Probing conservation of HAMP linker structure and signal transduction mechanism through analysis of hybrid sensor kinases

被引:58
作者
Appleman, JA [1 ]
Chen, LL [1 ]
Stewart, V [1 ]
机构
[1] Univ Calif Davis, Microbiol Sect, Davis, CA 95616 USA
关键词
D O I
10.1128/JB.185.16.4872-4882.2003
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The RAMP linker, a predicted structural element observed in many sensor kinases and methyl-accepting chemotaxis proteins, transmits signals between sensory input modules and output modules. HAMP linkers are located immediately inside the cytoplasmic membrane and are predicted to form two short amphipathic alpha-helices (AS-1 and AS-2) joined by an unstructured connector. RAMP linkers are found in the Escherichia coli nitrate- and nitrite-responsive sensor kinases NarX and NarQ (which respond to ligand by increasing kinase activity) and the sensor kinase CpxA (which responds to ligand by decreasing kinase activity). We constructed a series of hybrids with fusion points throughout the HAMP linker, in which the sensory modules of NarX or NarQ are fused to the transmitter modules of NarX, NarQ, or CpxA. A hybrid of the NarX sensor module and the CpxA RAMP linker and transmitter module (NarX-CpxA-1) responded to nitrate by decreasing kinase activity, whereas a hybrid in which the HAMP linker of NarX was replaced by that of CpxA (NarX-CpxA-NarX-1) responded to nitrate by increasing kinase activity. However, sequence variations between HAMP linkers do not allow free exchange of HAMP linkers or their components. Certain deletions in the NarX RAMP linker resulted in characteristic abnormal responses to ligand; similar deletions in the NarQ and NarX-CpxA-1 HAMP linkers resulted in responses to ligand generally similar to those seen in NarX. We conclude that the structure and action of the HAMP linker are conserved and that the HAMP linker transmits a signal to the output domain that ligand is bound.
引用
收藏
页码:4872 / 4882
页数:11
相关论文
共 54 条
[1]   TRANSMEMBRANE SIGNALING BY BACTERIAL CHEMORECEPTORS - ESCHERICHIA-COLI TRANSDUCERS WITH LOCKED SIGNAL OUTPUT [J].
AMES, P ;
PARKINSON, JS .
CELL, 1988, 55 (05) :817-826
[2]  
[Anonymous], 2 COMPONENT SIGNAL T
[3]   Rapid dephosphorylation of the TorR response regulator by the TorS unorthodox sensor in Escherichia coli [J].
Ansaldi, M ;
Jourlin-Castelli, C ;
Lepelletier, M ;
Théraulaz, L ;
Méjean, V .
JOURNAL OF BACTERIOLOGY, 2001, 183 (08) :2691-2695
[4]   Mutational analysis of a conserved signal-transducing element:: the HAMP linker of the Escherichia coli nitrate sensor NarX [J].
Appleman, JA ;
Stewart, V .
JOURNAL OF BACTERIOLOGY, 2003, 185 (01) :89-97
[5]  
Aravind L, 1999, FEMS MICROBIOL LETT, V176, P111, DOI 10.1111/j.1574-6968.1999.tb13650.x
[6]   TRANSMEMBRANE SIGNALING BY A HYBRID PROTEIN - COMMUNICATION FROM THE DOMAIN OF CHEMORECEPTOR TRG THAT RECOGNIZES SUGAR-BINDING PROTEINS TO THE KINASE/PHOSPHATASE DOMAIN OF OSMOSENSOR ENVZ [J].
BAUMGARTNER, JW ;
KIM, C ;
BRISSETTE, RE ;
INOUYE, M ;
PARK, C ;
HAZELBAUER, GL .
JOURNAL OF BACTERIOLOGY, 1994, 176 (04) :1157-1163
[7]   Domain organization and flavin adenine dinucleotide-binding determinants in the aerotaxis signal transducer Aer of Escherichia coli [J].
Bibikov, SI ;
Barnes, LA ;
Gitin, Y ;
Parkinson, JS .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (11) :5830-5835
[8]   SUPERPOLYLINKERS IN CLONING AND EXPRESSION VECTORS [J].
BROSIUS, J .
DNA-A JOURNAL OF MOLECULAR & CELLULAR BIOLOGY, 1989, 8 (10) :759-777
[9]   Cysteine and disulfide scanning reveals two amphiphilic helices in the linker region of the aspartate chemoreceptor [J].
Butler, SL ;
Falke, JJ .
BIOCHEMISTRY, 1998, 37 (30) :10746-10756
[10]   TRANSPOSITION AND FUSION OF LAC GENES TO SELECTED PROMOTERS IN ESCHERICHIA-COLI USING BACTERIOPHAGE-LAMBDA AND BACTERIOPHAGE-MU [J].
CASADABAN, MJ .
JOURNAL OF MOLECULAR BIOLOGY, 1976, 104 (03) :541-555