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

Article English OPEN
Marciano, G. ; Huang, D.T. (2016)
  • Publisher: Wiley
  • Journal: Acta Crystallographica. Section F, Structural Biology Communications (vol: 72, pp: 121-128)
  • Related identifiers: doi: 10.1107/s2053230x15024565, pmc: PMC4741192
  • Subject: FACT | histones | Spt16 | aminopeptidase | pita-bread fold | histone chaperone | Research Communications
    mesheuropmc: congenital, hereditary, and neonatal diseases and abnormalities

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