Two-Component Signaling Systems, Part C

Edited by

  • Melvin Simon, The Salk Institute, La Jolla, CA, USA
  • Brian Crane, Cornell University, Ithaca, NY, USA
  • Alexandrine Crane, Cornell University, Ithaca, NY, USA

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.
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Audience

Researchers and students in biochemistry, genetics, and molecular biology

 

Book information

  • Published: March 2010
  • Imprint: ACADEMIC PRESS
  • ISBN: 978-0-12-381347-3


Table of Contents

  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