Results 221 to 230 of about 115,119 (230)
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LexA and λ Cl repressors as enzymes: Specific cleavage in an intermolecular reaction
Cell, 1993During the SOS response, LexA repressor is inactivated by specific cleavage. Although cleavage requires RecA protein in vivo, RecA acts indirectly as a coprotease by stimulating an inherent self-cleavage activity of LexA. In lambda lysogens, cleavage of lambda Cl repressor in a similar but far slower reaction results in prophage induction.
Baek Kim, John W. Little
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LexA, the Self-Cleaving Transcriptional Repressor of the SOS System
1993All living organisms are permanently exposed to variable amounts of chemical or physical agents which can form adducts with the cellular constituents. A particularly sensitive target is DNA due to its low copy number and its central role in the storage and readout of information for setting up the cell.
M. Granger-Schnarr, M. Schnarr
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Biochemistry, 1985
A rapid large-scale procedure for the purification of the LexA repressor of Escherichia coli is described. This procedure allows one to get more than 100 mg of purified protein from 100 g of bacterial paste with a purity of at least 97%. This method is comparable to earlier, far more complicated purification procedures giving clearly smaller yields. It
Michèle Granger-Schnarr +3 more
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A rapid large-scale procedure for the purification of the LexA repressor of Escherichia coli is described. This procedure allows one to get more than 100 mg of purified protein from 100 g of bacterial paste with a purity of at least 97%. This method is comparable to earlier, far more complicated purification procedures giving clearly smaller yields. It
Michèle Granger-Schnarr +3 more
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Biochemistry, 1991
An increasing number of eukaryotic transcription factors interacting specifically with DNA comprise a dimerization motif called the "leucine zipper".
Thomas Schmidt-Dorr +5 more
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An increasing number of eukaryotic transcription factors interacting specifically with DNA comprise a dimerization motif called the "leucine zipper".
Thomas Schmidt-Dorr +5 more
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The protein HU can displace the LexA repressor from its DNA‐binding sites
Molecular Microbiology, 1994SummaryThe major bacterial histone‐like protein HU is a small, basic, dimeric protein composed of two closely related subunits. HU is involved in several processes in the bacterial cell such as the initiation of replication, transposition, gene inversion and cell division.
Annie Boullard +4 more
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Isolation and characterization of LexA mutant repressers with enhanced DNA binding affinity
Journal of Molecular Biology, 1992The LexA repressor from Escherichia coli is a sequence-specific DNA binding protein that shows no pronounced sequence homology with any of the known structural motifs involved in DNA binding. Since little is known about how this protein interacts with DNA, we have selected and characterized a great number of intragenic, second-site mutations which ...
Michèle Granger-Schnarr +3 more
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The LexA-RecA* structure reveals a cryptic lock-and-key mechanism for SOS activation.
Nature Structural & Molecular BiologyMichael B. Cory +11 more
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Classic Protein With a New Twist: crystal structure of a LexA repressor DNA complex
, 2010A.P.P. Zhang, Y. Pigli, P. Rice
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