scholarly journals ETHYLENE RESPONSE 1 Histidine Kinase Activity of Arabidopsis Promotes Plant Growth

2007 ◽  
Vol 143 (2) ◽  
pp. 612-616 ◽  
Author(s):  
Young-Hee Cho ◽  
Sang-Dong Yoo
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.


2012 ◽  
Vol 159 (2) ◽  
pp. 682-695 ◽  
Author(s):  
Brenda P. Hall ◽  
Samina N. Shakeel ◽  
Madiha Amir ◽  
Noor Ul Haq ◽  
Xiang Qu ◽  
...  

2015 ◽  
Vol 58 ◽  
pp. 61-70 ◽  
Author(s):  
Paul B. Larsen

Ethylene is the simplest unsaturated hydrocarbon, yet it has profound effects on plant growth and development, including many agriculturally important phenomena. Analysis of the mechanisms underlying ethylene biosynthesis and signalling have resulted in the elucidation of multistep mechanisms which at first glance appear simple, but in fact represent several levels of control to tightly regulate the level of production and response. Ethylene biosynthesis represents a two-step process that is regulated at both the transcriptional and post-translational levels, thus enabling plants to control the amount of ethylene produced with regard to promotion of responses such as climacteric flower senescence and fruit ripening. Ethylene production subsequently results in activation of the ethylene response, as ethylene accumulation will trigger the ethylene signalling pathway to activate ethylene-dependent transcription for promotion of the response and for resetting the pathway. A more detailed knowledge of the mechanisms underlying biosynthesis and the ethylene response will ultimately enable new approaches to be developed for control of the initiation and progression of ethylene-dependent developmental processes, many of which are of horticultural significance.


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

2010 ◽  
Vol 397 (2) ◽  
pp. 139-143 ◽  
Author(s):  
Hans K. Carlson ◽  
Lars Plate ◽  
Mark S. Price ◽  
Jasmina J. Allen ◽  
Kevan M. Shokat ◽  
...  

2009 ◽  
Vol 50 (9) ◽  
pp. 1636-1650 ◽  
Author(s):  
Tao Chen ◽  
Jun Liu ◽  
Gang Lei ◽  
Yun-Feng Liu ◽  
Zhi-Gang Li ◽  
...  

mBio ◽  
2015 ◽  
Vol 6 (3) ◽  
Author(s):  
Susana Matamouros ◽  
Kyle R. Hager ◽  
Samuel I. Miller

ABSTRACTHAMP 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 resistance to antimicrobial peptides in a variety of enteric pathogens. These results support a mechanistic model in which periplasmic signals which induce an activation state generate a rotational movement accompanied by a tilt in α-helix 1 which activates kinase activity. Biochemical data and a high-confidence model of the PhoQ cytoplasmic domain indicate a possible physical interaction of the HAMP domain with the catalytic domain as necessary for kinase repression. These results support a model of PhoQ activation in which changes in the periplasmic domain lead to conformational movements in the HAMP domain helices which disrupt interaction between the HAMP and the catalytic domains, thus promoting increased kinase activity.IMPORTANCEMost studies on the HAMP domain signaling states have been performed with chemoreceptors or the HAMP domain of Af1503. Full-length structures of the HAMP-containing histidine kinases VicK and CpxA or a hybrid between the HAMP domain of Af1503 and the EnvZ histidine kinase agree with the parallel four-helix bundle structure identified in Af1503 and provide snapshots of structural conformations experienced by HAMP domains. We took advantage of the fact that we can easily regulate the activation state of PhoQ histidine kinase to study its HAMP domain in the context of the full-length protein in living cells and provide biochemical evidence for different conformational states experienced bySalmonella entericaserovar Typhimurium PhoQ HAMP domain upon signaling.


1998 ◽  
Vol 95 (13) ◽  
pp. 7825-7829 ◽  
Author(s):  
R. L. Gamble ◽  
M. L. Coonfield ◽  
G. E. Schaller

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