Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Noreen R. Francis"'
Autor:
Noreen R. Francis, Eyal Shimoni, Michael Eisenbach, Yael Sagi, Dror Noy, Gary Cecchini, Rose M. Johnstone, Yaacov Davidov, Galit N Cohen-Ben-Lulu, Krishna Prasad
Publikováno v:
The EMBO Journal. 27:1134-1144
The mechanism of function of the bacterial flagellar switch, which determines the direction of flagellar rotation and is essential for chemotaxis, has remained an enigma for many years. Here we show that the switch complex associates with the membran
Publikováno v:
Journal of Bacteriology. 188:7039-7048
Three-dimensional reconstructions from electron cryomicrographs of the rotor of the flagellar motor reveal that the symmetry of individual M rings varies from 24-fold to 26-fold while that of the C rings, containing the two motor/switch proteins FliM
Publikováno v:
Proceedings of the National Academy of Sciences. 101:17480-17485
Transmembrane signaling in bacterial chemotaxis has become an important model system for experimental and theoretical studies. These studies have provided a wealth of detailed molecular structures, including the structures of CheA, CheW, and the cyto
Publikováno v:
Journal of Molecular Biology. 235:1261-1270
A putative complex of the three switch proteins, FliG, FliM and FliN appears to be directly involved in torque generation and control of direction of rotation. We have developed a preparative procedure for flagellar motors that retains these proteins
Publikováno v:
Ultramicroscopy. 49:417-425
The size of the putative export channel in the bacterial flagellar filament appears small (25 A) in studies done by electron microscopy but large (60 A) in studies done by X-ray diffraction. We have undertaken additional studies by electron microscop
Publikováno v:
Journal of Molecular Biology. 229:79-84
The deduced amino acid sequences of the family of axial proteins of the bacterial flagellum possess N and C-terminal heptad repeats of hydrophobic amino acid residues, which suggests that these proteins all fold to form bundles of α-helices (e.g. co
Publikováno v:
Journal of Molecular Biology. 223:171-184
The Salmonella typhimurium basal body, a part of the flagellar rotary motor, consists of four rings (denoted M, S, P and L) and a coaxial rod. Using low-dose electron microscopy and image averaging methods on negatively stained and frozen-hydrated pr
Publikováno v:
Microscopy and Microanalysis. 13
Autor:
Noreen R. Francis, Peter M. Wolanin, Dennis R. Thomas, Jeffry B. Stock, Melinda D. Baker, David J. DeRosier
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 103(39)
Escherichia coli chemotaxis is mediated by membrane receptor/histidine kinase signaling complexes. Fusing the cytoplasmic domain of the aspartate receptor, Tar, to a leucine zipper dimerization domain produces a hybrid, lzTar C , that forms soluble c
Autor:
Mikhail N. Levit, Jeffry B. Stock, Tanvir R. Shaikh, Noreen R. Francis, David J. DeRosier, Linda A. Melanson
Publikováno v:
The Journal of biological chemistry. 277(39)
The Salmonella and Escherichia coli aspartate receptor, Tar, is representative of a large class of membrane receptors that generate chemotaxis responses by regulating the activity of an associated histidine protein kinase, CheA. Tar is composed of an