Insertion of a “chloroplast-like” regulatory segment responsible for thiol modulation into γ-subunit of F0F1-ATPase of the cyanobacterium Synechocystis 6803 by mutagenesis of atpC

1994 ◽  
Vol 244 (2) ◽  
pp. 144-150 ◽  
Author(s):  
Sabine Werner-Grüne ◽  
Dorothea Gunkel ◽  
Jürgen Schumann ◽  
Heinrich Strotmann
Keyword(s):  
Synechocystis 6803 ◽  
Γ Subunit

scholarly journals The primary structure of the γ-subunit of the ATPase from Synechocystis 6803

FEBS Letters ◽  
1990 ◽  
Vol 261 (1) ◽  
pp. 204-208 ◽  
Author(s):  
Sabine Werner ◽  
Jürgen Schumann ◽  
Heinrich Strotmann
Keyword(s):  
Primary Structure ◽  
Synechocystis 6803 ◽  
Γ Subunit

ATP synthase from a cyanobacterial Synechocystis 6803 mutant containing the regulatory segment of the chloroplast γ subunit shows thiol modulation

1995 ◽  
Vol 23 (4) ◽  
pp. 757-760 ◽  
Author(s):  
B. E. Krenn ◽  
P. Aardewijn ◽  
H. S. Van Walraven ◽  
S. Werner-Grüne ◽  
H. Strotmann ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Synechocystis 6803 ◽  
Γ Subunit

scholarly journals The ATP synthase γ subunit provides the primary site of activation of the chloroplast enzyme: experiments with a chloroplast-like Synechocystis 6803 mutant

1997 ◽  
Vol 323 (3) ◽  
pp. 841-845 ◽  
Author(s):  
Bea E. KRENN ◽  
Heinrich STROTMANN ◽  
Hendrika S. VAN WALRAVEN ◽  
Marijke J. C. SCHOLTS ◽  
Ruud KRAAYENHOF
Keyword(s):  
Atp Synthase ◽  
Membrane Vesicles ◽  
Enzyme Activation ◽  
Reduced Form ◽  
Synechocystis 6803 ◽  
Wild Type ◽  
Acid Base ◽  
Γ Subunit ◽  
Base Transition ◽  
Membrane Bound

The activation characteristics of the F1Fo-ATP synthase (where F1 and Fo are the hydrophilic and membrane-bound parts respectively of the enzyme) from Synechocystis 6803 wild-type and a Synechocystis 6803 mutant with a chloroplast-like insertion in the γ subunit have been studied. Activation of the ATP synthase in wild-type and mutant membrane vesicles was performed by acid–base transition-induced generation of a proton motive force (ΔH+). Since the mutant containing the regulatory segment of the chloroplast γ subunit showed thiol-modulation (typical of the chloroplast enzyme), this segment is indeed involved in the regulation of enzyme activation. It is shown that the ATP synthase from Synechocystis 6803 wild type corresponds functionally to the reduced form of the chloroplast ATP synthase, in view of the low ΔH+ required for activation of the enzyme and the high stability of the active state. Both the cyanobacterial wild-type and mutant ATP synthases can be activated by methanol, which apparently does not require the presence of the γ subunit regulatory segment.

GABAA receptors: Various stoichiometrics of subunit arrangement in α1β3 and α1β3ε receptors

2018 ◽  
Vol 24 (17) ◽  
pp. 1839-1844 ◽  
Author(s):  
Ahmad Tarmizi Che Has ◽  
Mary Chebib
Keyword(s):  
Central Nervous System ◽  
Gabaa Receptors ◽  
Binding Sites ◽  
New Drugs ◽  
Pharmacological Properties ◽  
Receptor Complex ◽  
The Third ◽  
Γ Subunit ◽  
Subunit Stoichiometry ◽  
The Central Nervous System

GABAA receptors are members of the Cys-loop family of ligand-gated ion channels which mediate most inhibitory neurotransmission in the central nervous system. These receptors are pentameric assemblies of individual subunits, including α1-6, β1-3, γ1-3, δ, ε, π, θ and ρ1-3. The majority of receptors are comprised of α, β and γ or δ subunits. Depending on the subunit composition, the receptors are located in either the synapses or extrasynaptic regions. The most abundant receptors are α1βγ2 receptors, which are activated and modulated by a variety of pharmacologically and clinically unrelated agents such as benzodiazepines, barbiturates, anaesthetics and neurosteroids, all of which bind at distinct binding sites located within the receptor complex. However, compared to αβγ, the binary αβ receptors lack a benzodiazepine α-γ2 interface. In pentameric αβ receptors, the third subunit is replaced with either an α1 or a β3 subunit leading to two distinct receptors that differ in subunit stoichiometry, 2α:3β or 3α:2β. The consequence of this is that 3α:2β receptors contain an α-α interface whereas 2α:3β receptors contain a β-β interface. Apart from the replacement of γ by α1 or β3 in binary receptors, the incorporation of ε subunit into GABAA receptors might be more complicated. As the ε subunit is not only capable of substituting the γ subunit, but also replacing the α/β subunits, receptors with altered stoichiometry and different pharmacological properties are produced. The different subunit arrangement of the receptors potentially constructs novel binding sites which may become new targets of the current or new drugs.

V. The epithelial sodium channel and its implication in human diseases

1999 ◽  
Vol 276 (3) ◽  
pp. G567-G571 ◽  
Author(s):  
Edith Hummler ◽  
Jean-Daniel Horisberger
Keyword(s):  
Distal Colon ◽  
Loss Of Function ◽  
Newborn Mice ◽  
Α Subunit ◽  
Salt Wasting ◽  
Lung Fluid ◽  
Wasting Syndrome ◽  
Rate Limiting Step ◽  
Γ Subunit ◽  
Rate Limiting

The epithelial Na+ channel (ENaC) controls the rate-limiting step in the process of transepithelial Na+ reabsorption in the distal nephron, the distal colon, and the airways. Hereditary salt-losing syndromes have been ascribed to loss of function mutations in the α-, β-, or γ-ENaC subunit genes, whereas gain of function mutations (located in the COOH terminus of the β- or γ-subunit) result in hypertension due to Na+ retention (Liddle’s syndrome). In mice, gene-targeting experiments have shown that, in addition to the kidney salt-wasting phenotype, ENaC was essential for lung fluid clearance in newborn mice. Disruption of the α-subunit resulted in a complete abolition of ENaC-mediated Na+ transport, whereas knockout of the β- or γ-subunit had only minor effects on fluid clearance in lung. Disruption of each of the three subunits resulted in a salt-wasting syndrome similar to that observed in humans.

scholarly journals The Mitochondrial Genome Integrity Gene, MGI1, of Kluyveromyces lactis Encodes the β-Subunit of F1-ATPase

Genetics ◽  
1996 ◽  
Vol 144 (4) ◽  
pp. 1445-1454 ◽  
Author(s):  
Xin Jie Chen ◽  
G Desmond Clark-Walker
Keyword(s):  
Mitochondrial Genome ◽  
Kluyveromyces Lactis ◽  
Three Dimensional ◽  
Genome Integrity ◽  
Dimensional Structure ◽  
Deletion Mutants ◽  
Β Subunit ◽  
Gain Of Function ◽  
F1 Atpase ◽  
Γ Subunit

In a previous report, we found that mutations at the mitochondrial genome integrity locus, MGI1, can convert Kluyveromyces lactis into a petite-positive yeast. In this report, we describe the isolation of the MGI1 gene and show that it encodes the β-subunit of the mitochondrial F1-ATPase. The site of mutation in four independently isolated mgi1 alleles is at Arg435, which has changed to Gly in three cases and Ile in the fourth isolate. Disruption of MGI1 does not lead to the production of mitochondrial genome deletion mutants, indicating that an assembled F1 complex is needed for the “gain-of-function” phenotype found in mgi1 point mutants. The location of Arg435 in the β-subunit, as deduced from the three-dimensional structure of the bovine F1-ATPase, together with mutational sites in the previously identified mgi2 and mgi5 alleles, suggests that interaction of the β- and α- (MGI2) subunits with the γ-subunit (MGI5) is likely to be affected by the mutations.

scholarly journals Two genes, atpC1 and atpC2, for the γ subunit of Arabidopsis thaliana chloroplast ATP synthase

1991 ◽  
Vol 266 (12) ◽  
pp. 7333-7338
Author(s):  
N Inohara ◽  
A Iwamoto ◽  
Y Moriyama ◽  
S Shimomura ◽  
M Maeda ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Atp Synthase ◽  
Chloroplast Atp Synthase ◽  
Γ Subunit

Rice G protein γ subunit qPE9‐1 modulates root elongation for phosphorus uptake by involving 14‐3‐3 protein OsGF14b and plasma membrane H + ‐ATPase

2021 ◽  
Author(s):  
Ke Wang ◽  
Feiyun Xu ◽  
Wei Yuan ◽  
Dongping Zhang ◽  
Jianping Liu ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
G Protein ◽  
Root Elongation ◽  
Phosphorus Uptake ◽  
Γ Subunit

scholarly journals Copper-mediated regulation of cytochrome c553 and plastocyanin in the cyanobacterium Synechocystis 6803.

1992 ◽  
Vol 267 (27) ◽  
pp. 19054-19059
Author(s):  
L Zhang ◽  
B McSpadden ◽  
H.B. Pakrasi ◽  
J Whitmarsh
Keyword(s):  
Synechocystis 6803 ◽  
Cytochrome C553
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