Poly(A) polymerase and a dissociable polyadenylation stimulatory factor encoded by vaccinia virus.

Abstract:

:mRNA made in eukaryotic cells typically has a 3' poly(A) tail that is added posttranscriptionally. To investigate mechanisms by which 3' poly(A) is formed, we identified the genes for the two vaccina virus-encoded polypeptides, VP55 and VP39. Primer-dependent polyadenylation activity was associated exclusively with purified VP55-VP39 heterodimer, which, although stable to column chromatography and glycerol gradient sedimentation, was readily dissociated by antibody to an N-terminal peptide of VP55. Poly(A) polymerase activity was associated with immunopurified VP55, but not with immunopurified or chromatographically purified VP39. VP39 was, however, required for the formation of long poly(A) molecules, in conjunction with either purified VP55 or low concentrations of the heterodimer, and was shown to bind free poly(A). Thus, a catalytic polypeptide and a dissociable poly(A)-binding stimulatory factor each contribute to poly(A) tail formation. No prokaryotic or eukaryotic homologs of either polypeptide were detected in sequence data bases, consistent with the absence of previously reported poly(A) polymerase genes from any source.

journal_name

Cell

journal_title

Cell

authors

Gershon PD,Ahn BY,Garfield M,Moss B

doi

10.1016/0092-8674(91)90048-4

subject

Has Abstract

pub_date

1991-09-20 00:00:00

pages

1269-78

issue

6

eissn

0092-8674

issn

1097-4172

pii

0092-8674(91)90048-4

journal_volume

66

pub_type

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