pHRS7-Histidyl-tRNA Synthetase (E.coli)

This plasmid expresses the full length E. coli Histidyl-tRNA synthetase.

Histidyl-tRNA synthetases attach amino acids to the 3' ends of their cognate transfer RNAs in a two-step reaction catalyzed by ATP. The accuracy of this reaction is crucial for the overall fidelity of protein synthesis.

From the laboratory of Christopher S. Francklyn, PhD, University of Vermont.

The Investigator's AnnexePart of The Investigator's Annexe program.

Catalog Number Product Size AVAILABILITY Price Qty
EVM104
pHRS7-Histidyl-tRNA Synthetase (E.coli)
Spotted on filter paper In stock
Regular Price:$404.00
Specifications

Product Type: Plasmid
Name: Histidine tRNA Synthetase
Organism: E. coli
Antibiotic Resistance: Ampicillin
Fusion Tag(s): None
Grow in E. coli at 37 C: Yes
Cloning Site 5': NcoI
Cloning Site 3': BamHI
5' Sequencing Primer: 1272 bp
3' Sequencing Primer: pTRC99, 4167 bp
Insert Size: High
Shipped: Ambient temperature (Liquid plasmid DNA in water for domestic orders, spotted on filter paper for international orders)

Provider
From the laboratory of Christopher S. Francklyn, PhD, University of Vermont.
References
  1. Yan, W. and Francklyn, C. Cytosine 73 is a discriminator nucleotide in vivo for histidyl-tRNA in Escherchia coli. Journal of Biological Chemistry, 269:13, 10022-10027 (1994).
  2. Bovee, M.L., Yan, W., Sproat, B.S.,  and Francklyn, C.S. tRNA discrimination at the binding step by a class II aminoacyl-tRNA synthetase. Biochemistry, 38: 41, 13725-13735 (1999).
  3. Arnez, J.G., Harris, D.C., Mitschler, A., Reese, B., Francklyn, C.S., and Moras, D.  Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate. EMBO Journal, 14:17, 4143-4155 (1995).
  4. Yan, W., Augustine, J., and Francklyn, C. A tRNA identity switch mediated by the binding interaction between a tRNA anticodon and the accessory domain of a class II aminoacyl-tRNA synthetase. Biochemistry, 35:21, 6559-6568 (1996).
  5. Arnez, J.G., Augustine, J.G., Moras, D., and Francklyn, C. The first step of aminoacylation at the atomic level in histidyl-tRNA synthase.  PNAS, 94, 7144-7149 (1997).
  6. Francklyn, C., Adams, J., and Augustine, J. Catalytic defects in mutants of class II histidyl-tRNA synthetase from Salmonella typhimurium previously linked to decreased control of histidine biosynthesis regulation.  Journal of Molecular Biology, 280, 847-858 (1998).
  7. Francklyn, C., Musier-Forsyth, K., and Martinis, S.A. Aminoacyl-tRNA synthetases in biology and disease: new evidence for structural and functional diversity in an ancient family of enzymes  RNA, 3, 945-960 (1997).
  8. Hawko, S.A., and Francklyn, C.S. Covariation of a specificity-determining structural motif in an aminoacyl-tRNA synthetase and a tRNA identity element. Biochemistry, 40:7, 1930-1936 (2001).
  9. Connoly, S.A., Rosen, A.E.,  Musier-Forsyth, K., and Francklyn, C.S. G-1:C73 recognition by an arginine cluster in the active site of Escherichia coli histidyl-tRNA synthetase.  Biochemistry, 43: 4, 962-969 (2004).
  10. Guth, E., Connoly, S.H., Bovee, M., and Francklyn, C.S. A substrate-assisted concerted mechanism for aminoacylation by a class II aminoacyl-tRNA synthetase. Biochemistry, 44:10, 3785-3794 (2005)
  11. Guth, E. and Francklyn, C.S. Kinetic discrimination of tRNA identity by the conserved motif 2 loop of a class II aminoacyl-tRNA synthetase. Molecular Cell, 25, 531-542 (2007).

If you publish research with this product, please let us know so we can cite your paper.

Loading...