The plastid phosphorylase as a multiple-role player in plant metabolism
Copyright © 2019 Elsevier B.V. All rights reserved.
| Veröffentlicht in: | Plant science : an international journal of experimental plant biology. - 1985. - 290(2020) vom: 03. Jan., Seite 110303 |
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| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2020
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| Zugriff auf das übergeordnete Werk: | Plant science : an international journal of experimental plant biology |
| Schlagworte: | Journal Article Review L80 domain PEST motif Photosynthesis Protein phosphorylation Sink-source limitation Starch initiation Starch phosphorylase Starch synthesis mehr... |
| Zusammenfassung: | Copyright © 2019 Elsevier B.V. All rights reserved. The physiological roles of the plastidial phosphorylase in starch metabolism of higher plants have been debated for decades. While estimated physiological substrate levels favor a degradative role, genetic evidence indicates that the plastidial phosphorylase (Pho1) plays an essential role in starch initiation and maturation of the starch granule in developing rice grains. The plastidial enzyme contains a unique peptide domain, up to 82 residues in length depending on the plant species, not found in its cytosolic counterpart or glycogen phosphorylases. The role of this extra peptide domain is perplexing, as its complete removal does not significantly affect the in vitro catalytic or enzymatic regulatory properties of rice Pho1. This peptide domain may have a regulatory function as it contains potential phosphorylation sites and, in some plant Pho1s, a PEST motif, a substrate for proteasome-mediated degradation. We discuss the potential roles of Pho1 and its L80 domain in starch biosynthesis and photosynthesis |
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| Beschreibung: | Date Completed 23.03.2020 Date Revised 30.09.2020 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1873-2259 |
| DOI: | 10.1016/j.plantsci.2019.110303 |