期刊
PLANT SCIENCE
卷 290, 期 -, 页码 -出版社
ELSEVIER IRELAND LTD
DOI: 10.1016/j.plantsci.2019.110303
关键词
Starch phosphorylase; Starch synthesis; Starch initiation; L80 domain; PEST motif; Protein phosphorylation; Sink-source limitation; Photosynthesis
资金
- Agriculture and Food Research Initiative from the USDA National Institute of Food and Agriculture [2018-67013-27458, 1014859]
- USDA Hatch Umbrella Project [1015621]
- Hatch Regional Project [NC-1200]
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 (Phol) 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 Phol. This peptide domain may have a regulatory function as it contains potential phosphorylation sites and, in some plant Phols, a PEST motif, a substrate for proteasome-mediated degradation. We discuss the potential roles of Phol and its L80 domain in starch biosynthesis and photosynthesis.
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