Literature DB >> 8028585

DNA cruciforms facilitate in vitro strand transfer on nucleosomal templates.

H Kotani1, E B Kmiec.   

Abstract

A single, phased nucleosome assembled on a 240 bp DNA duplex molecule blocked Escherichia coli RecA protein-promoted strand transfer of the complementary strand of the duplex onto a homologous single-stranded circle. However, when a four-armed cruciform structure was coupled to either end of the duplex the barrier to strand transfer was overcome and joint molecules were efficiently formed. Micrococcal nuclease digestion indicated that the nucleosome was dissociated by the juxtaposition of the cruciform. We interpret these results to mean that cruciform structures can act over a distance to destabilize adjacent nucleosomes and suggest that, as a consequence, the chromatin structure surrounding a crossed strand recombination intermediate might be disrupted, enabling other recombination events to initiate or the process of branch migration to proceed.

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Year:  1994        PMID: 8028585     DOI: 10.1007/bf00279578

Source DB:  PubMed          Journal:  Mol Gen Genet        ISSN: 0026-8925


  29 in total

1.  Patterns of nuclease protection during strand exchange. recA protein forms heteroduplex DNA by binding to strands of the same polarity.

Authors:  S A Chow; S M Honigberg; R J Bainton; C M Radding
Journal:  J Biol Chem       Date:  1986-05-25       Impact factor: 5.157

2.  By searching processively RecA protein pairs DNA molecules that share a limited stretch of homology.

Authors:  D K Gonda; C M Radding
Journal:  Cell       Date:  1983-09       Impact factor: 41.582

3.  Heteroduplex formation by recA protein: polarity of strand exchanges.

Authors:  S C West; E Cassuto; P Howard-Flanders
Journal:  Proc Natl Acad Sci U S A       Date:  1981-10       Impact factor: 11.205

4.  Polarity of heteroduplex formation promoted by Escherichia coli recA protein.

Authors:  R Kahn; R P Cunningham; C DasGupta; C M Radding
Journal:  Proc Natl Acad Sci U S A       Date:  1981-08       Impact factor: 11.205

5.  DNA motions in the nucleosome core particle.

Authors:  J Wang; M Hogan; R H Austin
Journal:  Proc Natl Acad Sci U S A       Date:  1982-10       Impact factor: 11.205

6.  The role of stable complexes that repress and activate eucaryotic genes.

Authors:  D D Brown
Journal:  Cell       Date:  1984-06       Impact factor: 41.582

7.  The pairing activity of stable nucleoprotein filaments made from recA protein, single-stranded DNA, and adenosine 5'-(gamma-thio)triphosphate.

Authors:  S M Honigberg; D K Gonda; J Flory; C M Radding
Journal:  J Biol Chem       Date:  1985-09-25       Impact factor: 5.157

8.  ATP-dependent DNA renaturation and DNA-dependent ATPase reactions catalyzed by the Ustilago maydis homologous pairing protein.

Authors:  E B Kmiec; W K Holloman
Journal:  Eur J Biochem       Date:  1994-02-01

9.  Homologous pairing of DNA molecules promoted by a protein from Ustilago.

Authors:  E Kmiec; W K Holloman
Journal:  Cell       Date:  1982-06       Impact factor: 41.582

10.  Nucleosomes inhibit both transcriptional initiation and elongation by RNA polymerase III in vitro.

Authors:  R H Morse
Journal:  EMBO J       Date:  1989-08       Impact factor: 11.598

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  3 in total

1.  Competence of an artificial bent DNA as a transcriptional activator in mouse ES cells.

Authors:  Jun-ichi Tanase; Tasuku Mitani; Koji Udagawa; Jun-ichi Nishikawa; Takashi Ohyama
Journal:  Mol Biol Rep       Date:  2010-03-20       Impact factor: 2.316

2.  Recognition and alignment of homologous DNA sequences between minichromosomes and single-stranded DNA promoted by RecA protein.

Authors:  J Ramdas; K Muniyappa
Journal:  Mol Gen Genet       Date:  1995-11-27

3.  Strand pairing by Rad54 and Rad51 is enhanced by chromatin.

Authors:  Vassilios Alexiadis; James T Kadonaga
Journal:  Genes Dev       Date:  2002-11-01       Impact factor: 11.361

  3 in total

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