfer / Q000378:metabolism*; D051381:Rats; D013947:Thymosin / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism
chemical_list: D011498:Protein Precursors; C040782:prothymosin alpha; D013947:Thymosin; D012343:RNA, Transfer