Serine hydroxymethyltransferase participates in the synthesis of cysteine-rich storage proteins in rice seed
Serine hydroxymethyltransferase participates in the synthesis of cysteine-rich storage proteins in rice seed
复制标题
丝氨酸羟甲基转移酶参与水稻种子中富含半胱氨酸的储存蛋白的合成
DOI:
10.1016/j.plantsci.2021.111049
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发表时间:
2021
期刊:
影响因子:
5.2
通讯作者:
Toshihiro Kumamaru
中科院分区:
文献类型:
--
作者:
Hiroaki Matsusaka;Masako Fukuda;Ammar Elakhdar;Toshihiro Kumamaru
Thelow level of cysteine-rich proteins(lcrp) mutation indicates a decrease in cysteine-rich (CysR) prolamines, α-globulin, and glutelin. To identify the causing factor oflcrpmutation, to elucidate its function, and to elucidate the role of CysR proteins in the formation of protein bodies (PBs),lcrpmutant was analyzed. A linkage map of theLCRPgene was constructed and genomic DNA sequencing of a predicted gene within the mapped region demonstrated thatLCRPencodes a serine hydroxymethyltransferase, which participates in glycine-serine interconversion of one-carbon metabolism in the sulfur assimilation pathway. The levels ofl-Ser, Gly, and Met in the sulfur assimilation pathway in thelcrpseeds increased significantly compared to that in the wildtype (WT). As thelcrpmutation influences the growth of shoot and root, the effects of the addition to the medium of amino acids and other compounds on the sulfur assimilation pathway were studied. Electron-lucent PBs surrounded by ribosome-attached membranes were observed accumulating cysteine-poor prolamines in thelcrpseeds. Additionally, glutelin-containing PBs were smaller and distorted in thelcrpseeds compared to those in the WT. These analyses of PBs in thelcrpseeds suggest that cysteine-rich proteins play an important role in the formation of PBs in rice.