منابع مشابه
Control of transcription of the repressor gene in bacteriophage lambda.
The rate of transcription of the structural gene for repressor (cI gene) in bacteriophage lambda is controlled by the amount of active repressor in the cell. When the (reversibly) thermolabile repressor in a bacterium lysogenic for lambdacI(857) is inactivated by heat, the rate of repressor gene transcription immediately falls. If the repressor is renatured, synthesis of repressor messenger is ...
متن کاملProteolytic cleavage of bacteriophage lambda repressor in induction.
The bacteriophage lambda repressor, a protein that maintains the lysogenic state of a bacterium containing a lambda prophage, is cleaved when the lysogen is induced by mitomycin C or ultraviolet light. This cleavage does not occur when induction is prevented by mutational alteration either of the phage repressor or of the host recA gene product. Proteolytic cleavage may be the primary mechanism...
متن کاملSolitons and Collapse in the lambda-repressor protein
The enterobacteria lambda phage is a paradigm temperate bacteriophage. Its lysogenic and lytic life cycles echo competition between the DNA binding λ-repressor (CI) and CRO proteins. Here we scrutinize the structure, stability and folding pathways of the λ-repressor protein, that controls the transition from the lysogenic to the lytic state. We first investigate the super-secondary helix-loophe...
متن کاملA fluorescence anisotropy study of tetramer-dimer equilibrium of lambda repressor and its implication for function.
Tetramer-dimer equilibrium of lambda repressor has been studied by fluorescence anisotropy techniques. We have chosen 1-dimethylamino naphthalene-5-sulfonyl chloride (dansyl chloride)-labeled repressor to study the dissociation-association equilibrium, because of relatively long life-time of the probe (> 10 ns). Polarization of the dansyl-labeled repressor decreases with decreasing protein conc...
متن کاملOne nanosecond molecular dynamics simulation of the N-terminal domain of the lambda repressor protein.
We have carried out molecular dynamics simulation of the N-terminal domain of the lambda repressor protein in a surrounding environment including explicit waters and ions. We observe two apparent dynamics substates in the nanosecond protein simulation, the transition occurring around 500 ps. The existence of these two apparent substates results from a high flexibility of the arm in each monomer...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section A Foundations of Crystallography
سال: 1981
ISSN: 0108-7673
DOI: 10.1107/s010876738109898x