Literature DB >> 8628992

Intercalation, DNA kinking, and the control of transcription.

M H Werner1, A M Gronenborn, G M Clore.   

Abstract

Biological processes involved in the control and regulation of transcription are dependent on protein-induced distortions in DNA structure that enhance the recruitment of proteins to their specific DNA targets. This function is often accomplished by accessory factors that bind sequence specifically and locally bend or kink the DNA. The recent determination of the three-dimensional structures of several protein-DNA complexes, involving proteins that perform such architectural tasks, brings to light a common theme of side chain intercalation as a mechanism capable of driving the deformation of the DNA helix. The protein scaffolds orienting the intercalating side chain (or side chains) are structurally diverse, presently comprising four distinct topologies that can accomplish the same task. The intercalating side chain (or side chains), however, is exclusively hydrophobic. Intercalation can either kink or bend the DNA, unstacking one or more adjacent base pairs and locally unwinding the DNA over as much as a full turn of helix. Despite these distortions, the return to B-DNA helical parameters generally occurs within the adjacent half-turns of DNA.

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Year:  1996        PMID: 8628992     DOI: 10.1126/science.271.5250.778

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  68 in total

1.  Separate domains in E1 and E2 proteins serve architectural and productive roles for cooperative DNA binding.

Authors:  E Gillitzer; G Chen; A Stenlund
Journal:  EMBO J       Date:  2000-06-15       Impact factor: 11.598

2.  Two patches of amino acids on the E2 DNA binding domain define the surface for interaction with E1.

Authors:  G Chen; A Stenlund
Journal:  J Virol       Date:  2000-02       Impact factor: 5.103

3.  DNA-protein cooperative binding through variable-range elastic coupling.

Authors:  J Rudnick; R Bruinsma
Journal:  Biophys J       Date:  1999-04       Impact factor: 4.033

Review 4.  The structural basis of damaged DNA recognition and endonucleolytic cleavage for very short patch repair endonuclease.

Authors:  S E Tsutakawa; K Morikawa
Journal:  Nucleic Acids Res       Date:  2001-09-15       Impact factor: 16.971

5.  DNA exhibits multi-stranded binding recognition on glass microarrays.

Authors:  S J Shi; A Scheffer; E Bjeldanes; M A Reynolds; L J Arnold
Journal:  Nucleic Acids Res       Date:  2001-10-15       Impact factor: 16.971

6.  Determinants for hairpin formation in Tn10 transposition.

Authors:  J S Allingham; S J Wardle; D B Haniford
Journal:  EMBO J       Date:  2001-06-01       Impact factor: 11.598

7.  Effects of HU binding on the equilibrium cyclization of mismatched, curved, and normal DNA.

Authors:  Haribabu Arthanari; Kristi Wojtuszewski; Ishita Mukerji; Philip H Bolton
Journal:  Biophys J       Date:  2004-03       Impact factor: 4.033

8.  Two distinct overstretched DNA structures revealed by single-molecule thermodynamics measurements.

Authors:  Xinghua Zhang; Hu Chen; Hongxia Fu; Patrick S Doyle; Jie Yan
Journal:  Proc Natl Acad Sci U S A       Date:  2012-04-24       Impact factor: 11.205

9.  p53-induced DNA bending and twisting: p53 tetramer binds on the outer side of a DNA loop and increases DNA twisting.

Authors:  A K Nagaich; V B Zhurkin; S R Durell; R L Jernigan; E Appella; R E Harrington
Journal:  Proc Natl Acad Sci U S A       Date:  1999-03-02       Impact factor: 11.205

10.  Structure and dynamics of the DNA-binding protein HU of B. stearothermophilus investigated by Raman and ultraviolet-resonance Raman spectroscopy.

Authors:  Doinita Serban; Sandra F Arcineigas; Constantinos E Vorgias; George J Thomas
Journal:  Protein Sci       Date:  2003-04       Impact factor: 6.725

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