Probing Conservation of HAMP Linker Structure and Signal Transduction Mechanism through Analysis of Hybrid Sensor Kinases
نویسندگان
چکیده
منابع مشابه
Signaling mechanisms of HAMP domains in chemoreceptors and sensor kinases.
HAMP domains mediate input-output signaling in histidine kinases, adenylyl cyclases, methyl-accepting chemotaxis proteins, and some phosphatases. HAMP subunits have two 16-residue amphiphilic helices (AS1, AS2) joined by a 14- to 15-residue connector segment. Two alternative HAMP structures in these homodimeric signaling proteins have been described: HAMP(A), a tightly packed, parallel, four-he...
متن کاملMutational analysis of a conserved signal-transducing element: the HAMP linker of the Escherichia coli nitrate sensor NarX.
The HAMP linker, a predicted structural element observed in sensor proteins from all domains of life, is proposed to transmit signals between extracellular sensory input domains and cytoplasmic output domains. HAMP (histidine kinase, adenylyl cyclase, methyl-accepting chemotaxis protein, and phosphatase) linkers are located just inside the cytoplasmic membrane and are projected to form two shor...
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UNLABELLED HAMP domains are α-helical coiled coils that often transduce signals from extracytoplasmic sensing domains to cytoplasmic domains. Limited structural information has resulted in hypotheses that specific HAMP helix movement changes downstream enzymatic activity. These hypotheses were tested by mutagenesis and cysteine cross-linking analysis of the PhoQ histidine kinase, essential for ...
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Recently determined structures have linked histidine kinases with class II topoisomerases, the DNA repair enzyme MutL and the molecular chaperone Hsp90. This surprising finding may foreshadow a shift in our understanding of energy coupling mechanisms in signal transduction networks.
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 2003
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.185.16.4872-4882.2003