Barrier-to-autointegration factor

From Wikipedia, the free encyclopedia
Jump to navigation Jump to search
PDB 1ci4 EBI.jpg
the crystal structure of human barrier-to-autointegration factor (baf)

In molecular biology, barrier-to-autointegration factor (BAF) is a family of essential proteins that is highly conserved in metazoan evolution, and which may act as DNA-bridging proteins.[1] BAF binds directly to double-stranded DNA, to transcription activators, and to inner nuclear membrane proteins, including lamin A filaments that anchor nuclear pore complexes in place, and nuclear LEM-domain proteins that bind to laminin filaments and chromatin. New findings suggest that BAF has structural roles in nuclear assembly and chromatin organization, represses gene expression and might interlink chromatin structure, nuclear architecture and gene regulation in metazoans.[2]

BAF can be exploited by retroviruses to act as a host component of pre-integration complexes, which promote the integration of the retroviral DNA into the host chromosome by preventing autointegration (integration into itself).[3] BAF might contribute to the assembly or activity of retroviral pre-integration complexes through direct binding to the retroviral proteins p55 Gag and matrix, as well as to DNA.


  1. ^ Furukawa K, Sugiyama S, Osouda S, Goto H, Inagaki M, Horigome T, Omata S, McConnell M, Fisher PA, Nishida Y (September 2003). "Barrier-to-autointegration factor plays crucial roles in cell cycle progression and nuclear organization in Drosophila". J. Cell Sci. 116 (Pt 18): 3811–23. doi:10.1242/jcs.00682. PMID 12902403.
  2. ^ Segura-Totten M, Wilson KL (May 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. PMID 15130582.
  3. ^ Mansharamani M, Graham DR, Monie D, Lee KK, Hildreth JE, Siliciano RF, Wilson KL (December 2003). "Barrier-to-autointegration factor BAF binds p55 Gag and matrix and is a host component of human immunodeficiency virus type 1 virions". J. Virol. 77 (24): 13084–92. doi:10.1128/jvi.77.24.13084-13092.2003. PMC 296067. PMID 14645565.
This article incorporates text from the public domain Pfam and InterPro: IPR004122