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 Lettjournal_title
FEBS lettersauthors
Lukashev DE,Chichkova NV,Vartapetian ABdoi
10.1016/s0014-5793(99)00580-3keywords:
subject
Has Abstractpub_date
1999-05-21 00:00:00pages
118-24issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(99)00580-3journal_volume
451pub_type
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