2008 OSU Molecular Life Sciences
Interdisciplinary Graduate Programs Symposium
Poster abstracts
Abstract:
NASP (nuclear autoantigenic sperm protein), a member of the N1/N2 family of
histone chaperone proteins, has been described as a linker histone-binding protein. Here, we use traditional and affinity chromatography methods to test the binding specificity of recombinant human somatic NASP (sNASP) using purified proteins in vitro. Our analyses indicate that recombinant human sNASP
specifically associates with core histones H3 and H4. Also, there is no evidence for a direct interaction between sNASP and histone H1. The interaction between sNASP and histones H3 and H4 is functional as sNASP is active in in vitro chromatin assembly assays using histones depleted of H1.
Keywords: Histone Chaperone