| FEBS Letters | |
| Leucine and its keto acid enhance the coordinated expression of genes for branched‐chain amino acid catabolism in Arabidopsis under sugar starvation | |
| Watanabe, Akira1  Fujiki, Yuki1  Ito, Masaki1  Nishida, Ikuo1  | |
| [1] Department of Biological Sciences, Graduate School of Science, University of Tokyo, Bunkyo-ku, Hongo, Tokyo 113-0033, Japan | |
| 关键词: Branched-chain amino acid; Branched-chain α-keto acid; Hexokinase; Sugar starvation; Arabidopsis; BCKDH; branched-chain α-keto acid dehydrogenase; Cab; chlorophyll a/b binding protein; DCMU; 3-(3; 4-dichlorophenyl)-1; 1-dimethylurea; KIC; α-ketoisocaproate; NR; nitrate reductase; MCCase; β-methylcrotonyl-coenzyme A carboxylase; | |
| DOI : 10.1016/S0014-5793(01)02536-4 | |
| 学科分类:生物化学/生物物理 | |
| 来源: John Wiley & Sons Ltd. | |
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【 摘 要 】
Branched-chain α-keto acid dehydrogenase (BCKDH), a multienzyme complex, plays a key role in branched-chain amino acid catabolism. However, it remains unclear whether expression of each subunit is coordinately regulated in plants, which should be important for the efficient assembly of subunits into a functional multienzyme complex. We show that the transcripts from the Arabidopsis E1α subunit gene accumulated in dark-adapted leaves and in sugar-starved suspension cells. These results are complementary to our previous report that the transcripts for the E1β and E2 subunit genes accumulated in sugar-starved cells. Expression of the E1α gene is likely to be regulated by hexokinase-mediated sugar signaling, indicating that sugar plays a regulatory role in the coordinated expression of BCKDH subunit genes. Furthermore, Leu and its metabolite α-ketoisocaproate have synergistic effects on the enhanced expression of BCKDH subunit genes under sugar starvation. We hence suggest that branched-chain amino acids activate their own degradation pathway in sugar-starved cells through co-induction of each subunit gene of BCKDH.
【 授权许可】
Unknown
【 预 览 】
| Files | Size | Format | View |
|---|---|---|---|
| RO201912020310660ZK.pdf | 239KB |
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