A bifunctional kinase-phosphatase in bacterial chemotaxis.
Phosphorylation-based signaling pathways employ dephosphorylation mechanisms for signal termination. Histidine to aspartate phosphosignaling in the two-component system that controls bacterial chemotaxis has been studied extensively. Rhodobacter sphaeroides has a complex chemosensory pathway with mu...
Hlavní autoři: | Porter, S, Roberts, M, Manning, C, Armitage, J |
---|---|
Médium: | Journal article |
Jazyk: | English |
Vydáno: |
2008
|
Podobné jednotky
-
Modeling chemotaxis reveals the role of reversed phosphotransfer and a bi-functional kinase-phosphatase
Autor: Tindall, M, a další
Vydáno: (2010) -
Modeling chemotaxis reveals the role of reversed phosphotransfer and a Bi-functional kinase-phosphatase
Autor: Tindall, M, a další
Vydáno: (2010) -
Modeling chemotaxis reveals the role of reversed phosphotransfer & a bi-functional kinase-phosphatase
Autor: Tindall, M, a další
Vydáno: (2010) -
Modeling chemotaxis reveals the role of reversed phosphotransfer and a bi-functional kinase-phosphatase.
Autor: Marcus J Tindall, a další
Vydáno: (2010-08-01) -
Chemotaxis in Rhodobacter sphaeroides requires an atypical histidine protein kinase.
Autor: Porter, S, a další
Vydáno: (2004)