Functional homology between E. coli ribosomal protein L11 and B. megaterium protein BM-L11

descriptionPublicationkeyboard_double_arrow_right Article 01 Nov 1980 English Publisher:Springer Science and Business Media LLCJournal:Molecular and General Genetics MGG, volume 180, pages 11-15 (issn: 0026-8925, eissn: 1432-1874,

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Authors: M J, Stark; E, Cundliffe; J, Dijk; G, Stöffler;

doi: 10.1007/bf00267346

pmid: 6777629

Functional homology between E. coli ribosomal protein L11 and B. megaterium protein BM-L11

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Abstract

Ribosomes from the thiostrepton-resistant mutant MJ1 of Bacillus megaterium completely lack a protein designated BM-L11. When assayed in vitro, such ribosomes show an impaired ability to hydrolyse GTP in the presence of the elongation factor EF-G and are unable to support the synthesis of (p)ppGpp in response to the stringent factor. Restoration of both these activities can be achieved by re-addition of either protein BM-L11 or its serological homologue from Escherichia coli, protein L11, implying that these two proteins are related functionally as well as immunologically.

Related Organizations

University of Leicester
United Kingdom
Max Planck Institute for Molecular Genetics
Germany
Max Planck Society
Germany

Keywords

Ribosomal Proteins, GTP Pyrophosphokinase, Bacterial Proteins, Species Specificity, Bacillus megaterium, Escherichia coli, Guanosine Pentaphosphate, Guanosine Tetraphosphate

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