Open AccessIdentification of proteins associating with poly(A)‐binding‐protein mRNA
Author(s) -
BERGER Lloyd C.,
BAG Jnanankur,
Sells Bruce H.
Publication year - 1992
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1992.tb16688.x
Subject(s) - messenger rna , binding protein , nucleotide , untranslated region , rna binding protein , translation (biology) , chemistry , microbiology and biotechnology , binding site , binding domain , biochemistry , biology , gene
Synthesis of poly(A)‐binding protein is regulated at the translational level. We have investigated the binding of proteins to this mRNA on the premise that the protein(s) of the mRNP complex may be involved in regulating the expression of the mRNA. We found the first 243 nucleotides of the 5′ untranslated region to contain sequences essential for RNP formation. A large, single‐stranded bulge structure encompassing stretches rich in adenine nucleotides and a potential stem‐loop domain appear to be the primary sites for protein binding. Removal of the 243‐nucleotide segment results in a drastic reduction in protein binding and a concomitant increase in translational efficiency in vitro . We suggest that proteins binding to this region, including poly(A)‐binding protein itself, may be essential for regulating translation of this mRNA.