Literature DB >> 10360363

Acceleration of the refolding of Arc repressor by nucleic acids and other polyanions.

D Rentzeperis1, T Jonsson, R T Sauer.   

Abstract

The refolding rate of the Arc repressor dimer can be accelerated 30-fold or more by negatively charged polymers including single-stranded and double-stranded DNA, RNA, and polyvinylsulfate but not by neutral or positively charged polymers. The salt-dependence of the polyanion-mediated process and mutant studies indicate that electrostatic interactions are important in the rate acceleration. Urea-dependence studies suggest that Arc is relatively unstructured in the transition state for polyanion-stimulated refolding. At low ionic strength, the observed kinetics of refolding are consistent with a model in which denatured Arc monomers bind rapidly and nonspecifically to the polyanion and complete folding in the bound state.

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Year:  1999        PMID: 10360363     DOI: 10.1038/9353

Source DB:  PubMed          Journal:  Nat Struct Biol        ISSN: 1072-8368


  22 in total

1.  DNA specificity enhanced by sequential binding of protein monomers.

Authors:  J J Kohler; S J Metallo; T L Schneider; A Schepartz
Journal:  Proc Natl Acad Sci U S A       Date:  1999-10-12       Impact factor: 11.205

2.  Speeding molecular recognition by using the folding funnel: the fly-casting mechanism.

Authors:  B A Shoemaker; J J Portman; P G Wolynes
Journal:  Proc Natl Acad Sci U S A       Date:  2000-08-01       Impact factor: 11.205

3.  Understanding the kinetic roles of the inducer heparin and of rod-like protofibrils during amyloid fibril formation by Tau protein.

Authors:  Gayathri Ramachandran; Jayant B Udgaonkar
Journal:  J Biol Chem       Date:  2011-09-19       Impact factor: 5.157

4.  A theoretical framework for gene induction and experimental comparisons.

Authors:  Karen M Ong; John A Blackford; Benjamin L Kagan; S Stoney Simons; Carson C Chow
Journal:  Proc Natl Acad Sci U S A       Date:  2010-03-29       Impact factor: 11.205

5.  Kinetic analysis of the interaction of b/HLH/Z transcription factors Myc, Max, and Mad with cognate DNA.

Authors:  Ozgur Ecevit; Mateen A Khan; Dixie J Goss
Journal:  Biochemistry       Date:  2010-03-30       Impact factor: 3.162

6.  N-terminal domains of native multidomain proteins have the potential to assist de novo folding of their downstream domains in vivo by acting as solubility enhancers.

Authors:  Chul Woo Kim; Kyoung Sim Han; Ki-Sun Ryu; Byung Hee Kim; Kyun-Hwan Kim; Seong Il Choi; Baik L Seong
Journal:  Protein Sci       Date:  2007-04       Impact factor: 6.725

7.  Arc-repressor dimerization on DNA: folding rate enhancement by colocalization.

Authors:  Amir Marcovitz; Yaakov Levy
Journal:  Biophys J       Date:  2009-05-20       Impact factor: 4.033

8.  The GCN4 bZIP targets noncognate gene regulatory sequences: quantitative investigation of binding at full and half sites.

Authors:  I-San Chan; Anna V Fedorova; Jumi A Shin
Journal:  Biochemistry       Date:  2007-02-13       Impact factor: 3.162

9.  The folding competence of HIV-1 Tat mediated by interaction with TAR RNA.

Authors:  Jung Min Kim; Hee Sun Choi; Baik Lin Seong
Journal:  RNA Biol       Date:  2017-04-18       Impact factor: 4.652

10.  DNA-mediated assembly of weakly interacting DNA-binding protein subunits: in vitro recruitment of phage 434 repressor and yeast GCN4 DNA-binding domains.

Authors:  Corrado Guarnaccia; Bakthisaran Raman; Sotir Zahariev; András Simoncsits; Sándor Pongor
Journal:  Nucleic Acids Res       Date:  2004-09-23       Impact factor: 16.971

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