Two-Component Signaling Systems, Part C

Erscheinungsjahr 2010
ISBN: 978-0-12-381347-3
Verlag: William Andrew Publishing

Buch, Englisch, 496 Seiten, Format (B × H): 152 mm x 229 mm, Gewicht: 950 g

Multicellular organisms must be able to adapt to cellular events to accommodate prevailing conditions. Sensory-response circuits operate by making use of a phosphorylation control mechanism known as the "two-component system." This volume, the third in a three-volume treatment edited by the same group of editors, includes a wide range of methods, including those dealing with the Sln-1 kinase pathway, triazole sensitivity in C. albicans, and histidine kinases in cyanobacteria circadian clock.

Zielgruppe

<p>Researchers and students in biochemistry, genetics, and molecular biology</p>

Autoren/Hrsg.

Weitere Mitwirkende

Simon, Melvin I.

Crane, Brian

Crane, Alexandrine

Fachgebiete

• Naturwissenschaften Biowissenschaften Enzymologie

Inhaltsverzeichnis

- Characterizing cross-talk in vivo: avoiding pitfalls and over-interpretation Albert Siryaporn and Mark Goulian

- Inference of Direct Residue Contacts in Two-Component Signaling Bryan Lunt, Hendrik Szurmant, Andrea Procaccini, James A. Hoch, Terence Hwa and Martin Weigt

- Computational Modeling of Phosphotransfer Complexes in Two-Component Signaling Alexander Schug, Martin Weigt, James A. Hoch, Jose N. Onuchic, Terence Hwa, Hendrik Szurmant

- Kinetic studies of the yeast His-Asp phosphorelay signaling pathway Alla O. Kaserer, Babak Andi, Paul F. Cook and Ann H. West

- Purification of MBP-EnvZ fusion proteins using an automated system Ricardo Oropeza and Edmundo Calva

- Measurement of Response Regulator Autodephosphorylation Rates Spanning Six Orders of Magnitude Robert B. Bourret, Stephanie A. Thomas, Stephani C. Page, Rachel L. Creager-Allen, Aaron M. Moore, and Ruth E. Silversmith

- Transmembrane receptors chimeras to probe Hamp domain function Jürgen U. Linder and Joachim E. Schultz

- Light-Activated Bacterial LOV-domain Histidine Kinases Tong-Seung Tseng, Marcus A. Frederickson, Winslow R. Briggs and Roberto A. Bogomolni

- Characterization of Bacteriophytochromes from Photosynthetic Bacteria: Histidine Kinase Signaling Triggered by light and redox sensing Eric Giraud, Jérôme Lavergne and André Verméglio

- Biophysical assays for protein interactions in the Wsp sensory system and biofilm formation Nabanita De, Marcos V.A.S. Navarro, Qi Wang, Petya V. Krasteva and Holger Sondermann

- High throughput screening of bacterial protein localization John N. Werner and Zemer Gitai

- In vitro and in vivo analysis of the ArcB/A redox signaling pathway Adrián F. Alvarez and Dimitris Georgellis

- Potassium sensing histidine kinase in Bacillus subtilis Daniel López, Erin Gontang and Roberto Kolter

- Two Component Systems and Regulation of Developmental Progression in Myxococcus Xanthus Bongsoo Lee, Andreas Schramm, and Penelope I. Higgs

- Two-component signaling to the stress MAP kinase cascade in fission yeast Susumu Morigasaki and Kazuhiro Shiozaki

- Genetic and Biochemical Analysis of the SLN1 Pathway in Saccharomyces cerevisiae Jan S. Fassler

- Analysis of mitogen-activated protein kinase phosphorylation in response to stimulation of histidine kinase signaling pathways in Neurospora Carol A. Jones and Katherine A. Borkovich

- Biochemical Characterization of Plant Hormone Cytokinin Receptor Histidine Kinases Using Microorganisms Takeshi Mizuno and Takafumi Yamashino

- Characterization of Pseudo-Response Regulators In Plants Woe-Yeon Kim, Patrice A. Salomé, Sumire Fujiwara, David E. Somers and C. Robertson McClung

- Reversible Histidine Phosphorylation in Mammalian Cells: A Teeter-Totter Formed by Nucleoside Diphosphate Kinase and Protein Histidine Phosphatase Thomas Wieland, Hans-Jörg Hippe, Katrin Ludwig, Xiao-Bo Zhou, Michael Korth and Susanne Klumpp

- Histidine phosphorylation in histones and in other mammalian proteins Paul G. Besant and P.V. Attwood