The protein encoded by this gene was identified by its ability to protect retroviruses from intramolecular integration and therefore promote intermolecular integration into the host cell genome. The endogenous function of the protein is unknown. The protein forms a homodimer which localizes to the nucleus and is specifically associated with chromosomes during mitosis. This protein binds to DNA in a non-specific manner and studies in rodents suggest that it also binds to lamina-associated polypeptide 2, a component of the nuclear lamina.[2] It also associates with the LEM Domain containing proteins LAP2, Emerin, and MAN1.
↑Furukawa K (August 1999). "LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-chromatin interaction". J. Cell Sci. 112 (Pt 15): 2485–92. PMID10393804.
Goldberg M, Harel A, Gruenbaum Y (2000). "The nuclear lamina: molecular organization and interaction with chromatin". Crit. Rev. Eukaryot. Gene Expr. 9 (3–4): 285–93. doi:10.1615/critreveukargeneexpr.v9.i3-4.130. PMID10651245.
Segura-Totten M, Wilson KL (2004). "BAF: roles in chromatin, nuclear structure and retrovirus integration". Trends Cell Biol. 14 (5): 261–6. doi:10.1016/j.tcb.2004.03.004. PMID15130582.
Van Maele B, Debyser Z (2005). "HIV-1 integration: an interplay between HIV-1 integrase, cellular and viral proteins". AIDS reviews. 7 (1): 26–43. PMID15875659.
Van Maele B, Busschots K, Vandekerckhove L, et al. (2006). "Cellular co-factors of HIV-1 integration". Trends Biochem. Sci. 31 (2): 98–105. doi:10.1016/j.tibs.2005.12.002. PMID16403635.
Dear PH, Bankier AT, Piper MB (1998). "A high-resolution metric HAPPY map of human chromosome 14". Genomics. 48 (2): 232–41. doi:10.1006/geno.1997.5140. PMID9521877.
Lynch RA, Piper M, Bankier A, et al. (1999). "Genomic and functional map of the chromosome 14 t(12;14) breakpoint cluster region in uterine leiomyoma". Genomics. 52 (1): 17–26. doi:10.1006/geno.1998.5406. PMID9740667.
Cai M, Huang Y, Zheng R, et al. (1998). "Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration". Nat. Struct. Biol. 5 (10): 903–9. doi:10.1038/2345. PMID9783751.
Furukawa K (1999). "LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-chromatin interaction". J. Cell Sci. 112 (15): 2485–92. PMID10393804.
Umland TC, Wei SQ, Craigie R, Davies DR (2000). "Structural basis of DNA bridging by barrier-to-autointegration factor". Biochemistry. 39 (31): 9130–8. doi:10.1021/bi000572w. PMID10924106.
Harris D, Engelman A (2001). "Both the structure and DNA binding function of the barrier-to-autointegration factor contribute to reconstitution of HIV type 1 integration in vitro". J. Biol. Chem. 275 (50): 39671–7. doi:10.1074/jbc.M002626200. PMID11005805.
Lee KK, Haraguchi T, Lee RS, et al. (2002). "Distinct functional domains in emerin bind lamin A and DNA-bridging protein BAF". J. Cell Sci. 114 (Pt 24): 4567–73. PMID11792821.
Haraguchi T, Koujin T, Segura-Totten M, et al. (2002). "BAF is required for emerin assembly into the reforming nuclear envelope". J. Cell Sci. 114 (Pt 24): 4575–85. PMID11792822.
Holaska JM, Lee KK, Kowalski AK, Wilson KL (2003). "Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro". J. Biol. Chem. 278 (9): 6969–75. doi:10.1074/jbc.M208811200. PMID12493765.
1qck: SOLUTION STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR BAF, NMR, REGULARIZED MEAN STRUCTURE PLUS 20 INDIVIDUAL SIMULATED ANNEALING STRUCTURES