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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Lukashev DE,Chichkova NV,Vartapetian AB

doi

10.1016/s0014-5793(99)00580-3

keywords:

subject

Has Abstract

pub_date

1999-05-21 00:00:00

pages

118-24

issue

2

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(99)00580-3

journal_volume

451

pub_type

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