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Publication Abstract from PubMed

The histone chaperone FACT is an essential and abundant heterodimer found in all eukaryotes. Here we report a crystal structure of the middle domain of the large subunit of FACT (Spt16-M), revealing a double pleckstrin homology architecture. This motif was found previously in the Pob3-M domain of the small subunit of FACT, as well as in the related histone chaperone Rtt106, although Spt16-M is distinguished from these structures by the presence of an extended alpha-helix and a C-terminal addition. Consistent with our finding that the double pleckstrin homology structure is common to these three histone chaperone proteins and reports that Pob3 and Rtt106 double PH domains bind histones H3-H4, we also find that Spt16-M binds H3-H4 with low micromolar affinity. Our structure provides a framework for interpreting a large body of genetic data regarding the physiological functions of FACT, including the identification of potential interaction surfaces for binding histones or other proteins. We also describe a set of intragenic suppressors of a mutation of SPT16 that reveal important structural features of Spt16-M.

Structure of the Spt16 Middle Domain Reveals Functional Features of the Histone Chaperone FACT.,Kemble DJ, Whitby FG, Robinson H, McCullough LL, Formosa T, Hill CP J Biol Chem. 2013 Feb 15. PMID:23417676^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.