Two-Component Signaling Systems, Part C

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.

• Includes time-tested core methods and new innovations applicable to any researcher studing two-component signaling systems or histidine kinases
• Methods included are useful to both established researchers and newcomers to the field
• Relevant background and reference information given for procedures can be used as a guide to developing protocols in a number of disciplines

Contenu

1. Characterizing cross-talk in vivo: avoiding pitfalls and over-interpretation Albert Siryaporn and Mark Goulian
2. Inference of Direct Residue Contacts in Two-Component Signaling Bryan Lunt, Hendrik Szurmant, Andrea Procaccini, James A. Hoch, Terence Hwa and Martin Weigt
3. Computational Modeling of Phosphotransfer Complexes in Two-Component Signaling Alexander Schug, Martin Weigt, James A. Hoch, Jose N. Onuchic, Terence Hwa, Hendrik Szurmant
4. Kinetic studies of the yeast His-Asp phosphorelay signaling pathway Alla O. Kaserer, Babak Andi, Paul F. Cook and Ann H. West
5. Purification of MBP-EnvZ fusion proteins using an automated system Ricardo Oropeza and Edmundo Calva
6. 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
7. Transmembrane receptors chimeras to probe Hamp domain function Jürgen U. Linder and Joachim E. Schultz
8. Light-Activated Bacterial LOV-domain Histidine Kinases Tong-Seung Tseng, Marcus A. Frederickson, Winslow R. Briggs and Roberto A. Bogomolni
9. Characterization of Bacteriophytochromes from Photosynthetic Bacteria: Histidine Kinase Signaling Triggered by light and redox sensing Eric Giraud, Jérôme Lavergne and André Verméglio
10. 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
11. High throughput screening of bacterial protein localization John N. Werner and Zemer Gitai
12. In vitro and in vivo analysis of the ArcB/A redox signaling pathway Adrián F. Alvarez and Dimitris Georgellis
13. Potassium sensing histidine kinase in Bacillus subtilis Daniel López, Erin Gontang and Roberto Kolter
14. Two Component Systems and Regulation of Developmental Progression in Myxococcus Xanthus Bongsoo Lee, Andreas Schramm, and Penelope I. Higgs
15. Two-component signaling to the stress MAP kinase cascade in fission yeast Susumu Morigasaki and Kazuhiro Shiozaki
16. Genetic and Biochemical Analysis of the SLN1 Pathway in Saccharomyces cerevisiae Jan S. Fassler
17. 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
18. Biochemical Characterization of Plant Hormone Cytokinin Receptor Histidine Kinases Using Microorganisms Takeshi Mizuno and Takafumi Yamashino
19. Characterization of Pseudo-Response Regulators In Plants Woe-Yeon Kim, Patrice A. Salomé, Sumire Fujiwara, David E. Somers and C. Robertson McClung
20. 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
21. Histidine phosphorylation in histones and in other mammalian proteins Paul G. Besant and P.V. Attwood