Leucine-specific domain modulates the aminoacylation and proofreading functional cycle of bacterial leucyl-tRNA synthetase. 2013

Wei Yan, and Min Tan, and Gilbert Eriani, and En-Duo Wang
State Key Laboratory of Molecular Biology, Center for RNA Research, Institute of Biochemistry and Cell Biology, the Chinese Academy of Sciences, 320 Yue Yang Road, Shanghai 200031, PR China.

The leucine-specific domain (LSD) is a compact well-ordered module that participates in positioning of the conserved KMSKS catalytic loop in most leucyl-tRNA synthetases (LeuRSs). However, the LeuRS from Mycoplasma mobile (MmLeuRS) has a tetrapeptide GKDG instead of the LSD. Here, we show that the tetrapeptide GKDG can confer tRNA charging and post-transfer editing activity when transplanted into an inactive Escherichia coli LeuRS (EcLeuRS) that has had its LSD deleted. Reciprocally, the LSD, together with the CP1-editing domain of EcLeuRS, can cooperate when inserted into the scaffold of the minimal MmLeuRS, and this generates an enzyme nearly as active as EcLeuRS. Further, we show that LSD participates in tRNA(Leu) recognition and favours the binding of tRNAs harbouring a large loop in the variable arm. Additional analysis established that the Lys598 in the LSD is the critical residue for tRNA binding. Conversion of Lys598 to Ala simultaneously reduces the tRNA-binding strength and aminoacylation and editing capacities, indicating that these factors are subtly connected and controlled at the level of the LSD. The present work provides a novel framework of co-evolution between LeuRS and its cognate tRNA through LSD.

UI MeSH Term Description Entries
D007935 Leucine-tRNA Ligase An enzyme that activates leucine with its specific transfer RNA. EC 6.1.1.4. Leucyl T RNA Synthetase,Leu-tRNA Ligase,Leucine-tRNA Synthetase,Leu tRNA Ligase,Leucine tRNA Ligase,Leucine tRNA Synthetase,Ligase, Leu-tRNA,Ligase, Leucine-tRNA,Synthetase, Leucine-tRNA
D008239 Lysine An essential amino acid. It is often added to animal feed. Enisyl,L-Lysine,Lysine Acetate,Lysine Hydrochloride,Acetate, Lysine,L Lysine
D009154 Mutation Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations. Mutations
D009174 Mycoplasma A genus of gram-negative, mostly facultatively anaerobic bacteria in the family MYCOPLASMATACEAE. The cells are bounded by a PLASMA MEMBRANE and lack a true CELL WALL. Its organisms are pathogens found on the MUCOUS MEMBRANES of humans, ANIMALS, and BIRDS. Eperythrozoon,Haemobartonella,Mycoplasma putrefaciens,PPLO,Pleuropneumonia-Like Organisms,Pleuropneumonia Like Organisms
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D001426 Bacterial Proteins Proteins found in any species of bacterium. Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial
D012356 RNA, Transfer, Leu A transfer RNA which is specific for carrying leucine to sites on the ribosomes in preparation for protein synthesis. Leucine-Specific tRNA,Transfer RNA, Leu,tRNALeu,tRNA(Leu),Leu Transfer RNA,Leucine Specific tRNA,RNA, Leu Transfer,tRNA, Leucine-Specific
D013379 Substrate Specificity A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts. Specificities, Substrate,Specificity, Substrate,Substrate Specificities
D017393 RNA Editing A process that changes the nucleotide sequence of mRNA from that of the DNA template encoding it. Some major classes of RNA editing are as follows: 1, the conversion of cytosine to uracil in mRNA; 2, the addition of variable number of guanines at pre-determined sites; and 3, the addition and deletion of uracils, templated by guide-RNAs (RNA, GUIDE, KINETOPLASTIDA). RNA, Messenger, Editing,Editing, RNA,Editings, RNA,RNA Editings
D017434 Protein Structure, Tertiary The level of protein structure in which combinations of secondary protein structures (ALPHA HELICES; BETA SHEETS; loop regions, and AMINO ACID MOTIFS) pack together to form folded shapes. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Tertiary Protein Structure,Protein Structures, Tertiary,Tertiary Protein Structures

Related Publications

Wei Yan, and Min Tan, and Gilbert Eriani, and En-Duo Wang
June 2012, Nature structural & molecular biology,
Wei Yan, and Min Tan, and Gilbert Eriani, and En-Duo Wang
December 2006, Biochemistry,
Wei Yan, and Min Tan, and Gilbert Eriani, and En-Duo Wang
August 2010, The Biochemical journal,
Wei Yan, and Min Tan, and Gilbert Eriani, and En-Duo Wang
August 2006, The Journal of biological chemistry,
Wei Yan, and Min Tan, and Gilbert Eriani, and En-Duo Wang
February 2013, Nucleic acids research,
Wei Yan, and Min Tan, and Gilbert Eriani, and En-Duo Wang
June 1977, Proceedings of the National Academy of Sciences of the United States of America,
Wei Yan, and Min Tan, and Gilbert Eriani, and En-Duo Wang
April 2007, Biochemistry,
Wei Yan, and Min Tan, and Gilbert Eriani, and En-Duo Wang
October 1986, European journal of biochemistry,
Wei Yan, and Min Tan, and Gilbert Eriani, and En-Duo Wang
December 2011, The Biochemical journal,
Wei Yan, and Min Tan, and Gilbert Eriani, and En-Duo Wang
January 2003, Journal of protein chemistry,
Copied contents to your clipboard!