| Literature DB >> 27207856 |
Doreen Feike1, David Seung2, Alexander Graf1, Sylvain Bischof2, Tamaryn Ellick2, Mario Coiro2, Sebastian Soyk2, Simona Eicke2, Tabea Mettler-Altmann2, Kuan Jen Lu2, Martin Trick1, Samuel C Zeeman2, Alison M Smith3.
Abstract
To uncover components of the mechanism that adjusts the rate of leaf starch degradation to the length of the night, we devised a screen for mutant Arabidopsis thaliana plants in which starch reserves are prematurely exhausted. The mutation in one such mutant, named early starvation1 (esv1), eliminates a previously uncharacterized protein. Starch in mutant leaves is degraded rapidly and in a nonlinear fashion, so that reserves are exhausted 2 h prior to dawn. The ESV1 protein and a similar uncharacterized Arabidopsis protein (named Like ESV1 [LESV]) are located in the chloroplast stroma and are also bound into starch granules. The region of highest similarity between the two proteins contains a series of near-repeated motifs rich in tryptophan. Both proteins are conserved throughout starch-synthesizing organisms, from angiosperms and monocots to green algae. Analysis of transgenic plants lacking or overexpressing ESV1 or LESV, and of double mutants lacking ESV1 and another protein necessary for starch degradation, leads us to propose that these proteins function in the organization of the starch granule matrix. We argue that their misexpression affects starch degradation indirectly, by altering matrix organization and, thus, accessibility of starch polymers to starch-degrading enzymes.Entities:
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Year: 2016 PMID: 27207856 PMCID: PMC4944407 DOI: 10.1105/tpc.16.00011
Source DB: PubMed Journal: Plant Cell ISSN: 1040-4651 Impact factor: 11.277