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The antiparallel loops in gal DNA

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  • Giuseppe Lia
  • Szabolcs Semsey
  • Dale E A Lewis
  • Sankar Adhya
  • David Bensimon
  • David Dunlap
  • Laura Finzi

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.

OriginalsprogEngelsk
TidsskriftNucleic Acids Research
Vol/bind36
Udgave nummer12
Sider (fra-til)4204-10
Antal sider7
ISSN0305-1048
DOI
StatusUdgivet - jul. 2008
Eksternt udgivetJa

ID: 163917635