Results 281 to 290 of about 188,329 (316)

Regulation in repressor inactivation by RecA protein

Advances in Biophysics, 1990
Treatments that damage DNA or inhibit DNA synthesis in E. coli induce the expression of a set of functions called SOS functions that are involved in DNA repair, mutagenesis, arrest of cell division and prophage induction. Induction of SOS functions is triggered by inactivation of the LexA repressor or a phage repressor. Inactivation of these repressors
H, Ogawa, T, Ogawa
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PIAS Proteins as Repressors of Oct4 Function

Journal of Molecular Biology, 2007
The POU domain transcription factor Oct4 plays essential functions in the maintenance of pluripotent embryonic and germ cells of mammals. Molecular mechanisms of Oct4 action remain poorly understood. To isolate modulators of Oct4 activity, we performed a yeast two-hybrid screen with the Oct4 POU domain as a bait and isolated PIASy as an Oct4 ...
Tolkunova, E., Malashicheva, A., Parfenov, V., Sustmann, C., Grosschedl, R., Tomilin, A.   +5 more
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Escherichia coli Repressor Proteins

1989
Genetic regulation is an essential function in all living organisms. In prokaryotes genetic control provides responsivity to a constantly changing external milieu, and bacterial systems have proved extremely valuable in elucidating the variety of potential mechanisms.
Kyle L. Wick, Kathleen S. Matthews
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Ultraviolet difference spectra of the lactose repressor protein

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1973
Abstract Ultraviolet difference spectra of the lactose repressor have been studied under various conditions. Changes in the aromatic residues of the protein upon addition of inducers, but not anti-inducers, are found. The extent of exposure of aromatic residues to solvent perturbation is also found to differ in the presence of inducers and anti ...
K S, Matthews, H R, Matthews, H W, Thielmann, G, Jardetzky   +3 more
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Lactose Repressor Protein: Functional Properties and Structure

1997
The lactose repressor protein (LacI), the prototype for genetic regulatory proteins, controls expression of lactose metabolic genes by binding to its cognate operator sequences in E. coli DNA. Inducer binding elicits a conformational change that diminishes affinity for operator sequences with no effect on nonspecific binding. The release of operator is
K S, Matthews, J C, Nichols
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Lac repressor is a transient gene-activating protein

Cell, 1987
We show, using a combination of methods, that contrary to the usual view, lac repressor increases, by more than 100-fold, the initial binding of RNA polymerase to E. coli lac UV5 promoter DNA. Kinetic studies revealed that the repressor acts to block the isomerization step in transcription initiation.
S B, Straney, D M, Crothers
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Trp repressor protein controls its own structural gene

Journal of Molecular Biology, 1981
Abstract To study the regulation of expression of the trpR gene of Escherichia coli , fused transcriptional units consisting of the promoter-operator region of trpR and a functional but promoterless lacZ gene were constructed by techniques of cleavage and ligation in vitro .
G, Bogosian, K, Bertrand, R, Somerville
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Lactose repressor protein reaction with 2-chloromercuri-4-nitrophenol

Journal of Molecular Biology, 1976
Abstract Reaction of the lactose repressor protein with 2-chloromercuri-4-nitrophenol resulted in modification of two of the three cysteine residues per monomer at all pH values tested. At pH 8.1 it was possible to detect two equivalence points, corresponding to one and two mercurinitrophenol residues introduced per monomer.
D S, Yang, K S, Matthews
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Leukemia fusion proteins and co‐repressor complexes: Changing paradigms

Journal of Cellular Biochemistry, 2005
AbstractMany cases of acute myelogenous leukemia (AML) are characterized by non‐random chromosomal translocations that fuse a DNA‐binding protein with a transcriptional regulator, which in turn may aberrantly recruit a co‐repressor complex. The similarities in this pattern between different AML chimeric fusions have led to a paradigm that stresses the ...
Robert L, Redner, Johnson M, Liu
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Modification of tyrosine residues of the lactose repressor protein

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1977
Reaction of the lactose repressor protein from Escherichia coli with high molar excesses (up to 800 fold) of tetranitromethane resulted in modification of tyrosine residues in the amino-terminal and core regions of the molecule. Tyrosines 7 and 17 exhibit significant reactivity at low levels (5-10 fold molar excess) of tetranitromethane.
M E, Alexander, A A, Burgum, R A, Noall, M D, Shaw, K S, Matthews   +4 more
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