Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Brigitte Kisters–Woike"'
Publikováno v:
J Biol Chem
The integrity of the inner membrane of mitochondria is maintained by a membrane-embedded quality control system that ensures the removal of misfolded membrane proteins. Two ATP-dependent AAA proteases with catalytic sites at opposite membrane surface
Publikováno v:
Journal of Molecular Biology. 296:673-684
Assembly of the lactose repressor tetramer involves two subunit interfaces, the C-terminal heptad repeats, and the monomer-monomer interface. Dimerisation between two monomers of Lac repressor of Escherichia coli lacking the two C-terminal heptad rep
Publikováno v:
Journal of Molecular Biology. 286:983-987
Homodimeric DNA-binding proteins with relaxed half-site spacing requirements for their DNA targets have been described. As an example, the yeast transcriptional activator Gcn4p binds in vitro equally well to the AP1 site (5′A 4 T 3 G 2 A 1 C 0 T 1
Autor:
Fumin Dong, Benno Müller-Hill, Brigitte Kisters-Woike, Andrew Barker, Olav Zimmermann, Stefanie Spott
Publikováno v:
Journal of Molecular Biology. 290:653-666
Dimer formation between monomers of the Escherichia coli Lac repressor is substantially specificed by the interactions between three α-helices in each monomer which form a hydrophobic interface. As a first step in analysing the specificity of this i
Autor:
Brigitte Kisters-Woike, Markus Hartung
Publikováno v:
Journal of Biological Chemistry. 273:22884-22891
The recombinase Cre of bacteriophage P1 is a member of the family of site-specific recombinases and integrases that catalyze inter- and intramolecular DNA rearrangements. To understand how this protein specifically recognizes its target sequence, we
Autor:
Brigitte Kisters-Woike, Jeffrey H Miller, Peter Markiewicz, Lynn G. Kleina, Benno Müller-Hill, Jörg Suckow
Publikováno v:
Journal of Molecular Biology. 261:509-523
Each amino acid from position 2 to 329 of Lac repressor was replaced by 12 or 13 of the 20 natural occurring amino acids. The resulting phenotypes are discussed on the basis of (1) the recently published structure of the Lac repressor core complexed
Autor:
B von Wilcken-Bergmann, Manfred Suckow, A. Seydel, Benno Müller-Hill, M. Lopata, Brigitte Kisters-Woike
Publikováno v:
The EMBO Journal. 15:598-606
The complex between the yeast transcriptional activator GCN4 and the palindromic ATF/CREB site 5'- A4T3G2A1C0*G0'T1'C2'A3'T4'-3' shows dyad symmetry. The basic region of GCN4 contains a segment of 18 amino acids with a partially palindromic sequence:
Autor:
Manfred Suckow, Brigitte von Wilcken-Bergmann, Benno Müller-Hill, Brigitte Kisters-Woike, Klaus Schwamborn
Publikováno v:
Nucleic Acids Research. 22:4395-4404
Two residues are invariant in all bZip basic regions: asparagine -18 and arginine -10 (we define the first leucine of the leucine zipper of GCN4 as +1). X-ray structures of two specific GCN4-DNA complexes (Ellenberger et al., Cell, 71, 1223-1237, 199
Publikováno v:
Journal of Molecular Biology. 228:460-473
The deposition of amyloid protein aggregates in brain is the main pathological feature of Alzheimer's disease. Their principal constituent is a peptide termed beta A4, which comprises up to 43 amino acid residues. It is highly insoluble under physiol
Autor:
Norbert Lehming, Brigitte von Wilcken-Bergmann, Benno Müller-Hill, Brigitte Kisters-Woike, J. Sartorius
Publikováno v:
Journal of Molecular Biology. 218:313-321
We constructed expression libraries for Lac repressor mutants with amino acid exchanges in positions 1, 2, 5 and 9 of the recognition helix. We then analysed the interactions of residues 5 and 9 with operator variants bearing single or multiple symme