L. Triana et al., INVOLVEMENT OF A 50-KDA MRNP PROTEIN FROM SACCHAROMYCES-CEREVISIAE INMESSENGER-RNA BINDING TO RIBOSOMES, Archives of biochemistry and biophysics, 344(1), 1997, pp. 1-10
A yeast 50-kDa mRNA-binding protein (50mRNP) is found selectively asso
ciated with the 48S and 80S initiation complexes. This protein is stru
cturally related to the translational elongation factor EF-1 alpha. Th
e protein reacts with antibodies directed against EF-1 alpha and, simi
larly, EF-1 alpha recognizes antibodies against the 50mRNP protein. Th
is is evidence that they share at least one epitope which allows a sim
ilar antigenic behavior, In addition, both proteins show similar cleav
age patterns upon treatment with the endoproteinase Lys-C. A murine an
tibody raised against 50mRNP inhibits both 48S and 80S initiation comp
lex formation. The inhibitory effect is relieved by preincubating anti
-50mRNP with EF-1 alpha. Antibody to EF-1 alpha manifests a similar in
hibitory pattern for the formation of 48S and 80S complexes. These dat
a strongly suggest that 50mRNP is an EF-1 alpha-like polypeptide essen
tial for the formation of the above complexes. (C) 1997 Academic Press
.