Literature DB >> 1100506

The primary structure of the 5s rRNA binding protein L25 of Escherichia coli ribosomes.

K G Bitar, B Wittmann-Liebold.   

Abstract

The primary structure of protein L25 from the large subunit of Escherichia coli ribosomes was determined by isolation and analysis of peptides obtained after cleavage of the protein with trypsin, thermolysin and Staphylococcus protease as well as by Edman degradation of the intact protein and of a CNBr peptide. The complete amino acid sequence is shown in Fig. 4. There are sequence homologies within protein L25 (Table 6) as well as between protein L25 and other ribosomal proteins (Table 5).

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Year:  1975        PMID: 1100506     DOI: 10.1515/bchm2.1975.356.2.1343

Source DB:  PubMed          Journal:  Hoppe Seylers Z Physiol Chem        ISSN: 0018-4888


  2 in total

1.  Cloning, characterization, and physical location of the rplY gene which encodes ribosomal protein L25 in Escherichia coli K12.

Authors:  Y Uemura; S Isono; K Isono
Journal:  Mol Gen Genet       Date:  1991-04

2.  The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general stress proteins and glutaminyl-tRNA synthetases.

Authors:  M Stoldt; J Wöhnert; M Görlach; L R Brown
Journal:  EMBO J       Date:  1998-11-02       Impact factor: 11.598

  2 in total

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