Journal of Protein Chemistry

, Volume 12, Issue 6, pp 725–734

The complete primary structure of ribosomal protein L1 fromThermus thermophilus

  • R. Amons
  • T. A. Muranova
  • A. I. Rykunova
  • I. A. Eliseikina
  • S. E. Sedelnikova
Article

DOI: 10.1007/BF01024930

Cite this article as:
Amons, R., Muranova, T.A., Rykunova, A.I. et al. J Protein Chem (1993) 12: 725. doi:10.1007/BF01024930

Abstract

The primary structure of the 23S rRNA binding ribosomal protein L1 from the 50S ribosomal subunit ofThermus thermophilus ribosomes has been elucidated by direct protein sequencing of selected peptides prepared by enzymatic and chemical cleavage of the intact purified protein. The polypeptide chain contains 228 amino acids and has a calculated molecular mass of 24,694 D. A comparison with the primary structures of the corresponding proteins fromEscherichia coli andBacillus stearothermophilus reveals a sequence homology of 49% and 58%, respectively. With respect to both proteins, L1 fromT. thermophilus contains particularly less Ala, Lys, Gln, and Val, whereas its content of Glu, Gly, His, Ile, and Arg is higher. In addition, two fragments obtained by limited proteolysis of the intact, unmodified protein were characterized.

Key words

Amino acid sequenceribosomal proteinL1 fromThermus thermophilusdomain structure

Copyright information

© Plenum Publishing Corporation 1993

Authors and Affiliations

  • R. Amons
    • 1
  • T. A. Muranova
    • 2
  • A. I. Rykunova
    • 2
  • I. A. Eliseikina
    • 3
  • S. E. Sedelnikova
    • 3
  1. 1.Department of Medical BiochemistryUniversity of LeidenLeidenThe Netherlands
  2. 2.Branch of Shemyakin Institute of Bioorganic Chemistry of the Russian Academy of SciencesPushchino, Moscow RegionRussia
  3. 3.Department of the Structure and Function of RibosomesInstitute of Protein ResearchPushchino, Moscow RegionRussia