Disease relevance of hisS

• The entire nucleotide sequence of the Escherichia coli hisS locus was determined [1].
• The crystal structure of the Staphylococcus aureus histidyl-tRNA synthetase apoprotein has been determined at 2.7 A resolution [2].

High impact information on hisS

• The amino acid sequences of Escherichia coli histidyl-tRNA synthetase and alanyl-tRNA synthetase, two proteins recently identified as autoantigens in polymyositis, were compared by a computer alignment procedure with those of the 3600 proteins tabulated in the National Biomedical Research Foundation protein sequence database [3].
• Herein, we describe a class of aminoacyl-tRNA synthetase-like (HisZ) proteins based on the catalytic core of the contemporary class II histidyl-tRNA synthetase whose members lack aminoacylation activity but are instead essential components of the first enzyme in histidine biosynthesis ATP phosphoribosyltransferase (HisG) [4].
• The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase [5].
• The crystal structure of an enzyme-substrate complex with histidyl-tRNA synthetase from Escherichia coli, ATP, and the amino acid analog histidinol is described and compared with the previously obtained enzyme-product complex with histidyl-adenylate [5].
• Crystals of the complex containing histidyl-tRNA synthetase, ATP and histidine have been grown by vapor diffusion against reservoirs containing 0.1 M Tris (pH 7.4), 0.5 M NaCl and 10% polyethylene glycol 6000 [6].

Chemical compound and disease context of hisS

• Histidyl-tRNA synthetase from Escherichia coli was over-expressed and purified by Q Sepharose and hydroxyapatite chromatography [6].
• G-1:C73 recognition by an arginine cluster in the active site of Escherichia coli histidyl-tRNA synthetase [7].
• These identity conversions mediated by the G-1.C73 base pair were exploited to isolate secondary site revertants in the histidyl-tRNA synthetase from E. coli which restore histidine identity to a histidyl-tRNA suppressor carrying U73 [8].
• Recent affinity labeling studies have revealed that dimeric histidyl-tRNA synthetase from Escherichia coli displayed half-of-the-sites reactivity toward labeling with pyridoxal 5'-phosphate [Kalogerakos, T., Hountondji, C., Berne, P. F., Dutka, S. & Blanquet, S. (1994) Biochimie (Paris) 76, 33-44] [9].

Biological context of hisS

• A plasmid has been constructed which carries hisS, the structural gene for histidyl-RNA synthetase of E. coli, on a 1.6-kb fragment bounded by PvuII and BstEII sites [10].
• The gene ssyA was mapped at a new locus between hisS and glyA on the chromosome [11].
• A dynamic and cooperative active site is most likely necessary for the proper functioning of the histidyl-tRNA synthetase, and suggests a novel mechanism for improving charging fidelity [2].
• In Escherichia coli, the aminoacylation of tRNA(His) by histidyl-tRNA synthetase (HisRS) is highly dependent upon the recognition of the unique G-1:C73 base pair and the 5'-monophosphate [7].
• In this study, two chemically synthesized 24-nucleotide RNA microhelices, each of which recapitulates the acceptor stem of either E. coli or Saccharomyces cervisiae tRNAHis, were used to facilitate an atomic group "mutagenesis" study of the -1:73 base pair recognition by S. cerevisiae HisRS [12].

Other interactions of hisS

• The probable transcription terminator of gcpE overlaps the hisS promoter [13].
• These include tRNA-modifying enzymes, the histidyl-tRNA synthetase, and the hisG enzyme [14].
• This vector family has been successfully used for the expression and purification of the isoleucyl-tRNA synthetase from Saccharomyces cerevisiae and the histidyl-tRNA synthetase from E. coli [15].

Analytical, diagnostic and therapeutic context of hisS

• Crystallization of histidyl-tRNA synthetase from Escherichia coli [6].
• Affinity labeling of Escherichia coli histidyl-tRNA synthetase with reactive ATP analogues. Identification of labeled amino acid residues by matrix assisted laser desorption-ionization mass spectrometry [9].

References