Enzymatic acylation of histidine to tobacco mosaic virus RNA

Salomon, R.; Sela, Ilan; Soreq, Hermona; Giveon, David; Littauer, Uriel Z.

doi:10.1016/0042-6822(76)90095-7

Cited by 34 publications

(11 citation statements)

References 23 publications

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“…The figure of 4300 ct/min/pmol for 27S TMV RNA control represents a specific histidine binding activity of 0.15 pmol His/pmol RNA; all other figures are directly proportional. This is within the range of published values Perham & Wilson, 1976;Salomon et al, 1976) and reflects the quality of our crude yeast enzyme preparation.…”

Section: Cell-free Protein Synthesissupporting

confidence: 63%

Dimethyl Sulphoxide (DMSO) Disassembles Tobacco Mosaic Virus Predominantly from the 5'-end of the Viral RNA

Wilson

Lomonossoff

Glover

1981

Journal of General Virology

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SUMMARYThe effect of dimethyl sulphoxide (DMSO) on the stability of native and EDTA-treated tobacco mosaic virus (TMV, Vulgare strain) has been reinvestigated using a variety of chemical and biochemical techniques. Contrary to earlier reports, we conclude that TMV rods behave as a heterodisperse population, exhibiting one of two modes of uncoating. More than 50% of the rods disassemble rapidly and extensively in a unique polar fashion beginning at the 5'-end of the viral RNA. The remainder of the rod population uncoats more slowly, less extensively, and exhibits substantial bidirectional exposure of the viral RNA, commencing at the 3'-terminus but proceeding for no more than 500 nucleotides before the major uncoating event again shifts to the 5'-ends of the particles. A portion of the coat protein gene and the region around the assembly initiation site on the viral RNA appears most resistant to uni-or bidirectional stripping; this is in contrast to previous reports. This complex, biphasic behaviour of the TMV rod population, which produces two broad and relatively ill-defined peaks of metastable nucleoprotein intermediates, may account for many of the inconsistencies prevalent in earlier work.

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Section: Cell-free Protein Synthesissupporting

confidence: 63%

Dimethyl Sulphoxide (DMSO) Disassembles Tobacco Mosaic Virus Predominantly from the 5'-end of the Viral RNA

Wilson

Lomonossoff

Glover

1981

Journal of General Virology

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“…In compilations of tRNA His sequences U-1 · A73 base pairs can also be found, for instance in phage T5; its importance for tRNA recognition has yet to be shown (compare Sprinzl et al, 1998). The observation that the RNAs of the tobacco mosaic virus and satellite tobacco mosaic virus could be aminoa- cylated with histidine by crude aaRS preparations from yeast, rat liver and other mammalian cells (Öberg and Philipson, 1972;Salomon et al, 1975Salomon et al, , 1976Litvak et al, 1973) was astonishing at first. The RNAs are acylated at their 3Ј-termini, which contain the tRNA-like sequence C-C-C-A (Carriquiry and Litvak, 1974;Guilley et al, 1975).…”

Section: Identity Of Trna Hismentioning

confidence: 99%

“…The intracellular concentration of HisRS was estimated at 2.3 M in Salmonella E. coli Muench and Berg, 1966 820-fold 85 (42.5) Kalousek and Konigsberg, 1974 351-fold, Kern and Lapointe, partial 1979purification Fromant et al, 1981del Rio et al, 1982crystals Francklyn et al, 1994(HisRS Yan et al, 1996; mutants) Rühlmann et al, 1997;Francklyn, 1997 B. stearo-102 Grosjean et al, 1976 thermophilus S. typhimurium 800-fold, 100 De Lorenzo and Ames, 95% 1970 78 (40) De Lorenzo et al, 1972;Boguslawski et al,1974 T. thermophilus 95%, Yaremchuk et al, 1995 crystals Streptococcus 99% (47.9) Menguito et al, 1993a equisimilis Baker's yeast 590-fold Tigerstrom and Tener, 1967 S. cerevisiae 100 Boguslawski et al,1974 N. crassa Takeda, 1969 921-fold 125 (62.5) Chen and Somberg, 1980 Rat liver 100 -150 Yang et al, 1984 11700-96 (50) Fahoum and Yang,1987 fold multi-enzyme Badyopadhyay and complexes Deutscher, 1971Vellekamp et al, 1985Salomon et al, 1976multiOgata et al, 1994enzyme Ogata and Terea, 1994 Rabbit reti-83780-122 (64) Kane et al, 1978 culocytes fold partial Alzhanova et al, 1982purifiSmith et al, 1979 Beef liver partial Walker et al, 1983 purification Bovine liver Ͼ 2650-160 (80) Walker and Jeffrey, fold 1987 HeLa cells 5110-120 (55) Biswas et al, 1987a…”

Section: Purification Of Histidyl-trna Synthetasesmentioning

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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“…It is clear that in some viruses these structures are involved in viral replication Miller et al, 1985;Bujarski et al, 1986;Dreher & Hall, 1988a, b), but the details are uncertain. Variants of tobacco mosaic virus (TMV) that lack the T-terminal five to 10 nucleotides are not infectious (Salomon et al, 1976), and certain point mutations within the tRNA-like structure of the brome mosaic virus genome destroy its infectivity (Dreher & Hall, 1988b), are not aminoacylated (Hall, 1979) and do not function as a template for synthesis of the genomic minus strand. By contrast, the fact that the T-terminal region of the ELV genome probably forms only part of the tRNA-like structure found in other tymoviruses indicates that the recognition by valine-acyl tRNA synthetase is not essential for tymovirus survival, and that other parts of the ELV genomes can replace its function.…”

Section: The Terminal Untranslated Regions Of the Genomesmentioning

confidence: 99%