| Literature DB >> 31040182 |
M Daniel Ricketts1,2, Nirmalya Dasgupta3, Jiayi Fan1, Joseph Han1,4, Morgan Gerace1, Yong Tang5, Ben E Black1,6, Peter D Adams3, Ronen Marmorstein7,2,4,5,6.
Abstract
The HIRA histone chaperone complex is composed of the proteins HIRA, UBN1, and CABIN1 and cooperates with the histone chaperone ASF1a to specifically bind and deposit H3.3/H4 into chromatin. We recently reported that the UBN1 Hpc2-related domain (HRD) specifically binds to H3.3/H4 over H3.1/H4. However, the mechanism for HIRA complex deposition of H3.3/H4 into nucleosomes remains unclear. Here, we characterize a central region of UBN1 (UBN1 middle domain) that is evolutionarily conserved and predicted to have helical secondary structure. We report that the UBN1 middle domain has dimer formation activity and binds to H3/H4 in a manner that does not discriminate between H3.1 and H3.3. We additionally identify a nearby DNA-binding domain in UBN1, located between the UBN1 HRD and middle domain, which binds DNA through electrostatic contacts involving several conserved lysine residues. Together, these observations suggest a mechanism for HIRA-mediated H3.3/H4 deposition whereby UBN1 associates with DNA and dimerizes to mediate formation of an (H3.3/H4)2 heterotetramer prior to chromatin deposition.Entities:
Keywords: DNA-binding protein; chromatin; epigenetics; histone; histone chaperone
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Year: 2019 PMID： 31040182 PMCID： PMC6556585 DOI： 10.1074/jbc.RA119.007480
Source DB: PubMed Journal: J Biol Chem ISSN： 0021-9258 Impact factor: 5.157