scholarly journals Ethylene Controls Autophosphorylation of the Histidine Kinase Domain in Ethylene Receptor ETR1

2008 ◽  
Vol 1 (2) ◽  
pp. 380-387 ◽  
Author(s):  
Jan Voet-van-Vormizeele ◽  
Georg Groth
2003 ◽  
Vol 1646 (1-2) ◽  
pp. 136-144 ◽  
Author(s):  
Hideyuki Kumita ◽  
Seiji Yamada ◽  
Hiro Nakamura ◽  
Yoshitsugu Shiro

2007 ◽  
Vol 283 (2) ◽  
pp. 1167-1178 ◽  
Author(s):  
Xiaolei Ma ◽  
Nazish Sayed ◽  
Padmamalini Baskaran ◽  
Annie Beuve ◽  
Focco van den Akker

2004 ◽  
Vol 136 (2) ◽  
pp. 2971-2981 ◽  
Author(s):  
Zhi-Gang Zhang ◽  
Hua-Lin Zhou ◽  
Tao Chen ◽  
Yan Gong ◽  
Wan-Hong Cao ◽  
...  

2005 ◽  
Vol 83 (6) ◽  
pp. 563-570 ◽  
Author(s):  
Michael G Mason ◽  
G Eric Schaller

Ethylene is a gaseous hormone that regulates many aspects of plant growth and development. Although the effect of ethylene on plant growth was discovered a century ago, the key players in the ethylene response pathway were only identified over the last 15 years. In Arabidopsis, ethylene is perceived by a family of five receptors (ETR1, ETR2, ERS1, ERS2, and EIN4) that resemble two-component histidine kinases. Of these, only ETR1 and ERS1 contain all the conserved residues required for histidine kinase activity. The ethylene receptors appear to function primarily through CTR1, a serine/threonine kinase that actively suppresses ethylene responses in air (absence of ethylene). Despite recent progress toward understanding ethylene signal transduction, the role of the ethylene-receptor histidine-kinase activity remains unclear. This review considers the significance of histidine kinase activity in ethylene signaling and possible mechanisms by which it may modulate ethylene responses.Key words: ethylene receptor, ETR1, histidine kinase, two-component, phosphorylation, Arabidopsis.


Nature ◽  
10.1038/23968 ◽  
1998 ◽  
Vol 396 (6706) ◽  
pp. 88-92 ◽  
Author(s):  
Toshiyuki Tanaka ◽  
Soumitra K. Saha ◽  
Chieri Tomomori ◽  
Rieko Ishima ◽  
Dingjiang Liu ◽  
...  

2012 ◽  
Vol 415 (4) ◽  
pp. 768-779 ◽  
Author(s):  
Hubert Mayerhofer ◽  
Saravanan Panneerselvam ◽  
Jochen Mueller-Dieckmann

1998 ◽  
Vol 180 (1) ◽  
pp. 20-26 ◽  
Author(s):  
Hai-Ping Cheng ◽  
Graham C. Walker

ABSTRACT The Rhizobium meliloti exoS gene is involved in regulating the production of succinoglycan, which plays a crucial role in the establishment of the symbiosis between R. melilotiRm1021 and its host plant, alfalfa. TheexoS96::Tn5 mutation causes the upregulation of the succinoglycan biosynthetic genes, thereby resulting in the overproduction of succinoglycan. Through cloning and sequencing, we found that the exoS gene is a close homolog of theAgrobacterium tumefaciens chvG gene, which has been proposed to encode the sensor protein of the ChvG-ChvI two-component regulatory system, a member of the EnvZ-OmpR family. Further analyses revealed the existence of a newly discovered A. tumefaciens chvI homolog located just upstream of the R. meliloti exoS gene. R. meliloti ChvI may serve as the response regulator of ExoS in a two-component regulatory system. By using ExoS-specific antibodies, it was found that the ExoS protein cofractionated with membrane proteins, suggesting that it is located in the cytoplasmic membrane. By using the same antibodies, it was shown that the exoS96::Tn5 allele encodes an N-terminal truncated derivative of ExoS. The cytoplasmic histidine kinase domain of ExoS was expressed in Escherichia coli and purified, as was the R. meliloti ChvI protein. The ChvI protein autophosphorylated in the presence of acetylphosphate, and the ExoS cytoplasmic domain fragment autophosphorylated at a histidine residue in the presence of ATP. The ChvI protein was phosphorylated in the presence of ATP only when the histidine kinase domain of ExoS was also present. We propose a model for regulation of succinoglycan production by R. meliloti through the ExoS-ChvI two-component regulatory system.


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