Catalytic defects in mutants of class II histidyl-tRNA synthetase from Salmonella typhimurium previously linked to decreased control of histidine biosynthesis regulation 1 1Edited by D. Draper

Francklyn, Christopher S.; Adams, J.R.; Augustine, John

doi:10.1006/jmbi.1998.1902

Cited by 16 publications

(21 citation statements)

References 56 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…As shown in Table 1, the kinetic parameters for pyrophosphate exchange were as follows: K M His = 9.0 6 1 mM; k cat = 40 6 9 sec ÿ1 ; K M ATP = 500 6 94 mM. In comparison to the values for the E. coli enzyme reported previously (Augustine and Francklyn 1997;Francklyn et al 1998), the yeast enzyme has an approximately threefold lower K M (histidine), and k cat is also reduced threefold (Table 1). This analysis suggests that the yeast enzyme purified from bacterial sources retains full activity, allowing further studies of its tRNA specificity.…”

Section: Initial Characterization Of Yeast Hisrsmentioning

confidence: 69%

See 1 more Smart Citation

Evolutionary conservation of a functionally important backbone phosphate group critical for aminoacylation of histidine tRNAs

Rosen¹,

Brooks²,

Guth³

et al. 2006

RNA

View full text Add to dashboard Cite

All histidine tRNA molecules have an extra nucleotide, G-1, at the 59 end of the acceptor stem. In bacteria, archaea, and eukaryotic organelles, G-1 base pairs with C73, while in eukaryotic cytoplasmic tRNA His , G-1 is opposite A73. Previous studies of Escherichia coli histidyl-tRNA synthetase (HisRS) have demonstrated the importance of the G-1:C73 base pair to tRNA His identity. Specifically, the 59-monophosphate of G-1 and the major groove amine of C73 are recognized by E. coli HisRS; these individual atomic groups each contribute ; ;4 kcal/mol to transition state stabilization. In this study, two chemically synthesized 24-nucleotide RNA microhelices, each of which recapitulates the acceptor stem of either E. coli or Saccharomyces cervisiae tRNA His , were used to facilitate an atomic group ''mutagenesis'' study of the ÿ1:73 base pair recognition by S. cerevisiae HisRS. Compared with E. coli HisRS, microhelixHis is a much poorer substrate relative to full-length tRNA His for the yeast enzyme. However, the data presented here suggest that, similar to the E. coli system, the 59 monophosphate of yeast tRNA His is critical for aminoacylation by yeast HisRS and contributes ; ;3 kcal/mol to transition state stability. The primary role of the unique ÿ1:73 base pair of yeast tRNA His appears to be to properly position the critical 59 monophosphate for interaction with the yeast enzyme. Our data also suggest that the eukaryotic HisRS/tRNA His interaction has coevolved to rely less on specific major groove interactions with base atomic groups than the bacterial system.

show abstract

Section: Initial Characterization Of Yeast Hisrsmentioning

confidence: 69%

“…The protocol for this assay was described previously (Francklyn et al 1998) and was used without modification. Reactions were initiated by the addition of yeast HisRS to a final concentration of 8.2 nM.…”

Section: Pyrophosphate Exchange and Aminoacylation Assaysmentioning

confidence: 99%

Evolutionary conservation of a functionally important backbone phosphate group critical for aminoacylation of histidine tRNAs

Rosen¹,

Brooks²,

Guth³

et al. 2006

RNA

View full text Add to dashboard Cite

show abstract

“…The latter two ranges for the Michaelis constants are remarkably large for unknown reasons; a possible explanation would be that the values were obtained over a wide pH range. The K m values of the ATP/PP i exchange reaction are between (Yan et al, 1996;Augustine and Francklyn, 1997;Rühlmann et al, 1997;Francklyn et al, 1998). The enzyme from rabbit reticulocytes shows a turnover of 84 min -1 (= 1.4 s -1 ) and has an isoelectric point of 5.1 (Kane et al, 1978).…”

Section: Mechanism Of Enzyme Actionmentioning

confidence: 99%

“…The resulting loss/drop of HisRS activity may reduce the cellular concentration of cyclin D1, resulting in a G1 arrest. In addition, some of the mutant HisRS linked to decreased control of histidine biosynthesis isolated from S. typhimurium by Roth, Ames and coworkers have recently been biochemically characterized in light of the three-dimensional structural information, linking some critical interactions in the active center of HisRS and regulation of histidine biosynthesis (Francklyn et al, 1998).…”

Section: Histidyl-trna Synthetase Genesmentioning

confidence: 99%

“…There are structural similarities to tRNA His in the promoter sequences of the HisRS gene transcript from E. coli (Freedman et al, 1985) and in the leader region of that from S. typhimurium (Ames et al, 1983). The cellular levels of tRNA His , His-tRNA His (McGinnis and Williams, 1972a, b;Lewis and Ames, 1972;Francklyn et al, 1998) and HisRS Brenner et al, 1972;Wyche et al, 1974;Coleman and Williams, 1974) have been identified as important regulatory parameters in S. typhimurium. The GCN2 protein, which contains sequences homologous to histidyl-tRNA synthetases and protein kinases, stimulates the expression of amino acid biosynthetic genes under conditions of amino acid starvation in S. cerevisiae (Wek et al, 1989(Wek et al, , 1990(Wek et al, , 1995Zhu et al, 1996).…”

Section: Histidyl-trna Synthetase Genesmentioning

confidence: 99%

See 1 more Smart Citation

Histidyl-tRNA Synthetase

Freist¹,

Jf²,

Rühlmann³

et al. 1999

Biological Chemistry

View full text Add to dashboard Cite

Histidyl-tRNA synthetase (HisRS) is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. This amino acid has uniquely moderate basic properties and is an important group in many catalytic functions of enzymes.A compilation of currently known primary structures of HisRS shows that the subunits of these homodimeric enzymes consist of 420 -550 amino acid residues. This represents a relatively short chain length among aminoacyl-tRNA synthetases (aaRS), whose peptide chain sizes range from about 300 to 1100 amino acid residues.The crystal structures of HisRS from two organisms and their complexes with histidine, histidyl-adenylate and histidinol with ATP have been solved. HisRS from Escherichia coli and Thermus thermophilus are very similar dimeric enzymes consisting of three domains: the N-terminal catalytic domain containing the sixstranded antiparallel ␤-sheet and the three motifs characteristic of class II aaRS, a HisRS-specific helical domain inserted between motifs 2 and 3 that may contact the acceptor stem of the tRNA, and a C-terminal ␣/␤ domain that may be involved in the recognition of the anticodon stem and loop of tRNA His .The aminoacylation reaction follows the standard two-step mechanism. HisRS also belongs to the group of aaRS that can rapidly synthesize diadenosine tetraphosphate, a compound that is suspected to be involved in several regulatory mechanisms of cell metabolism. Many analogs of histidine have been tested for their properties as substrates or inhibitors of HisRS, leading to the elucidation of structure-activity relationships concerning configuration, importance of the carboxy and amino group, and the nature of the side chain.HisRS has been found to act as a particularly important antigen in autoimmune diseases such as rheumatic arthritis or myositis. Successful attempts have been made to identify epitopes responsible for the complexation with such auto-antibodies.

show abstract

Sequencing, Characterization, and Gene Expression Analysis of the Histidine Decarboxylase Gene Cluster of Morganella morganii

et al. 2013

View full text Add to dashboard Cite

The histidine decarboxylase gene cluster of Morganella morganii DSM30146(T) was sequenced, and four open reading frames, named hdcT1, hdc, hdcT2, and hisRS were identified. Two putative histidine/histamine antiporters (hdcT1 and hdcT2) were located upstream and downstream the hdc gene, codifying a pyridoxal-P dependent histidine decarboxylase, and followed by hisRS gene encoding a histidyl-tRNA synthetase. This organization was comparable with the gene cluster of other known Gram negative bacteria, particularly with that of Klebsiella oxytoca. Recombinant Escherichia coli strains harboring plasmids carrying the M. morganii hdc gene were shown to overproduce histidine decarboxylase, after IPTG induction at 37 °C for 4 h. Quantitative RT-PCR experiments revealed the hdc and hisRS genes were highly induced under acidic and histidine-rich conditions. This work represents the first description and identification of the hdc-related genes in M. morganii. Results support the hypothesis that the histidine decarboxylation reaction in this prolific histamine producing species may play a role in acid survival. The knowledge of the role and the regulation of genes involved in histidine decarboxylation should improve the design of rational strategies to avoid toxic histamine production in foods.

show abstract

Catalytic defects in mutants of class II histidyl-tRNA synthetase from Salmonella typhimurium previously linked to decreased control of histidine biosynthesis regulation 1 1Edited by D. Draper

Cited by 16 publications

References 56 publications

Evolutionary conservation of a functionally important backbone phosphate group critical for aminoacylation of histidine tRNAs

Evolutionary conservation of a functionally important backbone phosphate group critical for aminoacylation of histidine tRNAs

Histidyl-tRNA Synthetase

Sequencing, Characterization, and Gene Expression Analysis of the Histidine Decarboxylase Gene Cluster of Morganella morganii

Contact Info

Product

Resources

About