Characterization of a homogeneous arginyl- and lysyl-tRNA synthetase complex isolated from rat liver: arginyl- and lysyl-tRNA synthetases contain carbohydrates

Biochemistry ◽  
1982 ◽  
Vol 21 (20) ◽  
pp. 4891-4895 ◽  
Author(s):  
Chuan Van Dang ◽  
Thomas P. Mawhinney ◽  
Richard H. Hilderman
Keyword(s):  
Rat Liver ◽  
Trna Synthetase ◽  
Trna Synthetases

Functional characterization of leucine-specific domain 1 from eukaryal and archaeal leucyl-tRNA synthetases

2010 ◽  
Vol 429 (3) ◽  
pp. 505-513 ◽  
Author(s):  
Xiao-Long Zhou ◽  
Meng Wang ◽  
Min Tan ◽  
Qian Huang ◽  
Gilbert Eriani ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Trna Synthetase ◽  
Acid Activation ◽  
Reaction Step ◽  
Specific Domain ◽  
Binding Strength ◽  
Trna Synthetases ◽  
Amino Acid Activation ◽  
Common Domain

LeuRS (leucyl-tRNA synthetase) catalyses the esterification of tRNAsLeu with leucine. This family of enzymes is divided into prokaryotic and eukaryal/archaeal groups according to the presence and position of specific insertions and extensions. In the present study, we investigated the function of LSD1 (leucine-specific domain 1), which is naturally present in eukaryal/archaeal LeuRSs, but absent from prokaryotic LeuRSs. When mutated in their common domain, the eukaryal and archaeal LeuRSs exhibited defects in the first reaction step of amino acid activation with variations of leucine or ATP-binding strength, whereas the tRNA aminoacylation was moderately affected. When the eukaryal extension was mutated, severe tRNA charging defects were observed, suggesting that eukaryotes evolved this LSD1 extension in order to improve the aminoacylation reaction step. The results also showed that the LSD1s from organisms of both groups are dispensable for post-transfer editing. Together, the data provide us with a further understanding of the organization and structure of LeuRS domains.

Physical and biochemical characterization of a purified arginyl- and lysyl-tRNA synthetase complex from rat liver

Biochemistry ◽  
1982 ◽  
Vol 21 (8) ◽  
pp. 1959-1966 ◽  
Author(s):  
Chuan Van Dang ◽  
Raymant L. Glinski ◽  
Philip C. Gainey ◽  
Richard H. Hilderman
Keyword(s):  
Rat Liver ◽  
Biochemical Characterization ◽  
Trna Synthetase

scholarly journals Virus-Encoded Aminoacyl-tRNA Synthetases: Structural and Functional Characterization of Mimivirus TyrRS and MetRS

2007 ◽  
Vol 81 (22) ◽  
pp. 12406-12417 ◽  
Author(s):  
Chantal Abergel ◽  
Joëlle Rudinger-Thirion ◽  
Richard Giegé ◽  
Jean-Michel Claverie
Keyword(s):  
Active Site ◽  
Functional Characterization ◽  
Evolutionary Relationship ◽  
Trna Synthetase ◽  
Dna Viruses ◽  
Trna Synthetases ◽  
Functional Studies ◽  
Aminoacyl Trna Synthetases ◽  
Viral Enzyme

ABSTRACT Aminoacyl-tRNA synthetases are pivotal in determining how the genetic code is translated in amino acids and in providing the substrate for protein synthesis. As such, they fulfill a key role in a process universally conserved in all cellular organisms from their most complex to their most reduced parasitic forms. In contrast, even complex viruses were not found to encode much translation machinery, with the exception of isolated components such as tRNAs. In this context, the discovery of four aminoacyl-tRNA synthetases encoded in the genome of mimivirus together with a full set of translation initiation, elongation, and termination factors appeared to blur what was once a clear frontier between the cellular and viral world. Functional studies of two mimivirus tRNA synthetases confirmed the MetRS specificity for methionine and the TyrRS specificity for tyrosine and conformity with the identity rules for tRNATyr for archea/eukarya. The atomic structure of the mimivirus tyrosyl-tRNA synthetase in complex with tyrosinol exhibits the typical fold and active-site organization of archaeal-type TyrRS. However, the viral enzyme presents a unique dimeric conformation and significant differences in its anticodon binding site. The present work suggests that mimivirus aminoacyl-tRNA synthetases function as regular translation enzymes in infected amoebas. Their phylogenetic classification does not suggest that they have been acquired recently by horizontal gene transfer from a cellular host but rather militates in favor of an intricate evolutionary relationship between large DNA viruses and ancestral eukaryotes.

scholarly journals Characterization of an Inducible, Antibiotic-Resistant Aminoacyl-tRNA Synthetase Gene in Streptomyces coelicolor

2008 ◽  
Vol 190 (18) ◽  
pp. 6253-6257 ◽  
Author(s):  
James J. Vecchione ◽  
Jason K. Sello
Keyword(s):  
Streptomyces Coelicolor ◽  
Trna Synthetase ◽  
Aminoacyl Trna Synthetase ◽  
Antibiotic Resistant ◽  
Trna Synthetases ◽  
Genes Encoding

ABSTRACT Streptomyces coelicolor has two genes encoding tryptophanyl-tRNA synthetases, one of which (trpRS1) is resistant to and transcriptionally activated by indolmycin. We found that this gene also confers resistance to chuangxinmycin (another antibiotic that inhibits bacterial tryptophanyl-tRNA synthetases) and that its transcription is not absolutely dependent on either antibiotic.

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