Open AccessA single domain of yeast poly(A)-binding protein is necessary and sufficient for RNA binding and cell viability.
Author(s) -
Alan B. Sachs,
Ronald W. Davis,
Roger D. Kornberg
Publication year - 1987
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.7.9.3268
Subject(s) - biology , saccharomyces cerevisiae , poly(a) binding protein , binding site , yeast , binding domain , plasma protein binding , biochemistry , binding protein , rna , peptide sequence , rna binding protein , microbiology and biotechnology , gene
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.