In molecular biology, the ASF1 like histone chaperone family of proteins includes the yeast and human ASF1 proteins. These proteins are of the chaperone protein group and in particular can be placed into the histone chaperone subgroup.[1] ASF1 participates in both the replication-dependent and replication-independent pathways. The three-dimensional structure has been determined as a compact immunoglobulin-like beta sandwich fold topped by three helical linkers.[2]
| ASF1_hist_chap | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of the cia- histone h3-h4 complex | |||||||||
| Identifiers | |||||||||
| Symbol | ASF1_hist_chap | ||||||||
| Pfam | PF04729 | ||||||||
| Pfam clan | CL0463 | ||||||||
| InterPro | IPR006818 | ||||||||
| SCOP2 | 1roc / SCOPe / SUPFAM | ||||||||
| |||||||||
References
edit- ^ Daganzo SM, Erzberger JP, Lam WM, Skordalakes E, Zhang R, Franco AA, Brill SJ, Adams PD, Berger JM, Kaufman PD (December 2003). "Structure and function of the conserved core of histone deposition protein Asf1". Curr. Biol. 13 (24): 2148–58. doi:10.1016/j.cub.2003.11.027. PMID 14680630. S2CID 15164132.
- ^ Munakata T, Adachi N, Yokoyama N, Kuzuhara T, Horikoshi M (March 2000). "A human homologue of yeast anti-silencing factor has histone chaperone activity". Genes Cells. 5 (3): 221–33. doi:10.1046/j.1365-2443.2000.00319.x. PMID 10759893. S2CID 20198031.