Encyclopedia of AIDS

Living Edition
| Editors: Thomas J. Hope, Douglas Richman, Mario Stevenson


  • Xiaolei ZhuangEmail author
  • Robert Craigie
Living reference work entry
DOI: https://doi.org/10.1007/978-1-4614-9610-6_68-1


Barrier-to-autointegration factor (BAF or BANF1) is a highly conserved 10-KDa protein in multicellular eukaryotes. It was identified as a factor that blocks integration of Moloney murine leukemia virus DNA into itself (autointegration) in vitro. BAF binds DNA nonspecifically and, because it is a dimer, bridges together DNA molecules. BAF also binds the LEM domain, a domain that is shared among lamina-associated polypeptide 2, emerin, and MAN1. BAF is an essential cellular protein, and knockdown or knockout results in a defect in chromosome segregation during mitosis.


A role for barrier-to-autointegration factor (BAF or BANF1) in retroviral DNA integration was first inferred from in vitro experiments with Moloney murine leukemia virus. After entry of a virion into the cytoplasm of a newly infected cell, reverse transcriptionoccurs within the reverse transcription complex, a nucleoprotein complex derived from the core of the infecting virion. The resulting...


Total Internal Reflection Fluorescence Microscopy Reverse Transcription Complex Nuclear Envelope Assembly Sucrose Gradient Sedimentation Nuclear Envelope Formation 
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  1. Bengtsson L, Wilson KL. Barrier-to-autointegration factor phosphorylation on Ser-4 regulates emerin binding to lamin A in vitro and emerin localization in vivo. Mol Biol Cell. 2006;17:1154–63.PubMedCrossRefPubMedCentralGoogle Scholar
  2. Bradley CM, Ronning DR, Ghirlando R, Craigie R, Dyda F. Structural basis for DNA bridging by barrier-to-autointegration factor. Nat Struct Mol Biol. 2005;12:935–6.PubMedCrossRefGoogle Scholar
  3. Brown PO, Bowerman B, Varmus HE, Bishop JM. Correct integration of retroviral DNA in vitro. Cell. 1987;49:347–56.PubMedCrossRefGoogle Scholar
  4. Cai ML, Huang Y, Suh JY, Louis JM, Ghirlando R, Craigie R, Clore GM. Solution NMR structure of the barrier-to-autointegration factor-emerin complex. J Biol Chem. 2007;282:14525–35.PubMedCrossRefGoogle Scholar
  5. Farnet CM, Haseltine WA. Circularization of human immunodeficiency virus type 1 DNA in vitro. J Virol. 1991;65:6942–52.PubMedPubMedCentralGoogle Scholar
  6. Furukawa K. LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-chromatin interaction. J Cell Sci. 1999;112:2485–92.PubMedGoogle Scholar
  7. Furukawa K, Sugiyama S, Osouda S, Goto H, Inagaki M, Horigome T, Omata S, McConnell M, Fisher PA, Nishida Y. Barrier-to-autointegration factor plays crucial roles in cell cycle progression and nuclear organization in Drosophila. J Cell Sci. 2003;116:3811–23.PubMedCrossRefGoogle Scholar
  8. Gorjanacz M, Klerkx EPF, Galy V, Santarella R, Lopez-Iglesias C, Askjaer P, Mattaj IW. Caenorhabditis elegans BAF-1 and its kinase VRK-1 participate directly in post-mitotic nuclear envelope assembly. EMBO J. 2007;26:132–43.PubMedCrossRefPubMedCentralGoogle Scholar
  9. Huang Y, Cai ML, Clore GM, Craigie R. No interaction of barrier-to-autointegration factor (BAF) with HIV-1 MA, cone-rod homeobox (Crx) or MAN1-C in absence of DNA. PLoS One. 2011;6:e25123.PubMedCrossRefPubMedCentralGoogle Scholar
  10. Ibrahim N, Wicklund A, Wiebe MS. Molecular characterization of the host defense activity of the barrier to autointegration factor against vaccinia virus. J Virol. 2011;85:11588–600.PubMedCrossRefPubMedCentralGoogle Scholar
  11. Lee MS, Craigie R. Protection of retroviral DNA from autointegration: involvement of a cellular factor. Proc Natl Acad Sci U S A. 1994;91:9823–7.PubMedCrossRefPubMedCentralGoogle Scholar
  12. Lee MS, Craigie R. A previously unidentified host protein protects retroviral DNA from autointegration. Proc Natl Acad Sci U S A. 1998;95:1528–33.PubMedCrossRefPubMedCentralGoogle Scholar
  13. Lee KK, Haraguchi T, Lee RS, Koujin T, Hiraoka Y, Wilson KL. Distinct functional domains in emerin bind lamin A and DNA-bridging protein BAF. J Cell Sci. 2001;114:4567–73.PubMedGoogle Scholar
  14. Mansharamani M, Wilson KL. Direct binding of nuclear membrane protein MAN1 to emerin in vitro and two modes of binding to barrier-to-autointegration factor. J Biol Chem. 2005;280:13863–70.PubMedCrossRefGoogle Scholar
  15. Nichols RJ, Wiebe MS, Traktman P. The vaccinia-related kinases phosphorylate the N′ terminus of BAF, regulating its interaction with DNA and its retention in the nucleus. Mol Biol Cell. 2006;17:2451–64.PubMedCrossRefPubMedCentralGoogle Scholar
  16. Shumaker DK, Lee KK, Tanhehco YC, Craigie R, Wilson KL. LAP2 binds to BAF center dot DNA complexes: requirement for the LEM domain and modulation by variable regions. EMBO J. 2001;20:1754–64.PubMedCrossRefPubMedCentralGoogle Scholar
  17. Skoko D, Li M, Huang Y, Mizuuchi M, Cai ML, Bradley CM, Pease PJ, Xiao BT, Marko JF, Craigie R, et al. Barrier-to-autointegration factor (BAF) condenses DNA by looping. Proc Natl Acad Sci U S A. 2009;106:16610–5.PubMedCrossRefPubMedCentralGoogle Scholar
  18. Suzuki Y, Craigie R. Regulatory mechanisms by which barrier-to-autointegration factor locks autointegration and stimulates intermolecular integration of Moloney murine leukemia virus preintegration complexes. J Virol. 2002;76:12376–80.PubMedCrossRefPubMedCentralGoogle Scholar
  19. Suzuki Y, Ogawa K, Koyanagi Y, Suzuki Y. Functional disruption of the Moloney murine leukemia virus preintegration complex by vaccinia-related kinases. J Biol Chem. 2010;285:24032–43.PubMedCrossRefPubMedCentralGoogle Scholar
  20. Umland TC, Wei SQ, Craigie R, Davies DR. Structural basis of DNA bridging by barrier-to-autointegration factor. Biochemistry. 2000;39:9130–8.PubMedCrossRefGoogle Scholar
  21. Wang XJ, Xu SQ, Rivolta C, Li LY, Peng GH, Swain PK, Sung CH, Swaroop A, Berson EL, Dryja TP, et al. Barrier to autointegration factor interacts with the cone-rod homeobox and represses its transactivation function. J Biol Chem. 2002;277:43288–300.PubMedCrossRefGoogle Scholar
  22. Wiebe MS, Traktman P. Poxviral B1 kinase overcomes barrier to autointegration factor, a host defense against virus replication. Cell Host Microbe. 2007;1:187–97.PubMedCrossRefPubMedCentralGoogle Scholar
  23. Zheng RL, Ghirlando R, Lee MS, Mizuuchi K, Krause M, Craigie R. Barrier-to-autointegration factor (BAF) bridges DNA in a discrete, higher-order nucleoprotein complex. Proc Natl Acad Sci U S A. 2000;97:8997–9002.PubMedCrossRefPubMedCentralGoogle Scholar

Copyright information

© Springer Science+Business Media New York 2013

Authors and Affiliations

  1. 1.Protein Expression LaboratoryNational Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of HealthBethesdaUSA
  2. 2.Laboratory of Molecular BiologyNational Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of HealthBethesdaUSA