Pre-bending of a promoter sequence enhances affinity for the TATA-binding factor

TATA-binding protein (TBP) binds the minor groove of the TATA element with the DNA bent 80° towards the major groove1–4. A constrained minicircle strategy5 has been used to test the effect of DNA topology on the affinity of TBP for the TATA element. We report here that TBP bound to DNA which was slightly pre-bent towards the major groove with 100-fold higher affinity than unbent (linear) DNA of identical sequence and 300-fold higher affinity than DNA pre-bent towards the minor groove. Similar discrimination was observed with the holo-TFIID transcription complex. DNA topology, particularly bending, is determined by many factors including chromatin in cells and may, through changes in the affinity of the TATA factor, be important in the control of transcription.

[1]  D M Crothers,et al.  Protein-induced bending and DNA cyclization. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[2]  A. Berk,et al.  A mechanism for TAFs in transcriptional activation: activation domain enhancement of TFIID-TFIIA--promoter DNA complex formation. , 1994, Genes & development.

[3]  D. Bazett-Jones,et al.  Short-range DNA looping by the Xenopus HMG-box transcription factor, xUBF. , 1994, Science.

[4]  Steven Hahn,et al.  Crystal structure of a yeast TBP/TATA-box complex , 1993, Nature.

[5]  P. Sharp,et al.  Crystal structure of yeast TATA-binding protein and model for interaction with DNA. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[6]  D. K. Hawley,et al.  Kinetic analysis of yeast TFIID-TATA box complex formation suggests a multi-step pathway. , 1992, The Journal of biological chemistry.

[7]  Michael R. Green,et al.  Facilitated binding of TATA-binding protein to nucleosomal DNA , 1994, Nature.

[8]  Stephen K. Burley,et al.  Co-crystal structure of TBP recognizing the minor groove of a TATA element , 1993, Nature.

[9]  D. K. Hawley,et al.  TFIID binds in the minor groove of the TATA box , 1991, Cell.

[10]  A. Riggs,et al.  The lac repressor-operator interaction. 3. Kinetic studies. , 1970, Journal of molecular biology.

[11]  T. Maniatis,et al.  Mechanisms of transcriptional synergism between distinct virus-inducible enhancer elements , 1993, Cell.

[12]  M. Schmidt,et al.  Effect of the non-conserved N-terminus on the DNA binding activity of the yeast TATA binding protein. , 1993, Nucleic acids research.

[13]  P. Sharp,et al.  Yeast TATA-binding protein TFIID binds to TATA elements with both consensus and nonconsensus DNA sequences. , 1989, Proceedings of the National Academy of Sciences of the United States of America.

[14]  A. Riggs,et al.  The lac represser-operator interaction , 1970 .

[15]  M. Horikoshi,et al.  Transcription factor TFIID induces DNA bending upon binding to the TATA element. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[16]  Stephen K. Burley,et al.  1.9 Å resolution refined structure of TBP recognizing the minor groove of TATAAAAG , 1994, Nature Structural Biology.

[17]  Rudolf Grosschedl,et al.  The HMG domain of lymphoid enhancer factor 1 bends DNA and facilitates assembly of functional nucleoprotein structures , 1992, Cell.

[18]  D. Crothers,et al.  Determination of the extent of DNA bending by an adenine-thymine tract. , 1990, Biochemistry.

[19]  P. Sharp,et al.  Promoter specificity of basal transcription factors , 1992, Cell.

[20]  S. Burley,et al.  2.1 Å resolution refined structure of a TATA box-binding protein (TBP) , 1994, Nature Structural Biology.