ORIGINAL ARTICLE

Cell Research (2010): 529-538
© 2010 IBCB, SIBS, CAS All rights reserved 1001-0602/06 $ 30.00
www.nature.com/cr

Structural insights into selective histone H3 recognition by the human Polybromo bromodomain 2

Zachary Charlop-Powers, Lei Zeng, Qiang Zhang and Ming-Ming Zhou

Correspondence: Ming-Ming Zhou, Tel: +(212) 659-8652; Fax: +(212) 849-2456 E-mail: ming-ming.zhou@mssm.edu

Download as printable (PDF) file Full Text (html)file Search Medline for articles by: Zachary Charlop-Powers

The Polybromo (PB) protein functions as a key component of the human PBAF chromatin remodeling complex in regulation of gene transcription. PB is made up of modular domains including six bromodomains that are known as acetyl-lysine binding domains. However, histone-binding specificity of the bromodomains of PB has remained elusive. In this study, we report biochemical characterization of all six PB bromodomains' binding to a suite of lysine-acetylated peptides derived from known acetylation sites on human core histones. We demonstrate that bromodomain 2 of PB preferentially recognizes acetylated lysine 14 of histone H3 (H3K14ac), a post-translational mark known for gene transcriptional activation. We further describe the molecular basis of the selective H3K14ac recognition of bromodomain 2 by solving the protein structures in both the free and bound forms using X-ray crystallography and NMR, respectively.

Cell Research (2010) 20:529–538. doi:10.1038/cr.2010.43; published online 6 April 2010

Keywords: NMR; crystallography; bromodomain; chromatin; transcription regulator