(TrmD) from Aquifex aeolicus
نویسندگان
چکیده
Genes to Cells (2006) 11 , 1353–1365 Journal compilation © 2006 by the Molecular Biology Society of Japan/Blackwell Publishing Ltd. 1353 DOI: 10.1111/j.1365-2443.2006.01022.x Blackwell Publishing Inc M lden, USA GTC enes to Cells 1356-9597 © Blackwell Publ shing Ltd ? 2006 1 Original Artic e tRNA specificity of Aquifex aeolicus TrmD H. Takeda e al. The substrate specificity of tRNA (m 1 G37) methyltransferase (TrmD) from Aquifex aeolicus
منابع مشابه
Functionality of Purified s (s) and a NifA-Like Protein from the Hyperthermophile Aquifex aeolicus
Aquifex aeolicus Hyperthermophile NifA-Like Protein from the) and a 54 ς (N ς Functionality of Purified
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Ni-C in the O(2)-tolerant hydrogenase I from Aquifex aeolicus binds a hydride weaker than that in O(2)-sensitive hydrogenases. This is in line with the enhanced light-sensitivity of Ni-C, greater lability of the hydride complex and increased catalytic redox potentials relevant to bio-H(2) oxidation.
متن کاملHydrogen metabolism in the hyperthermophilic bacterium Aquifex aeolicus.
Aquifex aeolicus is a microaerophilic, hydrogen-oxidizing, hyperthermophilic bacterium containing three [NiFe] hydrogenases. Two of these three enzymes (one membrane-bound and one soluble) have been purified and characterized. The Aquifex hydrogenases are thermostable and tolerant to oxygen. A cellular function for the three hydrogenases has been proposed. The two membrane-bound periplasmic hyd...
متن کاملExpression, refolding and crystallization of Aquifex aeolicus elongation factor P.
Elongation factor P is a universally conserved protein stimulating peptidyltransferase activity during protein synthesis. The factor is sensitive to classical inhibitors of the ribosomal peptidyltransferase activity and is possibly involved in alignment of the substrate tRNAs in the catalytic centre of 70S ribosomes. Elongation factor P from the thermophilic Aquifex aeolicus was overexpressed a...
متن کاملInvestigation on the causes of codon and amino acid usages variation between thermophilic Aquifex aeolicus and mesophilic Bacillus subtilis.
Base composition, codon usages and amino acid usages have been analyzed by taking 529 orthologous sequences of Aquifex aeolicus and Bacillus subtilis, having different optimal growth temperatures. These two bacteria do not have significant difference in overall GC composition, but GC(1+2) and GC3 levels were found to vary significantly. Significant increments in purine content and GC3 compositi...
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