The antiparallel loops in gal DNA.

Abstract:

:Interactions between proteins bound to distant sites along a DNA molecule require bending and twisting deformations in the intervening DNA. In certain systems, the sterically allowed protein-DNA and protein-protein interactions are hypothesized to produce loops with distinct geometries that may also be thermodynamically and biologically distinct. For example, theoretical models of Gal repressor/HU-mediated DNA-looping suggest that the antiparallel DNA loops, A1 and A2, are thermodynamically quite different. They are also biologically different, since in experiments using DNA molecules engineered to form only one of the two loops, the A2 loop failed to repress in vitro transcription. Surprisingly, single molecule measurements show that both loop trajectories form and that they appear to be quite similar energetically and kinetically.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Lia G,Semsey S,Lewis DE,Adhya S,Bensimon D,Dunlap D,Finzi L

doi

10.1093/nar/gkn389

subject

Has Abstract

pub_date

2008-07-01 00:00:00

pages

4204-10

issue

12

eissn

0305-1048

issn

1362-4962

pii

gkn389

journal_volume

36

pub_type

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