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Biochemistry (Moscow)

, Volume 72, Issue 11, pp 1225–1232 | Cite as

Proteolysis of ribosomal protein S1 from Escherichia coli and Thermus thermophilus leads to formation of two different fragments

  • O. M. Selivanova
  • Yu. Yu. Fedorova
  • I. N. SerduykEmail author
Article

Abstract

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 

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Copyright information

© Pleiades Publishing, Ltd. 2007

Authors and Affiliations

  • O. M. Selivanova
    • 1
  • Yu. Yu. Fedorova
    • 1
  • I. N. Serduyk
    • 1
    Email author
  1. 1.Institute of Protein ResearchRussian Academy of SciencesPushchino, Moscow RegionRussia

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