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Proteolysis of Ribosomal Protein S1 from Escherichia coli and Thermus thermophilus Leads to Formation of Two Different Fragments

O. M. Selivanova, Yu. Yu. Fedorova, and I. N. Serduyk*

Institute of Protein Research, Russian Academy of Sciences, ul. Institutskaya 4, 142290 Pushchino, Moscow Region, Russia; fax: (495) 632-7871; E-mail: serdyuk@vega.protres.ru

* To whom correspondence should be addressed.

Received March 22, 2007; Revision received June 23, 2007
As a result of limited tryptic proteolysis of S1 ribosomal protein (molecular mass 60 kD) from Thermus thermophilus, 25 N-terminal amino acid residues and 71 C-terminal amino acid residues are split off and a stable high-molecular-weight fragment with molecular mass of 49 kD is formed that retains RNA-binding properties and is capable of interacting with 30S ribosomal subunit. Earlier, application of a similar procedure for the formation of a fragment of S1 protein from Escherichia coli resulted in splitting of 171 N-terminal amino acid residues with the formation of a 41.3 kD fragment that possesses RNA-binding properties only. Thus, in spite of high homology between E. coli and T. thermophilus proteins, the proteolysis leads to the formation of two different fragments, which points, in our opinion, to the fact of significant differences between their structures.
KEY WORDS: ribosome, S1 ribosomal protein, limited proteolysis, Thermus thermophilus

DOI: 10.1134/S0006297907110089