title: Involvement of a 50-kDa mRNP protein from Saccharomyces cerevisiae in mRNA binding to ribosomes.
abstract: A yeast 50-kDa mRNA-binding protein (50mRNP) is found selectively associated with the 48S and 80S initiation complexes. This protein is structurally related to the translational elongation factor EF-1alpha. The protein reacts with antibodies directed against EF-1alpha and, similarly, EF-1alpha recognizes antibodies against the 50mRNP protein. This is evidence that they share at least one epitope which allows a similar antigenic behavior. In addition, both proteins show similar cleavage patterns upon treatment with the endoproteinase Lys-C. A murine antibody raised against 50mRNP inhibits both 48S and 80S initiation complex formation. The inhibitory effect is relieved by preincubating anti-50mRNP with EF-1alpha. Antibody to EF-1alpha manifests a similar inhibitory pattern for the formation of 48S and 80S complexes. These data strongly suggest that 50mRNP is an EF-1alpha-like polypeptide essential for the formation of the above complexes.
authors.affiliation: Centro de Investigaciones Biomédicas (BIOMED), Facultad de Ciencias dela Salud, Universidad de Carabobo, Maracay, Venezuela.
authors.forename: L
authors.initials: L
authors.lastname: Triana
authors.forename: A C
authors.initials: AC
authors.lastname: Ferreras
authors.forename: E
authors.initials: E
authors.lastname: Cayama
authors.forename: H
authors.initials: H
authors.lastname: Correia
authors.forename: G
authors.initials: G
authors.lastname: Fraile
authors.forename: K
authors.initials: K
authors.lastname: Chakraburtty
authors.forename: F
authors.initials: F
authors.lastname: Herrera
mesh_terms: D000906:Antibodies / Q000276:immunology; D002499:Centrifugation, Density Gradient; D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes / Q000276:immunology; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism; D008666:Metalloendopeptidases / Q000378:metabolism; D010442:Peptide Chain Initiation, Translational; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors / Q000737:chemistry / Q000276:immunology / Q000502:physiology; D010446:Peptide Fragments / Q000302:isolation & purification; D010455:Peptides / Q000037:antagonists & inhibitors / Q000378:metabolism; D011132:Polyribosomes / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D012261:Ribonucleoproteins / Q000737:chemistry / Q000276:immunology / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000737:chemistry / Q000378:metabolism*
chemical_list: D000906:Antibodies; D000939:Epitopes; D005656:Fungal Proteins; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors; D010446:Peptide Fragments; D010455:Peptides; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D012261:Ribonucleoproteins; C026452:messenger ribonucleoprotein; C012001:polyphenylalanine; D008666:Metalloendopeptidases; C039830:peptidyl-Lys metalloendopeptidase