This is the dimerization domain found in structure-specific recognition protein SSRP1 (POB3 in yeast) and related proteins, which are components of the FACT complex - a general chromatin factor that acts to reorganise nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair [, , , ]. During transcription elongation the FACT complex acts as a histone chaperone that both destabilises and restores nucleosomal structure [, ].This domain has a Pleckstrin homology fold, made of 6 β-strands.
This domain is found at the N terminus of yeast POB3 and its metazoan homologue SSRP1 [, ]. POB3/SSRP1 is a subunit of the heterodimeric FACT complex involved in transcriptional initiation [, , ].
FACT (facilitates chromatin transactions) is a general chromatin factor that acts to reorganise nucleosomes. It is a complex that consists of several subunits [, , , ]. This entry represents the FACT complex subunits POB3, which is present in yeast, and the related SSRP1, found in higher eukaryotes. SSRP1 binds specifically to DNA modified with the anti-cancer drug cisplatin. It contains a high mobility group (HMG) box domain () that probably constitutes the structure recognition element for cisplatin-modified DNA, the probable recognition motif being the local duplex unwinding and bending that occurs on formation of intra-strand cross-links [, , ].
This is the dimerization domain found in structure-specific recognition protein SSRP1 (POB3 in yeast) and related proteins, which are components of the FACT complex - a general chromatin factor that acts to reorganise nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair [, , , ]. During transcription elongation the FACT complex acts as a histone chaperone that both destabilises and restores nucleosomal structure [, ].This domain has a Pleckstrin homology fold, made of 6 β-strands.
This entry represents a domain found in the middle region of several eukaryotic proteins [, ]. It is present in various FACT (facilitates chromatin transactions) complex subunits, such as Spt16 and either Pob3 (yeast) or the related SSRP1 (higher eukaryotes). FACT is a general chromatin factor that acts to reorganise nucleosomes [, ]. In these proteins, the middle domain shows a double pleckstrin homology (PH) configuration and plays a role in DNA binding [, , ]. This entry represents the second PH domain, which is also found in Rtt106p, a histone chaperone involved in heterochromatin-mediated silencing [].
