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A single domain of yeast poly(A)-binding protein is necessary and sufficient for RNA binding and cell viability.

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Sachs, A B, Davis, R W, Kornberg, R D·1987·Molecular and Cellular Biology

Abstract

The poly(A)-binding protein (PAB) gene of Saccharomyces cerevisiae is essential for cell growth. A 66-amino acid polypeptide containing half of a repeated N-terminal domain can replace the entire protein in vivo. Neither an octapeptide sequence conserved among eucaryotic RNA-binding proteins nor the C-terminal domain of PAB is required for function in vivo. A single N-terminal domain is nearly identical to the entire protein in the number of high-affinity sites for poly(A) binding in vitro (one site with an association constant of approximately 2 X 10(7) M-1) and in the size of the binding site (12 A residues). Multiple N-terminal domains afford a mechanism of PAB transfer between poly(A) strands.

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Metadata

Authors
Sachs, A. B., Davis, R. W., & Kornberg, R. D.
Venue
Molecular and Cellular Biology
Published
1987-09
Volume
7
Issue
9
Pages
3268-3276
ISSN
  • 0270-7306 (ISSN-L)
  • 1098-5549
OpenAlex
W1936434484
Cited by
423
References
0
FWCI
5.15
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: A single domain of yeast poly(A)-binding protein is necessary and sufficient for RNA binding and cell viability. https://app.cochat.ai/papers/10.1128/mcb.7.9.3268
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Sachs, A. B., Davis, R. W., & Kornberg, R. D. (1987). A single domain of yeast poly(A)-binding protein is necessary and sufficient for RNA binding and cell viability. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.7.9.3268

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