title: Mammalian valyl-tRNA synthetase forms a complex with the first elongation factor.
abstract: The high-molecular-mass form of valyl-tRNA synthetase is associated with the first elongation factor activity. It includes two polypeptides of about 50 kDa and two others of 40 and 30 kDa, identified as alpha, beta, gamma and delta subunits of eEF-1H. The complex of valyl-tRNA synthetase with eEF-1H is suggested to be a novel form of the first elongation factor.
authors.affiliation: A.N. Bakh Institute of Biochemistry, Academy of Sciences of the USSR, Moscow.
authors.lastname: Motorin YuA
authors.forename: A D
authors.initials: AD
authors.lastname: Wolfson
authors.forename: A F
authors.initials: AF
authors.lastname: Orlovsky
authors.forename: K L
authors.initials: KL
authors.lastname: Gladilin
mesh_terms: D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D000818:Animals; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors / Q000378:metabolism*; D011817:Rabbits; D014637:Valine-tRNA Ligase / Q000378:metabolism*
chemical_list: D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors; C057342:peptide elongation factor 1H; D000604:Amino Acyl-tRNA Synthetases; D014637:Valine-tRNA Ligase