A retroviral-like metal binding motif in an aminoacyl-tRNA synthetase is important for tRNA recognition.
نویسندگان
چکیده
منابع مشابه
Aminoacyl-tRNA synthetase-induced cleavage of tRNA.
Aminoacyl-tRNA synthetases interact with their cognate tRNAs in a highly specific fashion. We have examined the phenomenon that upon complex formation E. coli glutaminyl-tRNA synthetase destabilizes tRNA(Gln) causing chain scissions in the presence of Mg2+ ions. The phosphodiester bond cleavage produces 3'-phosphate and 5'-hydroxyl ends. This kind of experiment is useful for detecting conformat...
متن کاملCoevolution of an aminoacyl-tRNA synthetase with its tRNA substrates.
Glutamyl-tRNA synthetases (GluRSs) occur in two types, the discriminating and the nondiscriminating enzymes. They differ in their choice of substrates and use either tRNAGlu or both tRNAGlu and tRNAGln. Although most organisms encode only one GluRS, a number of bacteria encode two different GluRS proteins; yet, the tRNA specificity of these enzymes and the reason for such gene duplications are ...
متن کاملMutation in Aminoacyl Trna Synthetase 1 In Autosomal Recessive Intellectual Disability
Background: Intellectual disability (ID) is one of the most common neurodevelopment disorders that caused by both environment and genetic factors. Also genetic defects have involving for approximately 50% of ID etiology, it is demonstrated that genetics play significant role in ID development. The important risk factor in most country in ID is consanguinity marriage. Iran has high frequency of ...
متن کاملPyrrolysyl-tRNA synthetase, an aminoacyl-tRNA synthetase for genetic code expansion.
Genetic code expansion (GCE) has become a central topic of synthetic biology. GCE relies on engineered aminoacyl-tRNA synthetases (aaRSs) and a cognate tRNA species to allow codon reassignment by co-translational insertion of non-canonical amino acids (ncAAs) into proteins. Introduction of such amino acids increases the chemical diversity of recombinant proteins endowing them with novel propert...
متن کاملA truncated aminoacyl-tRNA synthetase modifies RNA.
Aminoacyl-tRNA synthetases are modular enzymes composed of a central active site domain to which additional functional domains were appended in the course of evolution. Analysis of bacterial genome sequences revealed the presence of many shorter aminoacyl-tRNA synthetase paralogs. Here we report the characterization of a well conserved glutamyl-tRNA synthetase (GluRS) paralog (YadB in Escherich...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1992
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.89.6.2032