Lei Zeng

TL;DR: The solution structure of the bromodomain of the HAT co-activator P/CAF (p300/CBP-associated factor) reveals an unusual left-handed up-and-down four-helix bundle, and it is shown by a combination of structural and site-directed mutagenesis studies that bromidomains can interact specifically with acetylated lysine, making them the first known protein modules to do so.

TL;DR: In this article, the authors found that chromobox 7 (CBX7) within the polycomb repressive complex 1 binds to ANRIL, and both CBX7 and ANrIL are found at elevated levels in prostate cancer tissues.

TL;DR: Using structural and biochemical analyses, it is demonstrated that the PAZ domain binds a 5-nucleotide RNA with 1:1 stoichiometry and it is shown that PAZ domains from different human Argonaute proteins also bind RNA, establishing a conserved function for this domain.

TL;DR: The study indicates that the interaction with BRD4 is critical for the oncogenic function of Twist in BLBC, and Pharmacologic inhibition of the Twist-BRD4 association reduced WNT5A expression and suppressed invasion, cancer stem cell (CSC)-like properties, and tumorigenicity of BLBC cells.

TL;DR: The three-dimensional solution structures and biochemical analysis of DPF3b highlight the molecular basis of the integrated tandem PHD finger, which acts as one functional unit in the sequence-specific recognition of lysine-14-acetylated histone H3 (H3K14ac).