PMID: 230041Dec 1, 1979

Nucleic acid binding and unfolding properties of ribosomal protein S1 and the derivatives S1-F1 and m1-S1

European Journal of Biochemistry
J O ThomasA R Subramanian


The nucleic acid binding and unwinding properties of wild-type Escherichia coli ribosomal protein S1 have been compared to those of a mutant form and a large trypsin-resistant fragment, both reported recently [J. Mol. Biol. 127, 41-45 (1979) and J. Biol. Chem. 254, 4309-4312 (1979). The mutant (m1-S1) contains 77% and the fragment (S1-F1) 66% of the polypeptide chain length (approximately 600 amino acid residues) of protein S1. The mutant is active in protein synthesis in vitro; the fragment, although retaining one or more of the functional domains of S1, is inactive in protein synthesis. We find that m1-S1 is is almost as effective as S1 in binding to poly(rU), phage MS2 RNA and simian virus 40 (SV40) DNA, and in unfolding poly(rU) and the helical structures present in MS2 RNA and phi X174 viral DNA. S1-F1, however, binds to poly(rU) and denatured SV40 DNA, but not to MS2 RNA. It unfolds neither poly(rU), nor the residual secondary structure of MS2 RNA or phi X174 viral DNA. Thus, there appears to be a correlation between the loss in ability of S1 to unwind RNA and the loss in its ability to function in protein synthesis.


Aug 5, 1978·Journal of Molecular Biology·J O ThomasW Szer
Jun 1, 1977·Proceedings of the National Academy of Sciences of the United States of America·A KolbW Szer
Nov 1, 1977·Proceedings of the National Academy of Sciences of the United States of America·D E DraperP H von Hippel
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Oct 4, 2012·Molecular & Cellular Proteomics : MCP·Matthew A LauberJames P Reilly
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Nov 19, 2015·Nucleic Acids Research·Heidi GytzCharlotte R Knudsen
Jun 17, 2005·BMC Molecular Biology·Jody BurksJacek Wower
Mar 14, 2007·Biochemical and Biophysical Research Communications·Young Seoub ParkGyoo Yeol Jung
Aug 23, 2005·Biochemical and Biophysical Research Communications·Reinhard DeppingWolfgang Rüger
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