Two-Component Signaling Systems, Part C

Volume 471
Herausgegeben:Simon, Melvin I.; Crane, Brian; Crane, Alexandrine

• Gebundenes Buch

Produktbeschreibung

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.

Produktdetails

• Methods in Enzymology Volume 471
• Verlag: Academic Press / Elsevier Science & Technology
• Artikelnr. des Verlages: C2009-0-01922-9
• Seitenzahl: 496
• Erscheinungstermin: 16. März 2010
• Englisch
• Abmessung: 238mm x 162mm x 34mm
• Gewicht: 950g
• ISBN-13: 9780123813473
• ISBN-10: 0123813476
• Artikelnr.: 28437938

Inhaltsangabe

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