Structure of the human histone chaperone FACT Spt16 N-terminal domain

Marciano, G. and Huang, D.T. (2016) Structure of the human histone chaperone FACT Spt16 N-terminal domain. Acta Crystallographica. Section F: Structural Biology Communications, 72(2), pp. 121-128. (doi: 10.1107/s2053230x15024565) (PMID:26841762) (PMCID:PMC4741192)

Abstract

The histone chaperone FACT plays an important role in facilitating nucleosome assembly and disassembly during transcription. FACT is a heterodimeric complex consisting of Spt16 and SSRP1. The N-terminal domain of Spt16 resembles an inactive aminopeptidase. How this domain contributes to the histone chaperone activity of FACT remains elusive. Here, the crystal structure of the N-terminal domain (NTD) of human Spt16 is reported at a resolution of 1.84 A˚ . The structure adopts an aminopeptidase-like fold similar to those of the Saccharomyces cerevisiae and Schizosaccharomyces pombe Spt16 NTDs. Isothermal titration calorimetry analyses show that human Spt16 NTD binds histones H3/H4 with low-micromolar affinity, suggesting that Spt16 NTD may contribute to histone binding in the FACT complex. Surface-residue conservation and electrostatic analysis reveal a conserved acidic patch that may be involved in histone binding.

• Item Type: Articles
• Additional Information: This work was funded by Cancer Research UK. DTH was funded by ERC grant No. 647849.
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Marciano, Mr Gabriele and Huang, Professor Danny
• Authors: Marciano, G., and Huang, D.T.
• College/School: College of Medical Veterinary and Life Sciences > School of Cancer Sciences
• Journal Name: Acta Crystallographica. Section F: Structural Biology Communications
• Publisher: Wiley
• ISSN: 1744-3091
• ISSN (Online): 2053-230X
• Copyright Holders: Copyright © 2016 The Authors
• First Published: First published in Acta Crystallographica Section F Structural Biology Communications 72:121-128
• Publisher Policy: Reproduced under a Creative Commons licence