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

DOI: 10.1107/S2053230X15024565 DOI Help

Authors: Gabriele Marciano (Beatson Institute for Cancer Research) , Danny Huang (Beatson Institute for Cancer Research)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 72 , PAGES 121 - 128

State: Published (Approved)
Published: February 2016
Diamond Proposal Number(s): 8659

Open Access Open Access

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 Å. 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.

Journal Keywords: FACT; Spt16; histone chaperone; histones; pita-bread fold; aminopeptidase

Subject Areas: Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography