4.6 Article

Ubiquitin-conjugated degradation of golden 2-like transcription factor is mediated by CUL4-DDB1-based E3 ligase complex in tomato

期刊

NEW PHYTOLOGIST
卷 209, 期 3, 页码 1028-1039

出版社

WILEY
DOI: 10.1111/nph.13635

关键词

26S proteasome; cullin4-DDB1-DET1 complex; golden 2-like transcription factor; tomato (Solanum lycopersicum); ubiquitin-conjugated degradation

资金

  1. National Natural Science Foundation of China [31171179, 90717110, 31471157, 31461143008]
  2. National Natural Science Foundation of China for Distinguished Young Scientists [30825030]
  3. National Basic Research Program of China [2011CB100401]
  4. Advanced Program of Doctoral Fund of Ministry of Education of China [20110181130009]
  5. China Postdoctoral Science Foundation [2014M561814, 2014M561815]

向作者/读者索取更多资源

CULLIN4-RING ubiquitin ligases (CRL4s) as well as their targets are fundamental regulators functioning in many key developmental and stress responses in eukaryotes. In tomato (Solanum lycopersicum), molecular cloning has revealed that the underlying genes of natural spontaneous mutations high pigment 1 (hp1), high pigment 2 (hp2) and uniform ripening (u) encode UV-DAMAGED DNA BINDING PROTEIN 1 (DDB1), DE-ETIOLATED 1 (DET1) and GOLDEN 2-LIKE (GLK2), respectively. However, the molecular basis of the opposite actions of tomato GLK2 vs CUL4-DDB1-DET1 complex on regulating plastid level and fruit quality remains unknown. Here, we provide molecular evidence showing that the tomato GLK2 protein is a substrate of the CUL4-DDB1-DET1 ubiquitin ligase complex for the proteasome degradation. SlGLK2 is degraded by the ubiquitin-proteasome system, which is mainly determined by two lysine residues (K11 and K253). SlGLK2 associates with the CUL4-DDB1-DET1 E3 complex in plant cells. Genetically impairing CUL4, DDB1 or DET1 results in a retardation of SlGLK2 degradation by the 26S proteasome. These findings are relevant to the potential of nutrient accumulation in tomato fruit by mediating the plastid level and contribute to a deeper understanding of an important regulatory loop, linking protein turnover to gene regulation.

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