Related ArticlesNMR studies of the Escherichia coli Trp repressor.trpRs operator complex.
Eur J Biochem. 1996 Dec 15;242(3):567-75
Authors: Evans PD, Jaseja M, Jeeves M, Hyde EI
To understand the specificity of the Escherichia coli Trp repressor for its operators, we have begun to study complexes of the protein with alternative DNA sequences, using 1H-NMR spectroscopy. We report here the 1H-NMR chemical shifts of a 20-bp oligodeoxynucleotide containing the sequence of a symmetrised form of the trpR operator in the presence and absence of the holorepressor. Deuterated protein was used to assign the spectrum of the oligodeoxynucleotide in a 37-kDa complex with the Trp holorepressor. Many of the resonances of the DNA shift on binding to the protein, which suggests changes in conformation throughout the sequence. The largest changes in shifts for the aromatic protons in the major groove are for A15 and G16, which are thought to hydrogen bond to the protein, possibly via water molecules. We have also examined the effect of DNA binding on the corepressor, tryptophan, in this complex. The indole proton resonance of the tryptophan undergoes a downfield shift of 1.2 ppm upon binding of DNA. This large shift is consistent with hydrogen bonding of the tryptophan to the phosphate backbone of the trpR operator DNA, as in the crystal structure of the holoprotein with the trp operator.
[NMR paper] Trp repressor-operator binding: NMR and electrophoretic mobility shift studies of the
Trp repressor-operator binding: NMR and electrophoretic mobility shift studies of the effect of DNA sequence and corepressor binding on two Trp repressor-operator complexes.
Related Articles Trp repressor-operator binding: NMR and electrophoretic mobility shift studies of the effect of DNA sequence and corepressor binding on two Trp repressor-operator complexes.
Biochemistry. 2002 Dec 17;41(50):14866-78
Authors: Jaseja M, Jeeves M, Hyde EI
In Trp repressor-DNA complexes, most interactions either occur with phosphate groups or are...
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[NMR paper] Structure and dynamics of the lac repressor-operator complex as determined by NMR.
Structure and dynamics of the lac repressor-operator complex as determined by NMR.
Related Articles Structure and dynamics of the lac repressor-operator complex as determined by NMR.
Toxicol Lett. 1995 Dec;82-83:591-9
Authors: Kaptein R, Slijper M, Boelens R
The structures of the lac repressor headpiece and of its complex with an 11 base-pair lac half-operator have been determined by NMR spectroscopy. By 15N relaxation studies the dynamic behavior of the free protein and of the protein in the complex could be established. In the three-helical...
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[NMR paper] Rapid corepressor exchange from the trp-repressor/operator complex: an NMR study of [
Rapid corepressor exchange from the trp-repressor/operator complex: an NMR study of -L-tryptophan.
Related Articles Rapid corepressor exchange from the trp-repressor/operator complex: an NMR study of -L-tryptophan.
J Biomol NMR. 1995 Jun;5(4):367-75
Authors: Lee W, Revington M, Farrow NA, Nakamura A, Utsunomiya-Tate N, Miyake Y, Kainosho M, Arrowsmith CH
-L-tryptophan was prepared biosynthetically and its dynamic properties and intermolecular interaction with a complex of Escherichia coli trp-repressor and a 20 base-pair operator DNA were...
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[NMR paper] The interactions of Escherichia coli trp repressor with tryptophan and with an operat
The interactions of Escherichia coli trp repressor with tryptophan and with an operator oligonucleotide. NMR studies using selectively 15N-labelled protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles The interactions of Escherichia coli trp repressor with tryptophan and with an operator oligonucleotide. NMR studies using selectively 15N-labelled protein.
Eur J Biochem. 1994 Oct 15;225(2):601-8
Authors: Ramesh V, Frederick RO, Syed SE,...
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[NMR paper] NMR studies of the activation of the Escherichia coli trp repressor.
NMR studies of the activation of the Escherichia coli trp repressor.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR studies of the activation of the Escherichia coli trp repressor.
Eur J Biochem. 1991 Nov 1;201(3):569-79
Authors: Hyde EI, Ramesh V, Frederick R, Roberts GC
The Escherichia coli trp repressor binds to the trp operator in the presence of tryptophan, thereby inhibiting tryptophan biosynthesis. Tryptophan analogues...
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[NMR paper] NMR studies of the activation of the Escherichia coli trp repressor.
NMR studies of the activation of the Escherichia coli trp repressor.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR studies of the activation of the Escherichia coli trp repressor.
Eur J Biochem. 1991 Nov 1;201(3):569-79
Authors: Hyde EI, Ramesh V, Frederick R, Roberts GC
The Escherichia coli trp repressor binds to the trp operator in the presence of tryptophan, thereby inhibiting tryptophan biosynthesis. Tryptophan analogues...
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08-21-2010 11:12 PM
[NMR paper] Assignment of the 1H-NMR spectrum of a lac repressor headpiece-operator complex in H2
Assignment of the 1H-NMR spectrum of a lac repressor headpiece-operator complex in H2O and identification of NOEs. Consequences for protein-DNA interaction.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Assignment of the 1H-NMR spectrum of a lac repressor headpiece-operator complex in H2O and identification of NOEs. Consequences for protein-DNA interaction.
Eur J Biochem. 1990 Dec 12;194(2):629-37
Authors: Lamerichs RM, Boelens R, Van der...
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[NMR paper] Two-dimensional NMR study of a protein-DNA complex. lac repressor headpiece-operator
Two-dimensional NMR study of a protein-DNA complex. lac repressor headpiece-operator interaction.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Two-dimensional NMR study of a protein-DNA complex. lac repressor headpiece-operator interaction.
Biochem Pharmacol. 1990 Jul 1;40(1):89-96
Authors: Kaptein R, Lamerichs RM, Boelens R, Rullmann JA
The interaction of the N-terminal DNA-binding domain (56 amino acid residues) of the lac repressor with lac operator DNA was...