Purification and some properties of the histidyl-tRNA synthetase from the cytosol of rabbit reticulocytes

Kane, Sherwin M.; Vugrincic, Cedomil; Finbloom, D S; Smith, David W.

doi:10.1021/bi00601a024

Cited by 36 publications

(12 citation statements)

References 41 publications

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“…Eusebe-Carre, and from baker's yeast (13) by H. Sternbach (Max-Planck-Institut fur Experimentelle Medizin, Gottingen). Partially purified sheep liver histidyl-tRNA synthetase was a gift from J.P. Waller and M. Mirande (Ecole Polytechnique, Palaiseau); the enzyme was further purified by successive chromatography (14) on DEAE-cellulose (Whatman) and phosphocellulose (Whatman). RNase Ti was from Sankyo, alkaline phosphatase from Sigma, and bovine serum albumin from Bethesda Research Laboratories.…”

Section: Methodsmentioning

confidence: 99%

Conformational requirements of tobacco mosaic virus RNA for aminoacylation and adenylation

Joshi¹,

Chapeville²,

Haenni³

1985

Nucl Acids Res

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The RNA conformational requirements for both aminoacylation and adenylation emerging from our studies performed using the valine- and the tyrosine-accepting plant viral RNAs are now strongly supported by the histidine-accepting tobacco mosaic virus RNA: an 'L'-shaped conformation is recognized by the aminoacyl-tRNA synthetase whereas only the aminoacyl RNA domain (equivalent in tRNAs to the continuous helix formed by the acceptor stem and the T stem and loop) interacts with the tRNA nucleotidyltransferase.

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Section: Methodsmentioning

confidence: 99%

Conformational requirements of tobacco mosaic virus RNA for aminoacylation and adenylation

Joshi¹,

Chapeville²,

Haenni³

1985

Nucl Acids Res

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“…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). HisRS can form diadenosine polyphosphates in a side reaction under physiological conditions.…”

Section: Mechanism Of Enzyme Actionmentioning

confidence: 99%

Histidyl-tRNA Synthetase

Freist¹,

Jf²,

Rühlmann³

et al. 1999

Biological Chemistry

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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.

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“…Numerous enzymes listed in table 1 have been described as migrating as a single population of molecules in focusing experiments (e.g., [28, [31][32][33]35,36,39,40,42,48]). …”

Section: Resultsmentioning

confidence: 99%

Isoelectric focusing and isoelectric points of aminoacyl‐tRNA synthetases

Lorber

Giegé

1983

FEBS Letters

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Isoelectric points and isoelectric focusing behaviour of 10 highly purified eukaryotic aminoacyl-tRNA synthetases from 3 sources, Saccharomyces cerevisiue, Euglena gracilis and Phaseolus vulgaris were examined. The PI-values measured on polyacrylamide gels under native conditions are situated between pH 5.0-7.5. A microheterogeneity was observed for 9 enzymes appearing otherwise homogeneous on gel electrophoresis. A compilation of the isoelectric points of aminoacyl-tRNA synthetases is given and literature data are compared with our experimental results. Aminoacyl-tRNA synthetase Isoelectric focusing

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Purification and some properties of the histidyl-tRNA synthetase from the cytosol of rabbit reticulocytes

Cited by 36 publications

References 41 publications

Conformational requirements of tobacco mosaic virus RNA for aminoacylation and adenylation

Conformational requirements of tobacco mosaic virus RNA for aminoacylation and adenylation

Histidyl-tRNA Synthetase

Isoelectric focusing and isoelectric points of aminoacyl‐tRNA synthetases

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