The bacterial YbaK protein is a Cys-tRNAPro and Cys-tRNA Cys deacylase

scientific article

The bacterial YbaK protein is a Cys-tRNAPro and Cys-tRNA Cys deacylase is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1074/JBC.M502174200
P698PubMed publication ID15886196

P2093author name stringDieter Söll
Benfang Ruan
P433issue27
P407language of work or nameEnglishQ1860
P921main subjectCys-tRNA(Pro) hydrolase activityQ22320425
P304page(s)25887-25891
P577publication date2005-05-10
P1433published inJournal of Biological ChemistryQ867727
P1476titleThe bacterial YbaK protein is a Cys-tRNAPro and Cys-tRNA Cys deacylase
P478volume280

Reverse relations

cites work (P2860)
Q28244233A genetic approach for finding small RNAs regulators of genes of interest identifies RybC as regulating the DpiA/DpiB two-component system
Q27972876A genomic glimpse of aminoacyl-tRNA synthetases in malaria parasite Plasmodium falciparum
Q37469532A multiple aminoacyl-tRNA synthetase complex that enhances tRNA-aminoacylation in African trypanosomes
Q41500207A present-day aminoacyl-tRNA synthetase with ancestral editing properties
Q34226243Amino-acid-dependent shift in tRNA synthetase editing mechanisms
Q36696214Aminoacyl-tRNA substrate and enzyme backbone atoms contribute to translational quality control by YbaK
Q36973475Aminoacyl-tRNA synthetase complexes: molecular multitasking revealed
Q34536872An archaeal tRNA-synthetase complex that enhances aminoacylation under extreme conditions
Q35451324Ancestral AlaX editing enzymes for control of genetic code fidelity are not tRNA-specific
Q39095907Borrelidin, a potent antimalarial: stage-specific inhibition profile of synchronized cultures of Plasmodium falciparum
Q34884208CP1-dependent partitioning of pretransfer and posttransfer editing in leucyl-tRNA synthetase
Q34209500Characterization of benzoxaborole-based antifungal resistance mutations demonstrates that editing depends on electrostatic stabilization of the leucyl-tRNA synthetase editing cap.
Q47998651Conformational and chemical selection by a trans-acting editing domain.
Q46640850Cys-tRNA(Pro) editing by Haemophilus influenzae YbaK via a novel synthetase.YbaK.tRNA ternary complex
Q34200440Cysteinyl-tRNA deacylation can be uncoupled from protein synthesis
Q24673381Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins from an ancient and the modern pathways of aminoacyl-tRNA formation
Q41862315Discovery and investigation of misincorporation of serine at asparagine positions in recombinant proteins expressed in Chinese hamster ovary cells
Q37680392Distinct tRNA recognition strategies used by a homologous family of editing domains prevent mistranslation
Q38088164Emergence and evolution
Q28552724Essentiality Assessment of Cysteinyl and Lysyl-tRNA Synthetases of Mycobacterium smegmatis
Q36850329Exclusive use of trans-editing domains prevents proline mistranslation
Q38260221Exploring the evolutionary diversity and assembly modes of multi-aminoacyl-tRNA synthetase complexes: lessons from unicellular organisms
Q46113351Fluorothreonyl-tRNA deacylase prevents mistranslation in the organofluorine producer Streptomyces cattleya
Q34253805Halofuginone and other febrifugine derivatives inhibit prolyl-tRNA synthetase
Q36502043In vitro assays for the determination of aminoacyl-tRNA synthetase editing activity
Q27676516Leucyl-tRNA synthetase editing domain functions as a molecular rheostat to control codon ambiguity in Mycoplasma pathogens
Q27930245Loss of editing activity during the evolution of mitochondrial phenylalanyl-tRNA synthetase.
Q34186873Naturally occurring aminoacyl-tRNA synthetases editing-domain mutations that cause mistranslation in Mycoplasma parasites
Q48358169Quality control by trans-editing factor prevents global mistranslation of non-protein amino acid α-aminobutyrate
Q35844603Restoring species-specific posttransfer editing activity to a synthetase with a defunct editing domain
Q93003081Stoichiometry of triple-sieve tRNA editing complex ensures fidelity of aminoacyl-tRNA formation
Q38741646Strictly conserved lysine of prolyl-tRNA Synthetase editing domain facilitates binding and positioning of misacylated tRNA(Pro.).
Q27694602Structural and functional analysis of the anti-malarial drug target prolyl-tRNA synthetase
Q30636920Structural basis for full-spectrum inhibition of translational functions on a tRNA synthetase
Q42203083Substrate and enzyme functional groups contribute to translational quality control by bacterial prolyl-tRNA synthetase
Q35728198Substrate specificity of bacterial prolyl-tRNA synthetase editing domain is controlled by a tunable hydrophobic pocket
Q35213173Substrate-mediated fidelity mechanism ensures accurate decoding of proline codons
Q38383986Synthetic biology approaches to biological containment: pre-emptively tackling potential risks
Q33810666The balance between pre- and post-transfer editing in tRNA synthetases
Q46819076Transfer RNA modulates the editing mechanism used by class II prolyl-tRNA synthetase
Q38132082Transfer RNA: a dancer between charging and mis-charging for protein biosynthesis
Q34476623Unusual domain architecture of aminoacyl tRNA synthetases and their paralogs from Leishmania major
Q37480875tRNAs: cellular barcodes for amino acids.

Search more.