Partial Purification and Properties of Acetolactate Synthase of Etiolated Pea Seedlings

Shimizu, Tsutomu; Nakayama, Ishizue; Nakao, Toshiko; Abe, Hiroshi

doi:10.1584/jpestics.19.3_187

Cited by 7 publications

(6 citation statements)

References 5 publications

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“…K m 1É5 to 5 mM have been reported for plants. 14,16,33 This hyperbolic response towards the substrate together with the behaviour towards the inhibitor (imazethapyr, see Fig. 5) strongly suggests that Rhizobium has a single enzyme or, if several enzymes are present, they share the same for pyruvate and for imazethapyr.…”

Section: Rhizobium Als Characterizationmentioning

confidence: 86%

“…In the few cases in which puriÐed ALS and crude extracts have been compared the inhibitory e †ects of di †erent compounds are identical. 16,33 Inhibition of ALS from enteric bacteria and higher plants by imidazolinones has been reported to be timedependent and biphasic,2,48 indicating that the mode of action of these herbicides should be examined under identical conditions to allow direct comparisons. Analysis of the time-dependent inhibition by imazethapyr (Fig.…”

Section: Imazethapyr Inhibition Of Alsmentioning

confidence: 99%

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Imazethapyr inhibition of acetolactate synthase inRhizobiumand its symbiosis with pea

et al. 1998

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: Acetolactate synthase (ALS) activity extracted from Rhizobium leguminosarum biovar. viciae has been characterized. The optimum pH for extraction was 7É6 and for the assay 7É0. The for pyruvate was 7É2 mM, and the enzyme K m was saturated at 40 mM. An obligatory requirement of TPP and Mg2`for full ALS activity was observed. Valine was the only branched-chain amino acid that caused ALS feedback inhibition. The speciÐc activity of Rhizobium ALS was nearly 20 times the activity found in pea (Pisum sativum) leaves. Bacteroids from pea nodules also showed high ALS activity, and the nodule plant fraction had higher ALS activity than other plant tissues. ALS sensitivity to imazethapyr was also dependent on the source : ALS activity of free-living Rhizobium and bacteroids was slightly more tolerant than that of other pea tissues, but the di †er-ences were less than those found in rates of speciÐc activity. It is proposed that the high ALS activity expressed by Rhizobium, both as free-living bacteria and as bacteroids, is related to the growth tolerance of rhizobia to imazethapyr and is also related to the relative tolerance of symbiotic pea plants.1998 SCI ( Pestic. Sci., 52, 372È380 (1998)

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Section: Rhizobium Als Characterizationmentioning

confidence: 86%

Section: Imazethapyr Inhibition Of Alsmentioning

confidence: 99%

Imazethapyr inhibition of acetolactate synthase inRhizobiumand its symbiosis with pea

et al. 1998

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“…Because of ALS lability; however, this has proved to be difficult 21. It is noteworthy that when crude extracts and purified enzyme fractions were compared for the inhibitory effects of different compounds on ALS activity, no differences were found 35, 36…”

Section: Discussionmentioning

confidence: 99%

Effect of chlorimuron‐ethyl on Bradyrhizobium japonicum and its symbiosis with soybean

Zawoznik

Tomaro

2005

Pest Management Science

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Possible side-effects of the acetolactate synthase (ALS)-inhibiting herbicide chlorimuron-ethyl on Bradyrhizobium japonicum (Kirchner & Jordan) in pure culture and on inoculated soybean plants growing under controlled conditions were investigated. Growth of B japonicum strain E109 was not affected by this herbicide even when exposed to concentrations 150 times higher than recommended field doses. However, nodulation of soybean plants treated 5 days after emergence with chlorimuron-ethyl at standard application rates was impaired: a 38% decrease in the number of nodules per plant was observed four weeks after treatment. Despite nodule number decrease, no changes in shoot nitrogen content could be detected. Total fresh biomass was diminished by 25% in herbicide-treated plants. Leghemoglobin content in nodules did not vary; nevertheless total nodule protein was diminished by 40% in the herbicide-treated group. ALS activity in different soybean tissues and their relative sensitivity to chlorimuron-ethyl were also investigated. Roots and bacteroids had the greatest specific ALS activities. On a fresh weight basis, the bacteroid fraction displayed the highest ALS activity and was also the most tolerant to in vitro chlorimuron addition: 72% of its activity was retained after including 10 microM chlorimuron-ethyl in the reaction mixture. These results indicate that standard application rates of chlorimuron-ethyl will have limited incidence on B japonicum survival, and effects on nodulation may have little long-term consequences on soybean nitrogen fixation potential. The differences found among soybean tissues not only in intrinsic ALS activity but also in their relative sensitivity to this herbicide suggests that, in leguminous plants living in symbiosis with rhizobia, nodules may contribute to an enhanced tolerance to ALS inhibitors.

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“…Partially purified enzyme solution containing ALS was extracted from 10 g leaves from WT and transgenic plants according to Shimizu (1994).…”

Section: Purification Of Als From Rice Leavesmentioning

confidence: 99%

A novel mutated acetolactate synthase gene conferring specific resistance to pyrimidinyl carboxy herbicides in rice

et al. 2007

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Acetolactate synthase (ALS) is the first common enzyme in the biosynthetic pathway of branched-chain amino acids. Mutations of specific amino acids in ALS have been known to confer resistance to ALS-inhibiting herbicides such as sulfonylureas and pyrimidinyl carboxy (PC) herbicides. However, mutations conferring exclusive resistance to PC have not yet been reported to date. We selected PC resistant rice calli, which were derived from anther culture, using one of the PCs, bispyribac-sodium (BS), as a selection agent. Two lines of BS-resistant plants carrying a novel mutation, the 95th Glycine to Alanine (G95A), in ALS were obtained. In vitro ALS activity assay indicated that the recombinant protein of G95A-mutated ALS (ALS-G95A) conferred highly specific resistance to PC herbicides. In order to determine if the ALS-G95A gene could be used as a selection marker for rice transformation, the ALS-G95A gene was connected to ubiquitin promoter and introduced into rice. PC resistant plants containing integrated ALS-G95A gene were obtained after selection with BS as a selection agent. In conclusion, novel G95A mutated ALS gene confers highly specific resistant to PC-herbicides and can be used as a selection marker.

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Partial Purification and Properties of Acetolactate Synthase of Etiolated Pea Seedlings

Cited by 7 publications

References 5 publications

Imazethapyr inhibition of acetolactate synthase inRhizobiumand its symbiosis with pea

Imazethapyr inhibition of acetolactate synthase inRhizobiumand its symbiosis with pea

Effect of chlorimuron‐ethyl on Bradyrhizobium japonicum and its symbiosis with soybean

A novel mutated acetolactate synthase gene conferring specific resistance to pyrimidinyl carboxy herbicides in rice

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