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. 1969 Apr;62(4):1181–1188. doi: 10.1073/pnas.62.4.1181

POLYPEPTIDE CHAIN INITIATION IN E. coli: ISOLATION OF HOMOGENEOUS INITIATION FACTOR F2 AND ITS RELATION TO RIBOSOMAL PROTEINS*

Yung-Bog Chae 1, Rajarshi Mazumder 1, Severo Ochoa 1
PMCID: PMC223631  PMID: 4894691

Abstract

Previous work has shown that F2, one of several ribosomal factors involved in polypeptide chain initiation, functions in the binding of formylmethionyl-transfer RNA (fMet ∼ tRNAf) to a messenger RNA-ribosome complex. F2 was isolated from 1.0 M ammonium chloride washes of E. coli Q13 ribosomes as a protein homogeneous on polyacrylamide gel electrophoresis at both pH 4.5 and 7.8. Its molecular weight is approximately 80,000. Comparison of electrophoretic patterns of ribosomal proteins from NH4Cl-washed and unwashed ribosomes and F2, at pH 4.5, shows that F2 corresponds to the slowest-moving component of the proteins derived from unwashed ribosomes. This component is missing from the NH4Cl-washed ribosomes. The activity of F2 is stimulated by two additional factors, initiation factor F1 and a factor(s) present in a narrow ammonium sulfate fraction of the ribosomal NH4Cl wash. The nature of the latter is unknown.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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