The B3 DNA binding domain (DBD) is a highly conserved domain found exclusively in transcription factors, from higher plants (≥40 species) (Pfam PF02362) combined with other domains (InterPro: IPR003340). It consists of 100-120 residues, includes seven beta strands and two alpha helices that form a DNA-binding pseudobarrel protein fold (SCOP 117343); it interacts with the major groove of DNA.[1]

B3 families

In Arabidopsis thaliana, there are three main families of transcription factors that contain B3 domain:[2]

  • ARF (Auxin Response Factors)
  • ABI3 (ABscisic acid Insensitive3)
  • RAV (Related to ABI3/VP1)
protein ARF1-B3 ABI3-B3 RAV1-B3
B3 structure derived by molecular model[1] molecular model[1] NMR[1]
B3 recognition sequence TGTCTC[3][4] CATGCA[5][6] CACCTG[7]

PDB: 1WID[1] and PDB: 1YEL[8] are only known NMR solution phase structures of the B3 DNA Binding Domain.

Related proteins

The N-terminal domain of restriction endonuclease EcoRII; the C-terminal domain of restriction endonuclease BfiI possess a similar DNA-binding pseudobarrel protein fold.[9][10]

See also


  1. ^ a b c d e Yamasaki K, Kigawa T, Inoue M, Tateno M, Yamasaki T, Yabuki T, Aoki M, Seki E, Matsuda T, Tomo Y, Hayami N, Terada T, Shirouzu M, Osanai T, Tanaka A, Seki M, Shinozaki K, Yokoyama S (2004). "Solution Structure of the B3 DNA Binding Domain of the Arabidopsis Cold-Responsive Transcription Factor RAV1". Plant Cell. 16 (12): 3448–59. doi:10.1105/tpc.104.026112. PMC 535885Freely accessible. PMID 15548737. 
  2. ^ Riechmann JL, Heard J, Martin G, Reuber L, Jiang C, Keddie J, Adam L, Pineda O, Ratcliffe OJ, Samaha RR, Creelman R, Pilgrim M, Broun P, Zhang JZ, Ghandehari D, Sherman BK, Yu G (2000). "Arabidopsis transcription factors: genome-wide comparative analysis among eukaryotes". Science. 290 (5499): 2105–10. doi:10.1126/science.290.5499.2105. PMID 11118137. 
  3. ^ Ulmasov T, Hagen G, Guilfoyle TJ (1997). "ARF1, a transcription factor that binds to auxin response elements". Science. 276 (5320): 1865–8. doi:10.1126/science.276.5320.1865. PMID 9188533. 
  4. ^ Tiwari SB, Hagen G, Guilfoyle TJ (2003). "The Roles of Auxin Response Factor Domains in Auxin-Responsive Transcription". Plant Cell. 15 (2): 533–43. doi:10.1105/tpc.008417. PMC 141219Freely accessible. PMID 12566590. 
  5. ^ Suzuki M, Kao CY, McCarty DR (1997). "The conserved B3 domain of VIVIPAROUS1 has a cooperative DNA binding activity". Plant Cell. 9 (5): 799–807. doi:10.1105/tpc.9.5.799. PMC 156957Freely accessible. PMID 9165754. 
  6. ^ Ezcurra I, Wycliffe P, Nehlin L, Ellerström M, Rask L (2000). "Transactivation of the Brassica napus napin promoter by ABI3 requires interaction of the conserved B2 and B3 domains of ABI3 with different cis-elements: B2 mediates activation through an ABRE, whereas B3 interacts with an RY/G-box". Plant J. 24 (1): 57–66. doi:10.1046/j.1365-313x.2000.00857.x. PMID 11029704. 
  7. ^ Kagaya Y, Ohmiya K, Hattori T (1999). "RAV1, a novel DNA-binding protein, binds to bipartite recognition sequence through two distinct DNA-binding domains uniquely found in higher plants". Nucleic Acids Res. 27 (2): 470–8. doi:10.1093/nar/27.2.470. PMC 148202Freely accessible. PMID 9862967. 
  8. ^ Waltner, J.K.; Peterson, F.C.; Lytle, B.L.; Volkman, B.F. (2005). "Structure of the B3 domain from Arabidopsis thaliana protein At1g16640". Protein Sci. 14 (9): 2478–83. doi:10.1110/ps.051606305. PMC 2253459Freely accessible. PMID 16081658. 
  9. ^ Zhou XE, Wang Y, Reuter M, Mücke M, Krüger DH, Meehan EJ, Chen L (2004). "Crystal structure of type IIE restriction endonuclease EcoRII reveals an autoinhibition mechanism by a novel effector-binding fold". J. Mol. Biol. 335 (1): 307–19. doi:10.1016/j.jmb.2003.10.030. PMID 14659759. 
  10. ^ Grazulis S, Manakova E, Roessle M, Bochtler M, Tamulaitiene G, Huber R, Siksnys V (2005). "Structure of the metal-independent restriction enzyme BfiI reveals fusion of a specific DNA-binding domain with a nonspecific nuclease". Proc. Natl. Acad. Sci. U.S.A. 102 (44): 15797–802. doi:10.1073/pnas.0507949102. PMC 1266039Freely accessible. PMID 16247004. 

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