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The N-terminal coiled-coil domain of Arabidopsis CROWDED NUCLEI 1 is required for nuclear morphology maintenance.
Yin, Chunmei; Wang, Yuanda; Wang, Pan; Chen, Guangxin; Sun, Aiqing; Fang, Yuda.
Affiliation
  • Yin C; Joint Center for Single-Cell Biology, School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai, 200240, China.
  • Wang Y; Joint Center for Single-Cell Biology, School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai, 200240, China.
  • Wang P; Joint Center for Single-Cell Biology, School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai, 200240, China.
  • Chen G; Joint Center for Single-Cell Biology, School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai, 200240, China.
  • Sun A; Joint Center for Single-Cell Biology, School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai, 200240, China. aqsun2019@sjtu.edu.cn.
  • Fang Y; Joint Center for Single-Cell Biology, School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai, 200240, China. yuda.fang@sjtu.edu.cn.
Planta ; 260(3): 62, 2024 Jul 27.
Article in En | MEDLINE | ID: mdl-39066892
ABSTRACT
The Arabidopsis CROWDED NUCLEI (CRWN) family proteins form a lamina-like meshwork beneath the nuclear envelope with multiple functions, including maintenance of nuclear morphology, genome organization, DNA damage repair and transcriptional regulation. CRWNs can form homodimers/heterodimers through protein‒protein interactions; however, the exact molecular mechanism of CRWN dimer formation and the diverse functions of different CRWN domains are not clear. In this report, we show that the N-terminal coiled-coil domain of CRWN1 facilitates its homodimerization and heterodimerization with the coiled-coil domains of CRWN2-CRWN4. We further demonstrated that the N-terminus but not the C-terminus of CRWN1 is sufficient to rescue the defect in nuclear morphology of the crwn1 crwn2 mutant to the WT phenotype. Moreover, both the N- and C-terminal fragments of CRWN1 are necessary for its normal function in the regulation of plant development. Collectively, our data shed light on the mechanism of plant lamina network formation and the functions of different domains in plant lamin-like proteins.
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Full text: 1 Database: MEDLINE Main subject: Cell Nucleus / Arabidopsis / Arabidopsis Proteins Language: En Journal: Planta Year: 2024 Type: Article Affiliation country: China

Full text: 1 Database: MEDLINE Main subject: Cell Nucleus / Arabidopsis / Arabidopsis Proteins Language: En Journal: Planta Year: 2024 Type: Article Affiliation country: China