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 Resjournal_title
Nucleic acids researchauthors
Lia G,Semsey S,Lewis DE,Adhya S,Bensimon D,Dunlap D,Finzi Ldoi
10.1093/nar/gkn389subject
Has Abstractpub_date
2008-07-01 00:00:00pages
4204-10issue
12eissn
0305-1048issn
1362-4962pii
gkn389journal_volume
36pub_type
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