Escherichia coli ribosomal protein S1 and its mutant, shorter, form‐S1 were cleaved at internal methionyl residues to yield, respectively, six and five gragments of M ranging from 1000 to 24000. Methods are described to isolate the fragments in pure form. Four of the fragments (designated F2a, F2b, F3 and F4) contain between 86 and 215 amino acids and are therefore as large as other robosomal proteins. Fragments F2a, derived of S1 [S. Giorginis and A.R. Subramanian (1980) J. Mol. biol. 141, 393‐408]. Here we show that the RNA binding domain of S1 is essentially contained of S1, whose activity is modified by ligand binding, was localized in F2b, a fragment with little RNA binding capacity. The charaterisitic RNAbinding domain and a weak riosome binding domain of S1 have previously been localized in the large trypsin‐resistent core S1‐F1 [T. Suryanarayana and A.R. Subramanian (1979) J. Mol. Biol. 127, 41–54]. Together these date indicate that two of the key functional domains S1 are located in two regions of the molecule separated by an open, exposed segment. The present study also revealed that the nonreactive ‐SH group of S1 becomes reactive m1‐S1 by the loss of remote C‐terminal region in the latter.
|Number of pages||5|
|Journal||European Journal of Biochemistry|
|Publication status||Published - Oct 1981|
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