A single gene from yeast for both nuclear and cytoplasmic polyadenylate-binding proteins: domain structure and expression.

Abstract:

:Nuclear and cytoplasmic poly(A)-binding proteins have been purified from Saccharomyces cerevisiae, and antisera have been used to isolate a gene that encodes them. The gene occurs in a single copy on chromosome 5 and gives rise to a unique, unspliced 2.1 kb transcript. The nuclear protein appears to be derived from the cytoplasmic one by proteolytic cleavage into 53 and 17 kd polypeptides that remain associated during isolation. DNA sequence determination reveals four tandemly arrayed 90 amino acid regions of homology that probably represent poly(A)-binding domains. A 55 residue A-rich region upstream of the initiator methionine codon in the mRNA shows an affinity for poly(A)-binding protein comparable to that of poly(A)180-220, raising the possibility of feedback regulation of translation.

journal_name

Cell

journal_title

Cell

authors

Sachs AB,Bond MW,Kornberg RD

doi

10.1016/0092-8674(86)90557-x

subject

Has Abstract

pub_date

1986-06-20 00:00:00

pages

827-35

issue

6

eissn

0092-8674

issn

1097-4172

pii

0092-8674(86)90557-X

journal_volume

45

pub_type

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