Specific hydrolysis of methionyl-tRNAfMetcatalyzed by a purified peptide initiation factor from rat liver | Zendy

Jan Hradec | Zendy

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Specific hydrolysis of methionyl-tRNA_f^Metcatalyzed by a purified peptide initiation factor from rat liver

Author(s) -

Jan Hradec

Publication year - 1975

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/2.11.2119

Subject(s) - transfer rna , biology , hydrolysis , biochemistry , peptide , ribosome , methionine , ribosomal rna , gtp' , amino acid , enzyme , rna , gene

A peptide initiation factor purified from rat liver and promoting the binding of initiator tRNA and model initiators to 40S and 80S ribosome at an acid pH liberates methionine and N-acetylmethionine from Trna Met f at neutral reaction. Phenylalanyl-tRNA, N-acetylphenylalanyl-tRNA and methionyl-tRNA Met m are not hydrolyzed under the same conditions. Hydrolysis of methionyl-tRNA Met f is stimulated by the presence of the 40S ribosomal subunit and preceeds at 37 degrees C until all the substrate has been split. No hydrolysis of initiator tRNA or N-acetylmethionyl-tRNA Met f occurs at 0 degrees C. Hydrolysis is slightly stimulated by GTP and MG2+ but not by KCl. The binding and hydrolyzing activity associated with a single protein factor may have an important function in regulating the rate of peptide initiation.

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