Evidence from Analysis of Synechocystis 6803 that the Chlorophyll A-Binding Protein CP43 Contains a DFP-Binding Domain Involved in D1 Protein Degradation

1995 ◽  
pp. 3433-3436
Author(s):  
A. Hugh Salter ◽  
Åsa Hagman ◽  
Wim F. J. Vermaas ◽  
Bertil Andersson
Keyword(s):  
Protein Degradation ◽  
Chlorophyll A ◽  
Binding Protein ◽  
D1 Protein ◽  
Binding Domain ◽  
Synechocystis 6803

scholarly journals Proteome Analysis for Understanding Abiotic Stress (Salinity and Drought) Tolerance in Date Palm (Phoenix dactyliferaL.)

2015 ◽  
Vol 2015 ◽  
pp. 1-11 ◽  
Author(s):  
Haddad A. El Rabey ◽  
Abdulrahman L. Al-Malki ◽  
Khalid O. Abulnaja ◽  
Wolfgang Rohde
Keyword(s):  
Drought Stress ◽  
Chlorophyll A ◽  
Date Palm ◽  
Light Harvesting ◽  
Binding Protein ◽  
Proteome Analysis ◽  
Rubisco Activase ◽  
Stress Conditions ◽  
Spectrometric Analysis ◽  
Salt And Drought Stress

This study was carried out to study the proteome of date palm under salinity and drought stress conditions to possibly identify proteins involved in stress tolerance. For this purpose, three-month-old seedlings of date palm cultivar “Sagie” were subjected to drought (27.5 g/L polyethylene glycol 6000) and salinity stress conditions (16 g/L NaCl) for one month. DIGE analysis of protein extracts identified 47 differentially expressed proteins in leaves of salt- and drought-treated palm seedlings. Mass spectrometric analysis identified 12 proteins; three out of them were significantly changed under both salt and drought stress, while the other nine were significantly changed only in salt-stressed plants. The levels of ATP synthase alpha and beta subunits, an unknown protein and some of RubisCO fragments were significantly changed under both salt and drought stress conditions. Changes in abundance of superoxide dismutase, chlorophyll A-B binding protein, light-harvesting complex1 protein Lhca1, RubisCO activase, phosphoglycerate kinase, chloroplast light-harvesting chlorophyll a/b-binding protein, phosphoribulokinase, transketolase, RubisCO, and some of RubisCO fragments were significant only for salt stress.

Detailed analysis of the atrial natriuretic factor receptor hormone-binding domain crystal structure

2001 ◽  
Vol 79 (8) ◽  
pp. 692-704 ◽  
Author(s):  
Focco van den Akker
Keyword(s):  
Crystal Structure ◽  
Atrial Natriuretic Factor ◽  
Binding Protein ◽  
Chloride Ion ◽  
Binding Domain ◽  
Protein Fold ◽  
Hormone Binding ◽  
Periplasmic Binding Protein ◽  
Natriuretic Factor ◽  
Hormone Binding Domain

The X-ray crystal structure of the dimerized atrial natriuretic factor (ANF) receptor hormone-binding domain has provided a first structural view of this anti-hypertensive receptor. The structure reveals a surprising evolutionary link to the periplasmic-binding protein fold family. Furthermore, the presence of a chloride ion in the membrane distal domain and the presence of a second putative effector pocket suggests that the extracellular domain of this receptor is allosterically regulated. The scope of this article is to extensively review the data published on this receptor and to correlate it with the hormone-binding domain structure. In addition, a more detailed description is provided of the important features of this structure including the different binding sites for the ANF hormone, chloride ion, putative effector pocket, glycosylation sites, and dimer interface.Key words: crystal structure, periplasmic-binding protein fold, guanylyl cyclase, hormone receptor.

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