Structure-specific recognition protein-1 (SSRP1) is an elongated homodimer that binds histones

Gabriele Marciano, Stefano Da Vela, Giancarlo Tria, Dmitri I. Svergun, Olwyn Byron, Danny T. Huang

Research output: Contribution to journalArticleAcademicpeer-review

Original languageEnglish
Pages (from-to)10071-10083
Number of pages13
JournalJournal of Biological Chemistry
Volume293
Issue number26
DOIs
Publication statusPublished - 29 Jun 2018

Keywords

  • analytical ultracentrifugation
  • small-angle X-ray scattering (SAXS)
  • histone chaperone
  • oligomerization
  • histone
  • H2A-H2B
  • H3-H4
  • homodimer
  • SSRP1
  • SMALL-ANGLE SCATTERING
  • DNA-POLYMERASE ALPHA
  • N-TERMINAL DOMAIN
  • CHAPERONE FACT
  • SACCHAROMYCES-CEREVISIAE
  • TRANSCRIPTIONAL ACTIVATION
  • NUCLEOSOME REORGANIZATION
  • CHROMATIN
  • REPLICATION
  • SPT16

Cite this

Marciano, G., Da Vela, S., Tria, G., Svergun, D. I., Byron, O., & Huang, D. T. (2018). Structure-specific recognition protein-1 (SSRP1) is an elongated homodimer that binds histones. Journal of Biological Chemistry, 293(26), 10071-10083. https://doi.org/10.1074/jbc.RA117.000994