F1-ATPase rotation and its inhibition from the viewpoint of solvent entropy

2020 ◽  
Vol 757 ◽  
pp. 137886
Author(s):  
Takashi Yoshidome
Keyword(s):  
F1 Atpase

Identification of the β- and γ-subunits of F1-ATPase as target antigens in anti-M2/PDC-E2 negative primary biliary cirrhosis (PBC)

2010 ◽  
Vol 48 (01) ◽  
Author(s):  
BE Preuß ◽  
J Dengjel ◽  
S Stevanovic ◽  
R Klein
Keyword(s):  
Primary Biliary Cirrhosis ◽  
Biliary Cirrhosis ◽  
F1 Atpase

Rotation of the engineered F1-ATPase with non-catalytic α-type P-loops

2018 ◽  
Vol 1859 ◽  
pp. e83
Author(s):  
Hiroshi Ueno ◽  
Rie Koga ◽  
Tomoko Masaike ◽  
Nobuyasu Koga ◽  
Hiroyuki Noji
Keyword(s):  
F1 Atpase

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 Properties of chloroplast F1-ATPase partially modified by 2-azido adenine nucleotides, including demonstration of three catalytic pathways.

1988 ◽  
Vol 263 (32) ◽  
pp. 16880-16885 ◽  
Author(s):  
Z X Xue ◽  
T Melese ◽  
K E Stempel ◽  
T J Reedy ◽  
P D Boyer
Keyword(s):  
Adenine Nucleotides ◽  
F1 Atpase

scholarly journals Lysine 155 in beta-subunit is a catalytic residue of Escherichia coli F1 ATPase.

1993 ◽  
Vol 268 (10) ◽  
pp. 6989-6994
Author(s):  
A.E. Senior ◽  
S. Wilke-Mounts ◽  
M.K. al-Shawi
Keyword(s):  
Escherichia Coli ◽  
Beta Subunit ◽  
Catalytic Residue ◽  
F1 Atpase

scholarly journals Probing the Energetic Metabolism of Resting Cysts under Different Conditions from Molecular and Physiological Perspectives in the Harmful Algal Blooms-Forming Dinoflagellate Scrippsiella trochoidea

2021 ◽  
Vol 22 (14) ◽  
pp. 7325
Author(s):  
Fengting Li ◽  
Aoao Yang ◽  
Zhangxi Hu ◽  
Siheng Lin ◽  
Yunyan Deng ◽  
...  
Keyword(s):  
Low Temperature ◽  
Harmful Algal Blooms ◽  
Algal Blooms ◽  
Atp Content ◽  
Energetic Metabolism ◽  
Scrippsiella Trochoidea ◽  
Vegetative Cells ◽  
F1 Atpase ◽  
Atpase Gene ◽  
Resting Cysts

Energetic metabolism is essential in maintaining the viability of all organisms. Resting cysts play important roles in the ecology of dinoflagellates, particularly for harmful algal blooms (HABs)-causative species. However, the energetic metabolism underlying the germination potency maintenance of resting cysts of dinoflagellate have been extremely scarce in studies from physiological and, particularly, molecular perspectives. Therefore, we used the cosmopolitan Scrippsiella trochoidea as a representative of HABs-forming and cyst-producing dinoflagellates in this work to obtain novel insights into the molecular mechanisms, regulating the energetic metabolism in dinoflagellate resting cysts, under different physical condition. As the starting step, we established a cDNA subtractive library via suppression subtractive hybridization (SSH) technology, from which we screened an incomplete sequence for the β subunit of ATP synthase gene (β-F1-ATPase), a key indicator for the status of cell’s energetic metabolism. The full-length cDNA of β-F1-ATPase gene from S.trochoidea (Stβ-F1-ATPase) was then obtained via rapid amplification of cDNA ends (RACE) (Accession: MZ343333). Our real-time qPCR detections, in vegetative cells and resting cysts treated with different physical conditions, revealed that (1) the expression of Stβ-F1-ATPase in resting cysts was generally much lower than that in vegetative cells, and (2) the Stβ-F1-ATPase expressions in the resting cysts under darkness, lowered temperature, and anoxia, and during an extended duration of dormancy, were significantly lower than that in cysts under the condition normally used for culture-maintaining (a 12 h light:12 h dark cycle, 21 °C, aerobic, and newly harvested). Our detections of the viability (via Neutral Red staining) and cellular ATP content of resting cysts, at the conditions corresponding to the abovementioned treatments, showed that both the viability and ATP content decreased rapidly within 12 h and then maintained at low levels within the 4-day experimentation under all the three conditions applied (4 °C, darkness, and anoxia), which are well in accordance with the measurements of the transcription of Stβ-F1-ATPase. These results demonstrated that the energy consumption of resting cysts reaches a low, but somehow stable, level within a short time period and is lower at low temperature, darkness, and anoxia than that at ambient temperature. Our work provides an important basis for explaining that resting cysts survive long-term darkness and low temperature in marine sediments from molecular and physiological levels.

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