Scaffold attachment factor B, also known as SAFB, is a gene with homologs that have been studied in humans and mice.[5]
Function
This gene encodes a DNA-binding protein that has specificity for scaffold or matrix attachment region DNA elements (S/MAR DNA). This protein is thought to be involved in attaching the base of chromatin loops to the nuclear matrix but there are conflicting views as to whether this protein is a component of chromatin, the nuclear matrix, or both. Scaffold attachment factors are a subset of nuclear matrix proteins (NMP) with enriched binding to AT-rich S/MAR sequences. The SAF-B protein is thought to serve as a molecular base to assemble a 'transcriptosome complex' in the vicinity of actively transcribed genes. It is involved in the regulation of the heat shock protein 27 transcription and also can act as an estrogen receptor corepressor. This gene is a candidate gene for breast tumorigenesis.[5]
^Arao Y, Kuriyama R, Kayama F, Kato S (August 2000). "A nuclear matrix-associated factor, SAF-B, interacts with specific isoforms of AUF1/hnRNP D". Arch. Biochem. Biophys. 380 (2): 228–36. doi:10.1006/abbi.2000.1938. PMID10933876.
Oesterreich S (2004). "Scaffold attachment factors SAFB1 and SAFB2: Innocent bystanders or critical players in breast tumorigenesis?". J. Cell. Biochem. 90 (4): 653–61. doi:10.1002/jcb.10685. PMID14587024. S2CID39178501.
Weighardt F, Cobianchi F, Cartegni L, Chiodi I, Villa A, Riva S, Biamonti G (1999). "A novel hnRNP protein (HAP/SAF-B) enters a subset of hnRNP complexes and relocates in nuclear granules in response to heat shock". J. Cell Sci. 112 (10): 1465–76. doi:10.1242/jcs.112.10.1465. PMID10212141.
Arao Y, Kuriyama R, Kayama F, Kato S (2000). "A nuclear matrix-associated factor, SAF-B, interacts with specific isoforms of AUF1/hnRNP D". Arch. Biochem. Biophys. 380 (2): 228–36. doi:10.1006/abbi.2000.1938. PMID10933876.
van den IJssel P, Wheelock R, Prescott A, Russell P, Quinlan RA (2003). "Nuclear speckle localisation of the small heat shock protein alpha B-crystallin and its inhibition by the R120G cardiomyopathy-linked mutation". Exp. Cell Res. 287 (2): 249–61. doi:10.1016/S0014-4827(03)00092-2. PMID12837281.
Tai HH, Geisterfer M, Bell JC, Moniwa M, Davie JR, Boucher L, McBurney MW (2003). "CHD1 associates with NCoR and histone deacetylase as well as with RNA splicing proteins". Biochem. Biophys. Res. Commun. 308 (1): 170–6. doi:10.1016/S0006-291X(03)01354-8. PMID12890497.