Inhibition of F1-ATPase Rotational Catalysis by the Carboxyl-terminal Domain of the ϵ Subunit

Nakanishi‐Matsui, Mayumi; Sekiya, Motohiro; Yano, Shio; Futai, Masamitsu

doi:10.1074/jbc.m114.578872

Cited by 16 publications

(21 citation statements)

References 36 publications

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“…The very C‐terminal helix 2 in the ε e state interacts with the subunits α, β and γ . For some bacterial enzymes it was shown that the CTD of subunit ε has an ATP‐binding motive that can act as an ATP sensor . Similarly, Raghunathan et al .…”

Section: Discussionmentioning

confidence: 99%

“…proposed a model for the M. mazei Gö1 A‐ATP synthase, where ATP can bind to the CDT of subunit F. In this model, subunit F Mm facilitates the binding of ATP to the nucleotide‐binding site in subunit B . In contrast, unlike the stimulating role of subunit F the CTD of subunit ε in its extended conformation was shown to be an intrinsic inhibitor for ATP hydrolysis, but not for ATP synthesis, to prevent futile ATP hydrolysis at low ATP concentrations . Despite similar domain components subunits F and ε have very different regulatory functions in their respective ATP synthases.…”

Section: Discussionmentioning

confidence: 99%

“…The very C-terminal helix 2 in the e e state interacts with the subunits a, b and c [32][33][34][35]. For some bacterial enzymes it was shown that the CTD of subunit e has an ATP-binding motive that can act as an ATP sensor [36,37]. Similarly, Raghunathan et al proposed a model for the M. mazei G€ o1 A-ATP synthase, where ATP can bind to the CDT of subunit F. In this model, subunit F Mm facilitates the binding of ATP to the nucleotide-binding site in subunit B [10].…”

Section: Discussionmentioning

confidence: 99%

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Conformational dynamics of the rotary subunit F in the A₃B₃DF complex of Methanosarcina mazei Gö1 A‐ATP synthase monitored by single‐molecule FRET

et al. 2017

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In archaea the A A ATP synthase uses a transmembrane electrochemical potential to generate ATP, while the soluble A domain (subunits A B DF) alone can hydrolyse ATP. The three nucleotide-binding AB pairs form a barrel-like structure with a central orifice that hosts the rotating central stalk subunits DF. ATP binding, hydrolysis and product release cause a conformational change inside the A:B-interface, which enforces the rotation of subunits DF. Recently, we reported that subunit F is a stimulator of ATPase activity. Here, we investigated the nucleotide-dependent conformational changes of subunit F relative to subunit D during ATP hydrolysis in the A B DF complex of the Methanosarcina mazei Gö1 A-ATP synthase using single-molecule Förster resonance energy transfer. We found two conformations for subunit F during ATP hydrolysis.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Conformational dynamics of the rotary subunit F in the A₃B₃DF complex of Methanosarcina mazei Gö1 A‐ATP synthase monitored by single‐molecule FRET

et al. 2017

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“…In TF 1 , inhibition is apparent only at low concentrations of Mg-ATP (below 50 lM) [16,32]. By contrast, in EF 1 , inhibition is apparent at any concentration of Mg-ATP [33][34][35].…”

Section: Mechanism Of E-inhibitionmentioning

confidence: 96%

Structure of a thermophilic F₁‐ATPase inhibited by an ε‐subunit: deeper insight into the ε‐inhibition mechanism

et al. 2015

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F 1 -ATPase (F 1 ) is the catalytic sector in F o F 1 -ATP synthase that is responsible for ATP production in living cells. In catalysis, its three catalytic b-subunits undergo nucleotide occupancy-dependent and concerted open-close conformational changes that are accompanied by rotation of the c-subunit. Bacterial and chloroplast F 1 are inhibited by their own e-subunit. In the einhibited Escherichia coli F 1 structure, the e-subunit stabilizes the overall conformation (half-closed, closed, open) of the b-subunits by inserting its C-terminal helix into the a 3 b 3 cavity. The structure of e-inhibited thermophilic F 1 is similar to that of E. coli F 1 , showing a similar conformation of the e-subunit, but the thermophilic e-subunit stabilizes another unique overall conformation (open, closed, open) of the b-subunits. The e-C-terminal helix 2 and hook are conserved between the two structures in interactions with target residues and in their positions. Rest of the e-C-terminal domains are in quite different conformations and positions, and have different modes of interaction with targets. This region is thought to serve e-inhibition differently. For inhibition, the e-subunit contacts the second catches of some of the b-and a-subunits, the N-and C-terminal helices, and some of the Rossmann fold segments. Those contacts, as a whole, lead to positioning of those b-and a-second catches in e-inhibition-specific positions, and prevent rotation of the c-subunit. Some of the structural features are observed even in IF 1 inhibition in mitochondrial F 1 .

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“…This conformational change allows the C-terminus of subunit  to reach the α 3 β 3 hexamer. Recent findings clearly demonstrate that the Loop2/helix2 of the C-terminal domain plays a pivotal role in inhibiting activity through decreased rotation by extending duration of the inhibited state [130]. Residues εS108 in loop2 and εY114 have been identified as being important for inhibition [130].…”

Section: Subunit  Of F 1 F O Atp Synthasesmentioning

confidence: 99%

The role of N157 of A-ATP synthase subunit B in nucleotide binding and expression, production and structural and mechanistic features of subunits α and ε of Mycobacterium tuberculosis F-ATP synthase

Sundararaman¹

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NMR and attempts have been invested with crystallisation techniques to garner data to elucidate the structure of this protein. To explore the mechanistic features, chimeric proteins of M. tuberculosis and E. coli (Ec) were generated and have been studied parallel to Ecε and PSε to gain insight into the functioning of Mtε. Mtε on reconstitution with PS3α 3 β 3 γ had no effect on the ATPase activity of the PS3α 3 β 3 γ complex. Ecε also similarly did not alter the activity of the complex PS3α 3 β 3 γ. In contrast, PS3ε on reconstitution increased the ATPase activity of PS3α 3 β 3 γ, highlighting the specific interaction required between the subunits α and ε. This observation was further validated by reconstituting α chi 3 β 3 γ with Mtε that showed increased ATPase activity. Taken together, these studies demonstrate that the shorter length of Mtε is compensated with the longer Mt

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Inhibition of F1-ATPase Rotational Catalysis by the Carboxyl-terminal Domain of the ϵ Subunit

Cited by 16 publications

References 36 publications

Conformational dynamics of the rotary subunit F in the A₃B₃DF complex of Methanosarcina mazei Gö1 A‐ATP synthase monitored by single‐molecule FRET

Conformational dynamics of the rotary subunit F in the A₃B₃DF complex of Methanosarcina mazei Gö1 A‐ATP synthase monitored by single‐molecule FRET

Structure of a thermophilic F₁‐ATPase inhibited by an ε‐subunit: deeper insight into the ε‐inhibition mechanism

The role of N157 of A-ATP synthase subunit B in nucleotide binding and expression, production and structural and mechanistic features of subunits α and ε of Mycobacterium tuberculosis F-ATP synthase

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Inhibition of F1-ATPase Rotational Catalysis by the Carboxyl-terminal Domain of the ϵ Subunit

Cited by 16 publications

References 36 publications

Conformational dynamics of the rotary subunit F in the A3B3DF complex of Methanosarcina mazei Gö1 A‐ATP synthase monitored by single‐molecule FRET

Conformational dynamics of the rotary subunit F in the A3B3DF complex of Methanosarcina mazei Gö1 A‐ATP synthase monitored by single‐molecule FRET

Structure of a thermophilic F1‐ATPase inhibited by an ε‐subunit: deeper insight into the ε‐inhibition mechanism

The role of N157 of A-ATP synthase subunit B in nucleotide binding and expression, production and structural and mechanistic features of subunits α and ε of Mycobacterium tuberculosis F-ATP synthase

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Conformational dynamics of the rotary subunit F in the A₃B₃DF complex of Methanosarcina mazei Gö1 A‐ATP synthase monitored by single‐molecule FRET

Conformational dynamics of the rotary subunit F in the A₃B₃DF complex of Methanosarcina mazei Gö1 A‐ATP synthase monitored by single‐molecule FRET

Structure of a thermophilic F₁‐ATPase inhibited by an ε‐subunit: deeper insight into the ε‐inhibition mechanism