POLYPEPTIDE CHAIN INITIATION IN E. coli: STUDIES ON THE FUNCTION OF INITIATION FACTOR F1*

AUTOR(ES)

Chae, Yung-Bog

RESUMO

The requirement of initiation factors F1 (highly purified) and F2 (electrophoretically homogeneous) for ribosomal binding of N-formylmethionyl transfer RNA (fMet ∼ tRNA) at low Mg2+ concentration (3.5 mM), with the trinucleoside diphosphate ApUpG as messenger, was studied under various experimental conditions with 30S + 50S ribosomes and with 30S subunits alone. The results were qualitatively the same in both cases but the amount of binding was two to three times higher when both 30S and 50S subunits were present.

Documentos Relacionados

• POLYPEPTIDE CHAIN INITIATION IN E. coli: SULFHYDRYL GROUPS AND THE FUNCTION OF INITIATION FACTOR F2*
• POLYPEPTIDE CHAIN INITIATION IN E. coli: ISOLATION OF HOMOGENEOUS INITIATION FACTOR F2 AND ITS RELATION TO RIBOSOMAL PROTEINS*
• Isolation and Properties of Polypeptide Chain Initiation Factor FII from Escherichia coli: Evidence for a Dual Function
• Studies on the mechanism of polypeptide chain termination in cell-free extracts of E. coli.
• Thiostrepton Inhibition of Initiation Factor 1 Activity in Polypeptide Chain Initiation in Escherichia coli