The primary structure of protein L2 from the Escherichia coli ribosome

Makoto Kimura, Liane Mende, Brigitte Wittmann-Liebold

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

The complete primary structure of protein L2 which is the largest protein component of the E. coli 50 S subunit, has been established. A combination of enzymatic and chemical cleavages has been employed to isolate peptides, which were sequenced by the micro-DABITC/PITC double-coupling method [FEBS Lett. (1978) 93, 205-214]. The sequence determined shows protein L2 to consist of 272 amino acid residues with Mr = 29730. Secondary structure predictions were made based on the primary structure. Further, sequence regions homologous to other ribosomal proteins are presented. These results suggest protein L2, which binds specifically to the 23 S RNA, to show homologous sequence stretches to the other RNA-binding proteins.

Original languageEnglish
Pages (from-to)304-312
Number of pages9
JournalFEBS Letters
Volume149
Issue number2
DOIs
Publication statusPublished - Nov 29 1982

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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