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Title: Structural and histone binding studies of the chromo barrel domain of TIP60

Journal Article · · FEBS Letters
 [1];  [2];  [1];  [3];  [4];  [3];  [3];  [4];  [2];  [2]
  1. Central China Normal Univ., Wuhan (China)
  2. Central China Normal Univ., Wuhan (China); Univ. of Toronto, ON (Canada)
  3. Univ. of Toronto, ON (Canada)
  4. Wuhan Sports Univ. (China)

Tat-interactive protein 60 consists of an N-terminal chromo barrel domain (TIP60-CB) and a C-terminal acetyltransferase domain and acetylates histone and nonhistone proteins in diverse cellular processes. While TIP60-CB is thought to recognize histone tails, molecular details of this interaction remain unclear. In this work, we attempted a quantitative analysis of the interaction between the human TIP60-CB and histone peptides, but did not observe any detectable binding by either fluorescence polarization or isothermal titration calorimetry assays. We also determined the crystal structure of the TIP60-CB alone. Analysis of the apo-tructure reveals a putative peptide-binding site that might be occluded by the basic side chain of a residue in a unique β hairpin between the two N-terminal strands of the β barrel, leading to the inability of TIP60-CB to bind histones.

Research Organization:
Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Organization:
USDOE Office of Science (SC), Biological and Environmental Research (BER); National Natural Science Foundation of China (NSFC); Hubei Chenguang Talented Youth Development Foundation; AbbVie; Bayer Pharma AG; Boehringer Ingelheim; Canada Foundation for Innovation; Eshelman Institute for Innovation; Genome Canada; Ontario Genomics Institute; Innovative Medicines Initiative; Janssen; Merck KGaA; MSD; Novartis Pharma AG; Ontario Ministry of Research, Innovation and Science (MRIS); Pfizer; São Paulo Research Foundation (FAPESP); Takeda; Wellcome
Grant/Contract Number:
AC02-06CH11357; 31500613; 115766
OSTI ID:
1439636
Alternate ID(s):
OSTI ID: 1464428
Journal Information:
FEBS Letters, Vol. 592, Issue 7; ISSN 0014-5793
Publisher:
Federation of European Biochemical SocietiesCopyright Statement
Country of Publication:
United States
Language:
ENGLISH
Citation Metrics:
Cited by: 6 works
Citation information provided by
Web of Science

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Cited By (1)