Identification of the Interacting Surface Between ZMYND8 and RBBP4,a Core Components of the Nucleosome Remodeling and Deacetylase（NuRD）Complex

doi:10.13560/j.cnki.biotech.bull.1985.2018-0567

Abstract

Abstract: Nucleosome remodeling and histone deacetylase（NuRD）complex contains multiple subunits and plays a critical role in transcription regulation and DNA damage repair. Human ZMYND8（Zinc finger MYND-type containing 8）participates in transcription regulation and DNA damage repair by forming complex with NuRD. Rbbp4, a core submit of NuRD, was expressed in baculovirus expression system in vitro and purified by Ni-NTA column and molecular sieve chromatography column to electrophoretic purity. Isothermal titration calorimetry（ITC）experiment was used to identify the interacting surface between ZMYND8 and RBBP4,and results from which demonstrated that RBBP4 bound to the basic amino acids（residues 43-54）at the N-terminus of ZMYND8. The site-directed mutation experiment at the amino acid residues of RBBP4 further confirmed the interacting surface of both. Combined with the previous findings,it is revealed that ZMYND8 binds to the surface of NuRD complex using the N-terminal basic region and C-terminal MYND domain by surrounding way.

Key words: ZMYND8, RBBP4, NuRD, interaction

XIE Chang-lin, WU Ji-hui, TANG Ya-jun. Identification of the Interacting Surface Between ZMYND8 and RBBP4,a Core Components of the Nucleosome Remodeling and Deacetylase（NuRD）Complex[J]. Biotechnology Bulletin, 2018, 34(12): 159-165.

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