7CNA

Crystal structure of Spindlin1/C11orf84 complex bound to histone H3K4me3K9me3 peptide

Summary for 7CNA

• Entry DOI: 10.2210/pdb7cna/pdb
• Descriptor: Spindlin-1, Spindlin interactor and repressor of chromatin-binding protein, ALA-ARG-THR-M3L-GLN-THR-ALA-ARG-M3L-SER-THR, ... (8 entities in total)
• Functional Keywords: epigenetic reader, protein binding
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 6
• Total formula weight: 58780.56

Authors

Qian, C.M. (deposition date: 2020-07-30, release date: 2021-01-13, Last modification date: 2023-11-29)

Primary citation

Du, Y.,Yan, Y.,Xie, S.,Huang, H.,Wang, X.,Ng, R.K.,Zhou, M.M.,Qian, C.
Structural mechanism of bivalent histone H3K4me3K9me3 recognition by the Spindlin1/C11orf84 complex in rRNA transcription activation.
Nat Commun, 12:949-949, 2021

PubMed Abstract: Spindlin1 is a unique multivalent epigenetic reader that facilitates ribosomal RNA transcription. In this study, we provide molecular and structural basis by which Spindlin1 acts in complex with C11orf84 to preferentially recognize non-canonical bivalent mark of trimethylated lysine 4 and lysine 9 present on the same histone H3 tail (H3K4me3K9me3). We demonstrate that C11orf84 binding stabilizes Spindlin1 and enhances its association with bivalent H3K4me3K9me3 mark. The functional analysis suggests that Spindlin1/C11orf84 complex can displace HP1 proteins from H3K4me3K9me3-enriched rDNA loci, thereby facilitating the conversion of these poised rDNA repeats from the repressed state to the active conformation, and the consequent recruitment of RNA Polymerase I for rRNA transcription. Our study uncovers a previously unappreciated mechanism of bivalent H3K4me3K9me3 recognition by Spindlin1/C11orf84 complex required for activation of rRNA transcription.

PubMed: 33574238
DOI: 10.1038/s41467-021-21236-x

Experimental method

X-RAY DIFFRACTION (1.6 Å)