Fragments of Ribosomal Protein S1 and Its Mutant Form m1‐S1: Localization of Nucleic‐Acid‐Binding Domain in the Middle Region of S1

Alap R. SUBRAMANIAN, Peter RIENHARDT, Makoto KIMURA, Tangirala SURYANARAYANA

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33 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)245-249
Number of pages5
JournalEuropean Journal of Biochemistry
Volume119
Issue number2
DOIs
Publication statusPublished - Oct 1981

All Science Journal Classification (ASJC) codes

  • Biochemistry

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