Response: DNA Looping and Lac Repressor--CAP Interaction
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چکیده
منابع مشابه
Modeling the Lac repressor-operator assembly: the influence of DNA looping on Lac repressor conformation.
Repression of transcription of the Escherichia coli Lac operon by the Lac repressor (LacR) is accompanied by the simultaneous binding of LacR to two operators and the formation of a DNA loop. A recently developed theory of sequence-dependent DNA elasticity enables one to relate the fine structure of the LacR-DNA complex to a wide range of heretofore-unconnected experimental observations. Here, ...
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The 50th anniversary of Biopolymers coincides closely with the like celebration of the discovery of the Escherichia coli (lac) lactose operon, a classic genetic system long used to illustrate the influence of biomolecular structure on function. The looping of DNA induced by the binding of the Lac repressor protein to sequentially distant operator sites on DNA continues to serve as a paradigm fo...
متن کاملTwo helix DNA binding motif of CAP found in lac repressor and gal repressor.
Comparison of both the DNA and protein sequences of catabolite gene activator protein (CAP) with the sequences of lac and gal repressors shows significant homologies between a sequence that forms a two alpha-helix motif in CAP and sequences near the amino terminus of both repressors. This two-helix motif is thought to be involved in specific DNA sequence recognition by CAP. The region in lac re...
متن کاملLac repressor hinge flexibility and DNA looping: single molecule kinetics by tethered particle motion
The tethered particle motion (TPM) allows the direct detection of activity of a variety of biomolecules at the single molecule level. First pioneered for RNA polymerase, it has recently been applied also to other enzymes. In this work we employ TPM for a systematic investigation of the kinetics of DNA looping by wild-type Lac repressor (wt-LacI) and by hinge mutants Q60G and Q60 + 1. We impleme...
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ژورنال
عنوان ژورنال: Science
سال: 1996
ISSN: 0036-8075,1095-9203
DOI: 10.1126/science.274.5294.1931