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alpha maltose/arabidopsis
Veza se sprema u međuspremnik
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A maltose transporter from apple is expressed in source and sink tissues and complements the Arabidopsis maltose export-defective mutant.
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Prior to the cytosolic synthesis of transport sugars during transitory starch utilization, intermediate products of starch breakdown, such as maltose, must be exported from chloroplasts. Recent work in Arabidopsis indicates that a novel transporter mediates maltose transfer across the chloroplast
Expression analysis of genes encoding malectin-like domain (MLD)- and leucine-rich repeat (LRR)- containing proteins in Arabidopsis thaliana.
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Malectin is a maltose-binding endoplasmic reticulum protein conserved in animals. In Arabidopsis thaliana, we identified four genes that encode malectin-like domain (MLD)- and leucine-rich repeat (LRR)-containing proteins (AtMLLRs): two were receptor-like proteins (AtMLLR1 and 2) and the
Characterization of the yam tuber storage proteins from Dioscorea batatas exhibiting unique lectin activities.
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Four major proteins designated DB1, DB2, DB3, and DB4 were isolated and characterized from the yam tuber Dioscorea batatas. The ratios of their yields were 20:50:20:10. DB1 was a mannose-binding lectin (20 kDa) consisting of 10-kDa subunits and was classified as the monocot mannose-binding lectin
EPR studies of the mitochondrial alternative oxidase. Evidence for a diiron carboxylate center.
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The alternative oxidase (AOX) is a ubiquinol oxidase found in the mitochondrial respiratory chain of plants as well as some fungi and protists. It has been predicted to contain a coupled diiron center on the basis of a conserved sequence motif consisting of the proposed iron ligands, four glutamate
Mutants of Arabidopsis lacking starch branching enzyme II substitute plastidial starch synthesis by cytoplasmic maltose accumulation.
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Three genes, BE1, BE2, and BE3, which potentially encode isoforms of starch branching enzymes, have been found in the genome of Arabidopsis thaliana. Although no impact on starch structure was observed in null be1 mutants, modifications in amylopectin structure analogous to those of other branching
Expression and Purification of the Arabidopsis E4 SUMO Ligases PIAL1 and PIAL2.
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The proteins PIAL1 (At1g08910) and PIAL2 (At5g41580) are members of the recently discovered group of plant E4 SUMO ligases. This protocol allows quick and simple expression of the recombinant proteins in Escherichia coli (E. coli) and subsequent affinity purification using a maltose binding protein
RNA interference of Arabidopsis beta-amylase8 prevents maltose accumulation upon cold shock and increases sensitivity of PSII photochemical efficiency to freezing stress.
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It has been suggested that beta-amylase (BMY) induction during temperature stress in Arabidopsis could lead to starch-dependent maltose accumulation, and that maltose may contribute to protection of the electron transport chain and proteins in the chloroplast stroma during acute stress. A
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