Peptide Chain Termination, VI. Purification and Site of Action of S | Zendy

J L Goldstein | Zendy; Gregory Milman | Zendy; Edward M. Scolnick | Zendy; T. Caskey | Zendy

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Peptide Chain Termination, VI. Purification and Site of Action of S

Author(s) -

J L Goldstein,

Gregory Milman,

Edward M. Scolnick,

T. Caskey

Publication year - 1970

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.65.2.430

Subject(s) - terminator (solar) , release factor , escherichia coli , peptide , elongation factor , transfer rna , ef tu , biochemistry , chemistry , polypeptide chain , elongation , cleavage (geology) , biology , enzyme , gene , rna , ribosome , physics , ionosphere , astronomy , paleontology , fracture (geology) , materials science , ultimate tensile strength , metallurgy

PEPTIDE CHAIN TERMINATION IS A RESULT OF AT LEAST TWO EVENTS: terminator codon recognition and hydrolysis of peptidyl tRNA. A protein factor S, isolated from the supernatant of Escherichia coli B, stimulates fMet release. Factor S lowers the K(m) for terminator trinucleotides without altering the V(max) of release and therefore acts at terminator codon recognition. The S protein differs from initiation factors, elongation factor G, several forms of elongation factor T and release factors. The importance of the 2% Tu content in purified S is unresolved.

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