Immature seeds of some dicotyledonous plants contain IAGlc synthase catalysing the synthesis of 1-O-IAGlc. This enzyme activity is comparable with 1-O-IAGlc synthase activity investigated earlier in liquid endosperm of Zea mays. Polyclonal antibodies against maize 1-O-IAGlc synthase cross-react with partially purified 1-O-IAGlc synthase from immature pea and rape seeds. Single immunoreactive bands were observed at a locus corresponding to 45.7 kDa and 43.7 kDa from pea and rape enzyme preparations, respectively, unlike that from the 50 kDa molecular mass of the maize enzyme. It was also observed that some high molecular weight compounds of pea seeds are labelled in vivo by [(14)C] IAA, and unlabelled 1-O-IAGlc inhibits that labelling. In immature pea seeds 43-49.8% of the IAA-modified high molecular weight compounds, obtained after ultracentrifugation, was found in the soluble fraction and 50.1-57% in the insoluble fraction. Ester-linked IAA accounted for about 6-9% and 38-45.6% in soluble and insoluble material, respectively, estimated after hydrolysis in 1 N NaOH. Enzymatic hydrolysis of IAA-labelled high molecular weight compounds gives free IAA and compound(s) corresponding to IAGlc isomers. These results suggest that 1-O-IAGlc synthesized in legume seeds may be used for the modification of some high molecular weight compounds.
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Proc Natl Acad Sci U S A
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Institute of Science and Technology Austria, AT-3400 Klosterneuburg, Austria.
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Helen Wills Neuroscience Institute, University of California Berkeley, Berkeley, CA 94720.
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Department of Immunology and Regenerative Biology, Weizmann Institute of Science, Rehovot 7610001, Israel.
Malignant gliomas are heterogeneous tumors, mostly incurable, arising in the central nervous system (CNS) driven by genetic, epigenetic, and metabolic aberrations. Mutations in isocitrate dehydrogenase (IDH1/2) enzymes are predominantly found in low-grade gliomas and secondary high-grade gliomas, with IDH1 mutations being more prevalent. Mutant-IDH1/2 confers a gain-of-function activity that favors the conversion of a-ketoglutarate (α-KG) to the oncometabolite 2-hydroxyglutarate (2-HG), resulting in an aberrant hypermethylation phenotype.
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Oncode Institute, Hubrecht Institute-Royal Netherlands Academy of Arts and Science, Utrecht 3584 CT, The Netherlands.
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