POLYPEPTIDE CHAIN INITIATION IN E. coli : ISOLATION OF HOMOGENEOUS INITIATION FACTOR F 2 AND ITS RELATION TO RIBOSOMAL PROTEINS
- 1 April 1969
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 62 (4) , 1181-1188
- https://doi.org/10.1073/pnas.62.4.1181
Abstract
Previous work has shown that F(2), one of several ribosomal factors involved in polypeptide chain initiation, functions in the binding of formylmethionyl-transfer RNA (fMet approximately tRNA(f)) to a messenger RNA-ribosome complex. F(2) 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 NH(4)Cl-washed and unwashed ribosomes and F(2), at pH 4.5, shows that F(2) corresponds to the slowest-moving component of the proteins derived from unwashed ribosomes. This component is missing from the NH(4)Cl-washed ribosomes. The activity of F(2) is stimulated by two additional factors, initiation factor F(1) and a factor(s) present in a narrow ammonium sulfate fraction of the ribosomal NH(4)Cl wash. The nature of the latter is unknown.Keywords
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