An <i>Arabidopsis</i> cDNA encoding a bifunctional glutamine amidotransferase/cyclase suppresses the histidine auxotrophy of a <i>Saccharomyces cerevisiae his7</i> mutant

Fujimori, Ko; Ohta, Daisaku

doi:10.1016/s0014-5793(98)00535-3

Cited by 19 publications

(12 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…S1), requires two catalytic functions: transfer of an amide from glutamine followed by a cyclization reaction. In prokaryotes, these reactions are catalyzed by two different monofunctional enzymes, HisH and HisF, respectively, which form a stable complex (Klem & Davisson, 1993), whereas in plants and yeasts this step is catalyzed by a bifunctional enzyme exhibiting both glutamine amidotransferase and cyclase activities (Fujimori & Ohta, 1998;Brilli & Fani, 2004). The scenario is very similar in the sixth step, the dehydration of IGP to imidazoleacetolphosphate (IAP).…”

Section: Introductionmentioning

confidence: 99%

Structures of native, substrate-bound and inhibited forms ofMycobacterium tuberculosisimidazoleglycerol-phosphate dehydratase

Ahangar

Vyas

Nasir

et al. 2013

Acta Crystallogr D Biol Cryst

View full text Add to dashboard Cite

Imidazoleglycerol-phosphate dehydratase (IGPD; HisB), which catalyses the conversion of imidazoleglycerol-phosphate (IGP) to imidazoleacetol-phosphate in the histidine biosynthesis pathway, is absent in mammals. This feature makes it an attractive target for herbicide discovery. Here, the crystal structure of Mycobacterium tuberculosis (Mtb) IGPD is reported together with the first crystal structures of substrate-bound and inhibited (by 3-amino-1,2,4-triazole; ATZ) forms of IGPD from any organism. The overall tertiary structure of Mtb IGPD, a four-helix-bundle sandwiched between two four-stranded mixed β-sheets, resembles the three-dimensional structures of IPGD from other organisms; however, Mtb IGPD possesses a unique structural feature: the insertion of a one-turn 310-helix followed by a loop ten residues in length. The functional form of IGPD is 24-meric, exhibiting 432 point-group symmetry. The structure of the IGPD-IGP complex revealed that the imidazole ring of the IGP is firmly anchored between the two Mn atoms, that the rest of the substrate interacts through hydrogen bonds mainly with residues Glu21, Arg99, Glu180, Arg121 and Lys184 which protrude from three separate protomers and that the 24-mer assembly contains 24 catalytic centres. Both the structural and the kinetic data demonstrate that the inhibitor 3-amino-1,2,4-triazole inhibits IGPD competitively.

show abstract

Section: Introductionmentioning

confidence: 99%

Structures of native, substrate-bound and inhibited forms ofMycobacterium tuberculosisimidazoleglycerol-phosphate dehydratase

Ahangar

Vyas

Nasir

et al. 2013

Acta Crystallogr D Biol Cryst

View full text Add to dashboard Cite

show abstract

“…The limited studies to date of His gene expression in plants by RNA gel‐blot and microarray analysis suggest that the biosynthetic pathway is expressed in all tissues in Arabidopsis and is not developmental stage‐specific (Fujimori and Ohta, 1 998a,b; Ohta et al ., 2000; Zimmermann et al ., 2004). In the Ni hyperaccumulator plant Alyssum lesbiacum , constitutively high expression of genes in the His biosynthetic pathway is associated with elevated tissue concentrations of free His in comparison with closely related non‐accumulator species (Ingle et al ., 2005).…”

Section: Introductionmentioning

confidence: 99%

Relative contributions of nine genes in the pathway of histidine biosynthesis to the control of free histidine concentrations inArabidopsis thaliana

Rees

Ingle

Smith

2009

Plant Biotechnology Journal

View full text Add to dashboard Cite

SummaryDespite the functional importance of histidine (His) as an essential amino acid in proteins and as a metal-coordinating ligand, comparatively little is known about the regulation of its biosynthesis in plants and the potential for metabolic engineering of this pathway. To investigate the contribution of different steps in the pathway to overall control of His biosynthesis, nine His biosynthetic genes were individually over-expressed in Arabidopsis thaliana to determine their effects on free amino acid pools. Constitutive, CaMV 35S -driven over-expression of the cDNAs encoding either isoform of ATP-phosphoribosyltransferase (ATP-PRT), the first enzyme in the pathway, was sufficient to increase the pool of free His by up to 42-fold in shoot tissue of Arabidopsis , with negligible effect on any other amino acid. In contrast, over-expression of cDNAs for seven other enzymes in the biosynthetic pathway had no effect on His content, suggesting that control of the pool of free His resides largely with ATP-PRT activity. Over-expression of ATP-PRT and increased His content had a negative pleiotropic effect on plant biomass production in 35S:PRT1 lines, but this effect was not observed in 35S:PRT2 lines. In the presence of 100 μ M Ni, which was inhibitory to wild-type plants, a strong positive correlation was observed between free His content and biomass production, indicating that the metabolic cost of His overproduction was outweighed by the benefit of increased tolerance to Ni. His-overproducing plants also displayed somewhat elevated tolerance to Co and Zn, but not to Cd or Cu, indicating chemical selectivity in intracellular metal binding by His.

show abstract

“…1). In plants, cDNAs have been identified which encode seven out of presumably eight enzymes involved in histidine biosynthesis, mostly by functional complementation of yeast and E. coli mutants [23][24][25][26][27][28][29][30][31][32]. The enzyme ATP phosphoribosyl transferase (ATP-PRT) catalyses the first committed step in histidine biosynthesis in bacteria (for example, E. coli and Salmonella typhimurium HisG proteins), yeast (ScHis1p) and in plants ( Fig.…”

Section: Introductionmentioning

confidence: 99%

Enhancing the first enzymatic step in the histidine biosynthesis pathway increases the free histidine pool and nickel tolerance in Arabidopsis thaliana

et al. 2004

View full text Add to dashboard Cite

Naturally selected nickel (Ni) tolerance in Alyssum lesbiacum has been proposed to involve constitutively high levels of endogenous free histidine. Transgenic Arabidopsis thaliana expressing a Salmonella typhimurium ATP phosphoribosyl transferase enzyme (StHisG) resistant to feedback inhibition by histidine contained approximately 2-fold higher histidine concentrations than wild type plants. Under exposure to a toxic Ni concentration, biomass production in StHisG expressing lines was between 14-and 40-fold higher than in wild-type plants. This suggested that enhancing the first step in the histidine biosynthesis pathway is sufficient to increase the endogenous free histidine pool and Ni tolerance in A. thaliana.

show abstract

An Arabidopsis cDNA encoding a bifunctional glutamine amidotransferase/cyclase suppresses the histidine auxotrophy of a Saccharomyces cerevisiae his7 mutant

Cited by 19 publications

References 30 publications

Structures of native, substrate-bound and inhibited forms ofMycobacterium tuberculosisimidazoleglycerol-phosphate dehydratase

Structures of native, substrate-bound and inhibited forms ofMycobacterium tuberculosisimidazoleglycerol-phosphate dehydratase

Relative contributions of nine genes in the pathway of histidine biosynthesis to the control of free histidine concentrations inArabidopsis thaliana

Enhancing the first enzymatic step in the histidine biosynthesis pathway increases the free histidine pool and nickel tolerance in Arabidopsis thaliana

Contact Info

Product

Resources

About