8J0H

Crystal structure of the fission yeast Rex1BD protein(C4H3.06)

Summary for 8J0H

• Entry DOI: 10.2210/pdb8j0h/pdb
• Descriptor: Uncharacterized protein C4H3.06 (1 entity in total)
• Functional Keywords: heterochromatin, dna repair, histone deacetylase, protein-protein interaction, nuclear protein
• Biological source: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
• Total number of polymer chains: 8
• Total formula weight: 130070.50

Authors

Li, J.,Sun, W.,Chen, Y. (deposition date: 2023-04-11, release date: 2023-11-01, Last modification date: 2024-10-16)

Primary citation

Gao, J.,Sun, W.,Li, J.,Ban, H.,Zhang, T.,Liao, J.,Kim, N.,Lee, S.H.,Dong, Q.,Madramootoo, R.,Chen, Y.,Li, F.
Rex1BD and the 14-3-3 protein control heterochromatin organization at tandem repeats by linking RNAi and HDAC.
Proc.Natl.Acad.Sci.USA, 120:e2309359120-e2309359120, 2023

PubMed Abstract: Tandem DNA repeats are often organized into heterochromatin that is crucial for genome organization and stability. Recent studies revealed that individual repeats within tandem DNA repeats can behave very differently. How DNA repeats are assembled into distinct heterochromatin structures remains poorly understood. Here, we developed a genome-wide genetic screen using a reporter gene at different units in a repeat array. This screen led to identification of a conserved protein Rex1BD required for heterochromatin silencing. Our structural analysis revealed that Rex1BD forms a four-helix bundle structure with a distinct charged electrostatic surface. Mechanistically, Rex1BD facilitates the recruitment of Clr6 histone deacetylase (HDAC) by interacting with histones. Interestingly, Rex1BD also interacts with the 14-3-3 protein Rad25, which is responsible for recruiting the RITS (RNA-induced transcriptional silencing) complex to DNA repeats. Our results suggest that coordinated action of Rex1BD and Rad25 mediates formation of distinct heterochromatin structure at DNA repeats via linking RNAi and HDAC pathways.

PubMed: 38048463
DOI: 10.1073/pnas.2309359120

Experimental method

X-RAY DIFFRACTION (3.383 Å)