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BPM1 regulates RdDM-mediated DNA methylation via a cullin 3 independent mechanism.
Jagic, Mateja; Vuk, Tamara; Skiljaica, Andreja; Markulin, Lucija; Vicic Bockor, Vedrana; Tokic, Mirta; Miskec, Karlo; Razdorov, Genadij; Habazin, Sinisa; Sostar, Marko; Weber, Igor; Bauer, Natasa; Leljak Levanic, Dunja.
Afiliación
  • Jagic M; Division of Molecular Biology, Department of Biology, Faculty of Science, University of Zagreb, Zagreb, Croatia.
  • Vuk T; Division of Molecular Biology, Department of Biology, Faculty of Science, University of Zagreb, Zagreb, Croatia.
  • Skiljaica A; Division of Molecular Biology, Department of Biology, Faculty of Science, University of Zagreb, Zagreb, Croatia.
  • Markulin L; Division of Molecular Biology, Department of Biology, Faculty of Science, University of Zagreb, Zagreb, Croatia.
  • Vicic Bockor V; Division of Molecular Biology, Department of Biology, Faculty of Science, University of Zagreb, Zagreb, Croatia.
  • Tokic M; Division of Molecular Biology, Department of Biology, Faculty of Science, University of Zagreb, Zagreb, Croatia.
  • Miskec K; Division of Molecular Biology, Department of Biology, Faculty of Science, University of Zagreb, Zagreb, Croatia.
  • Razdorov G; Genos Glycoscience Research Laboratory, Zagreb, Croatia.
  • Habazin S; Genos Glycoscience Research Laboratory, Zagreb, Croatia.
  • Sostar M; Division of Molecular Biology, Institute Ruder Boskovic, Zagreb, Croatia.
  • Weber I; Division of Molecular Biology, Institute Ruder Boskovic, Zagreb, Croatia.
  • Bauer N; Division of Molecular Biology, Department of Biology, Faculty of Science, University of Zagreb, Zagreb, Croatia.
  • Leljak Levanic D; Division of Molecular Biology, Department of Biology, Faculty of Science, University of Zagreb, Zagreb, Croatia. dunja@zg.biol.pmf.hr.
Plant Cell Rep ; 41(11): 2139-2157, 2022 Nov.
Article en En | MEDLINE | ID: mdl-36066603
KEY MESSAGE: BPM1 interacts with components of the DDR complex and stimulates DNA methylation at CHH sites, suggesting its involvement in the RdDM methylation pathway. The best-known function of MATH-BTB proteins, including Arabidopsis BPM proteins, is their role as substrate-specific adaptors of CUL3-based E3 ligases in the ubiquitin-proteasome pathway. This paper reports a new CUL3-independent role of BPM1 in RNA-directed DNA methylation (RdDM). Using quantitative and qualitative Y2H, pull down, microscale thermophoresis and FRET-FLIM, we demonstrate that BPM1 interacts with DMS3 and RDM1, components of the chromatin remodeling DDR complex involved in the recruitment of the RdDM methylation machinery. All three proteins colocalized predominantly in the nucleus. The MATH domain, which specifically binds proteins destined for degradation, was not essential for interactions with DMS3 and RDM1. In plants overexpressing BPM1, endogenous DMS3 protein levels were stable, indicating that BPM1 does not induce proteasomal degradation. In RDM1-overexpressing plants, RDM1 was not ubiquitinated. Together, these results suggest that BPM1 does not mediate the degradation of DMS3 and RDM1. Additionally, overexpression of BPM1 caused increased global methylation levels as well as CHH methylation in promoters of two RdDM-regulated genes, FWA and CML41. Overall, BPM1 seems to have a stimulating effect on RdDM activity, and this role appears to be unrelated to its known function as a Cul3-based E3 ligase adaptor.
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Texto completo: 1 Base de datos: MEDLINE Asunto principal: Arabidopsis / Proteínas de Arabidopsis Tipo de estudio: Qualitative_research Idioma: En Revista: Plant Cell Rep Asunto de la revista: BOTANICA Año: 2022 Tipo del documento: Article

Texto completo: 1 Base de datos: MEDLINE Asunto principal: Arabidopsis / Proteínas de Arabidopsis Tipo de estudio: Qualitative_research Idioma: En Revista: Plant Cell Rep Asunto de la revista: BOTANICA Año: 2022 Tipo del documento: Article