Gene Symbol: rplL
Description: 50S ribosomal protein L7/L12
Species: Thermotoga maritima MSB8
- The organization and expression of essential transcription translation component genes in the extremely thermophilic eubacterium Thermotoga maritimaD Liao
Canadian Institute for Advanced Research, University of British Columbia, Vancouver
J Biol Chem 267:22787-97. 1992..The T. maritima NusG protein exhibits 43% amino acid sequence identity when aligned to the E. coli protein; the alignment is interrupted by a large 171-amino acid-long insertion into the T. maritima protein after codon 45...
- The DNA-dependent RNA-polymerase of Thermotoga maritima; characterisation of the enzyme and the DNA-sequence of the genes for the large subunitsP Palm
Max Planck Institut fur Biochemie, Martinsried, Germany
Nucleic Acids Res 21:4904-8. 1993..The phylogenetic position of T.maritima within the bacterial domain was determined by various methods. It is the lowest bacterial offspring but slightly higher than the chloroplasts...
- Flexibility, conformational diversity and two dimerization modes in complexes of ribosomal protein L12M C Wahl
Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D 82152 Martinsried, Germany
EMBO J 19:174-86. 2000..The structures have been submitted to the Protein Databank (http://www.rcsb.org/pdb) under accession numbers 1DD3 and 1DD4...
- Oligomeric state and mode of self-association of Thermotoga maritima ribosomal stalk protein L12 in solutionPierre D J Moens
School of Biological, Biomedical, and Molecular Sciences, The University of New England, Armidale, New South Wales 2351, Australia
Biochemistry 44:3298-305. 2005..coli system. The exchange rate increases with increasing temperature and approaches the one observed for the E. coli system at 50 degrees C. Possible factors responsible for this difference are discussed...
- Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activationMihaela Diaconu
Röntgenkristallographie, Max Planck Institut fur biophysikalische Chemie, Am Fassberg 11, D 37077 Gottingen, Germany
Cell 121:991-1004. 2005..Highly mobile L7/12 C-terminal domains promote recruitment of translation factors to the ribosome and stimulate GTP hydrolysis by the ribosome bound factors through stabilization of their active GTPase conformation...