Literature DB >> 7567918

DNA recognition and superstructure formation by helix-turn-helix proteins.

M Suzuki1, N Yagi, M Gerstein.   

Abstract

The way helix-turn-helix proteins recognize DNA is analysed by comparing their sequences, structures, and binding specificities. Individual recognition helices in these proteins bind to four DNA base pairs with the same geometry. However, pairs of recognition helices in the protein dimers can have different separations and orientations. These differences are used for discriminating between DNAs which have different superstructures, in particular, different numbers of base pairs between sets of the four base pairs.

Mesh:

Substances:

Year:  1995        PMID: 7567918     DOI: 10.1093/protein/8.4.329

Source DB:  PubMed          Journal:  Protein Eng        ISSN: 0269-2139


  12 in total

1.  Modeling helix-turn-helix protein-induced DNA bending with knowledge-based distance restraints.

Authors:  W S Tzou; M J Hwang
Journal:  Biophys J       Date:  1999-09       Impact factor: 4.033

2.  A study of the CopF repressor of plasmid pAMbeta1 by phage display.

Authors:  E d'Alençon; S D Ehrlich
Journal:  J Bacteriol       Date:  2000-05       Impact factor: 3.490

3.  Common fold in helix-hairpin-helix proteins.

Authors:  X Shao; N V Grishin
Journal:  Nucleic Acids Res       Date:  2000-07-15       Impact factor: 16.971

4.  A single gene on the staphylococcal multiresistance plasmid pSK1 encodes a novel partitioning system.

Authors:  Alice E Simpson; Ronald A Skurray; Neville Firth
Journal:  J Bacteriol       Date:  2003-04       Impact factor: 3.490

5.  The MtrR repressor binds the DNA sequence between the mtrR and mtrC genes of Neisseria gonorrhoeae.

Authors:  C E Lucas; J T Balthazar; K E Hagman; W M Shafer
Journal:  J Bacteriol       Date:  1997-07       Impact factor: 3.490

6.  Recognition of DNA by single-chain derivatives of the phage 434 repressor: high affinity binding depends on both the contacted and non-contacted base pairs.

Authors:  J Chen; S Pongor; A Simoncsits
Journal:  Nucleic Acids Res       Date:  1997-06-01       Impact factor: 16.971

Review 7.  Regulation of bacterial drug export systems.

Authors:  Steve Grkovic; Melissa H Brown; Ronald A Skurray
Journal:  Microbiol Mol Biol Rev       Date:  2002-12       Impact factor: 11.056

8.  Analysis of co-crystal structures to identify the stereochemical determinants of the orientation of TBP on the TATA box.

Authors:  M Suzuki; M D Allen; N Yagi; J T Finch
Journal:  Nucleic Acids Res       Date:  1996-07-15       Impact factor: 16.971

9.  Information-driven protein-DNA docking using HADDOCK: it is a matter of flexibility.

Authors:  Marc van Dijk; Aalt D J van Dijk; Victor Hsu; Rolf Boelens; Alexandre M J J Bonvin
Journal:  Nucleic Acids Res       Date:  2006-07-04       Impact factor: 16.971

10.  Regulatory circuit based on autogenous activation-repression: roles of C-boxes and spacer sequences in control of the PvuII restriction-modification system.

Authors:  Iwona Mruk; Preeti Rajesh; Robert M Blumenthal
Journal:  Nucleic Acids Res       Date:  2007-10-11       Impact factor: 16.971

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.