Torque Generation and Utilization in Motor Enzyme F0F1-ATP Synthase

Usukura, Eiji; Suzuki, Toshiharu; Furuike, Shou; Soga, Naoki; Saita, Ei Ichiro; Hisabori, Toru; Kinosita, Kazuhiko; Yoshida, Masasuke

doi:10.1074/jbc.m111.305938

Cited by 40 publications

(25 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Recent single-molecule studies have revealed that the C -terminal region of the β subunit shows a large-scale conformational change at around 0°533, which contributes to generating half of the rotational torque, that is, approximately 20 pN·nm rad −1 3435. Our experimental results suggest that the TS reaction contributes greatly to torque generation at around 0°.…”

Section: Discussionmentioning

confidence: 49%

Characterization of the temperature-sensitive reaction of F1-ATPase by using single-molecule manipulation

Watanabe

Noji

2014

Sci Rep

View full text Add to dashboard Cite

F1-ATPase (F1) is a rotary motor protein that couples ATP hydrolysis to mechanical rotation with high efficiency. In our recent study, we observed a highly temperature-sensitive (TS) step in the reaction catalyzed by a thermophilic F1 that was characterized by a rate constant remarkably sensitive to temperature and had a Q10 factor of 6–19. Since reactions with high Q10 values are considered to involve large conformational changes, we speculated that the TS reaction plays a key role in the rotation of F1. To clarify the role of the TS reaction, in this study, we conducted a stall and release experiment using magnetic tweezers, and assessed the torque generated during the TS reaction. The results indicate that the TS reaction generates the same amount of rotational torque as does ATP binding, but more than that generated during ATP hydrolysis. Thus, we confirmed that the TS reaction contributes significantly to the rotation of F1.

show abstract

Section: Discussionmentioning

confidence: 49%

Characterization of the temperature-sensitive reaction of F1-ATPase by using single-molecule manipulation

Watanabe

Noji

2014

Sci Rep

View full text Add to dashboard Cite

show abstract

“…However, the mechanism contributing to the energy deficit remains unclear owing to the diversity of energy regulatory elements and complexity of energy production, transfer and control. Moreover, a growing body of evidence indicates that cellular energy levels are closely related to the activity, transcription and translation of certain regulatory elements [15-18]. Among these regulatory elements, proteins that synthesize (ATP synthase), dissipate (alternative oxidase, AOX; and mitochondrial inner membrane uncoupling proteins, UCP), transport [adenosine diphosphate (ADP)/ATP carrier, AAC] and regulate (sucrose non-fermenting-1-related kinase, SnRK) ATP have attracted considerable attention.…”

Section: Introductionmentioning

confidence: 99%

Energy status of ripening and postharvest senescent fruit of litchi (Litchi chinensis Sonn.)

Qian

et al. 2013

BMC Plant Biol

126

View full text Add to dashboard Cite

BackgroundRecent studies have demonstrated that cellular energy is a key factor switching on ripening and senescence of fruit. However, the factors that influence fruit energy status remain largely unknown.ResultsHPLC profiling showed that ATP abundance increased significantly in developing preharvest litchi fruit and was strongly correlated with fruit fresh weight. In contrast, ATP levels declined significantly during postharvest fruit senescence and were correlated with the decrease in the proportion of edible fruit. The five gene transcripts isolated from the litchi fruit pericarp were highly expressed in vegetative tissues and peaked at 70 days after flowering (DAF) consistent with fruit ADP concentrations, except for uncoupling mitochondrial protein 1 (UCP1), which was predominantly expressed in the root, and ATP synthase beta subunit (AtpB), which was up-regulated significantly before harvest and peaked 2 days after storage. These results indicated that the color-breaker stage at 70 DAF and 2 days after storage may be key turning points in fruit energy metabolism. Transcript abundance of alternative oxidase 1 (AOX1) increased after 2 days of storage to significantly higher levels than those of LcAtpB, and was down-regulated significantly by exogenous ATP. ATP supplementation had no significant effect on transcript abundance of ADP/ATP carrier 1 (AAC1) and slowed the changes in sucrose non-fermenting-1-related kinase 2 (SnRK2) expression, but maintained ATP and energy charge levels, which were correlated with delayed senescence.ConclusionsOur results suggest that senescence of litchi fruit is closely related with energy. A surge of LcAtpB expression marked the beginning of fruit senescence. The findings may provide a new strategy to extend fruit shelf life by regulating its energy level.

show abstract

“…The 22 residues of the N-terminal helix and the 43 residues of the C-terminal helix in the γ subunit are deleted. c The positions of deletion in the HTH structure are shown in red (Usukura et al 2012). d All residues of the HTH in contact with the γ subunit are substituted with glycine or alanine ( red region ) (Tanigawara et al 2012) …”

Section: Robustnessmentioning

confidence: 99%

“…The helix-turn-helix (HTH) structure of the β subunits forming the main interface of the stator orifice was investigated (Usukura et al 2012). Figure 5a highlights the HTH structure in blue.…”

Section: Robustnessmentioning

confidence: 99%

See 1 more Smart Citation

Catalytic robustness and torque generation of the F1-ATPase

2017

View full text Add to dashboard Cite

The F1-ATPase is the catalytic portion of the FoF1 ATP synthase and acts as a rotary molecular motor when it hydrolyzes ATP. Two decades have passed since the single-molecule rotation assay of F1-ATPase was established. Although several fundamental issues remain elusive, basic properties of F-type ATPases as motor proteins have been well characterized, and a large part of the reaction scheme has been revealed by the combination of extensive structural, biochemical, biophysical, and theoretical studies. This review is intended to provide a concise summary of the fundamental features of F1-ATPases, by use of the well-described model F1 from the thermophilic Bacillus PS3 (TF1). In the last part of this review, we focus on the robustness of the rotary catalysis of F1-ATPase to provide a perspective on the re-designing of novel molecular machines.

show abstract

Torque Generation and Utilization in Motor Enzyme F0F1-ATP Synthase

Cited by 40 publications

References 41 publications

Characterization of the temperature-sensitive reaction of F1-ATPase by using single-molecule manipulation

Characterization of the temperature-sensitive reaction of F1-ATPase by using single-molecule manipulation

Energy status of ripening and postharvest senescent fruit of litchi (Litchi chinensis Sonn.)

Catalytic robustness and torque generation of the F1-ATPase

Contact Info

Product

Resources

About