Identification of Proteolipid from an Extremely Halophilic ArchaeonHalobacterium salinarumas anN,N′-Dicyclohexyl-carbodiimide Binding Subunit of ATP Synthase

Ihara, Kenji; Watanabe, Satoshi; Sugimura, Ken-ichiro; Katagiri, Izumi; Mukohata, Yasuo

doi:10.1006/abbi.1997.9972

Cited by 20 publications

(11 citation statements)

References 30 publications

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“…38 Mass spectroscopy of the investigated sample corroborated the presence of proteins with a mass of 7517 and 7618 Da corresponding to the native c-ring sequence. 243 C-rings occurred as rings with 6.5 ± 0.5 nm diameter and 1.8 nm protrusion height, which formed dimers in the membrane. Dimer formation has been described for mitochondrial ATP synthases, but the prokaryotic homologues have been thought to be monomers.…”

Section: Dynamic Imaging Of Proteinsmentioning

confidence: 99%

Filming Biomolecular Processes by High-Speed Atomic Force Microscopy

2014

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Section: Dynamic Imaging Of Proteinsmentioning

confidence: 99%

Filming Biomolecular Processes by High-Speed Atomic Force Microscopy

2014

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“…Although subunit A carried a hexahistidine tag and although it was apparently accessible to the Ni 2+ -NTA-matrix, the enzyme could not be purified by affinity chromatography since it denatured on the column. Instability leading to the purification of only subcomplexes was observed very often [60][61][62][63][64][65][66][67][68][69][70]. This denaturation/ inactivation was seen before with the enzyme directly enriched from cells of M. mazei [71].…”

Section: Discussionmentioning

confidence: 90%

The a subunit of the A1AO ATP synthase of Methanosarcina mazei Gö1 contains two conserved arginine residues that are crucial for ATP synthesis

Gloger¹,

Born²,

Antosch³

et al. 2015

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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Like the evolutionary related F1FO ATP synthases and V1VO ATPases, the A1AO ATP synthases from archaea are multisubunit, membrane-bound transport machines that couple ion flow to the synthesis of ATP. Although the subunit composition is known for at least two species, nothing is known so far with respect to the function of individual subunits or amino acid residues. To pave the road for a functional analysis of A1AO ATP synthases, we have cloned the entire operon from Methanosarcina mazei into an expression vector and produced the enzyme in Escherichia coli. Inverted membrane vesicles of the recombinants catalyzed ATP synthesis driven by NADH oxidation as well as artificial driving forces. [Formula: see text] as well as ΔpH were used as driving forces which is consistent with the inhibition of NADH-driven ATP synthesis by protonophores. Exchange of the conserved glutamate in subunit c led to a complete loss of ATP synthesis, proving that this residue is essential for H+ translocation. Exchange of two conserved arginine residues in subunit a has different effects on ATP synthesis. The role of these residues in ion translocation is discussed.

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“…We found that the N-terminus of group 2 c-subunits is necessary for their correct membrane insertion both in homologous and in recombinant expression systems. Additionally, we found that such an N-terminus acts as a signal peptide not only in V-type c-subunits [29][30][31] but also in F-type c-subunits, which was not known to date. Finally, we found that the long N-terminus of the group 2 c-subunits cannot be replaced by the short N-terminus of group 1 c-subunits because such a replacement completely abolishes membrane insertion.…”

Section: Discussionmentioning

confidence: 99%

“…In nuclear‐encoded mitochondrial ATP synthases, the N‐terminus of the c‐subunit certainly plays a role in mitochondrial targeting, but membrane insertion is then guided by the YidC homolog Oxa1 . Furthermore, in certain bacterial and archaeal V‐type ATPases, the N‐terminus of the c‐subunits was shown not to be present in the mature form of the protein, suggesting a role as signal peptide . Finally, it is also possible that other factors, extrinsic to the c‐subunit, are involved in the assembly of c‐rings, i.e.…”

Section: Introductionmentioning

confidence: 99%

Role of the N‐terminal signal peptide in the membrane insertion of Aquifex aeolicus F₁F₀ATP synthase c‐subunit

et al. 2013

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Rotary ATPases are membrane protein complexes that couple ATP hydrolysis to ion translocation across the membrane. Overall, they are evolutionarily well conserved, but the N‐terminal segments of their rotary subunits (c‐subunits) possess different lengths and levels of hydrophobicity across species. By analyzing the N‐terminal variability, we distinguish four phylogenetic groups of c‐subunits (groups 1–4). We characterize a member of group 2, the c‐subunit from Aquifex aeolicus F1F0 ATP synthase, both in native cells and in a heterologous expression system. We demonstrate that its N‐terminal segment forms a signal peptide with signal recognition particle (SRP) recognition features and is obligatorily required for membrane insertion. Based on our study and on previous characterizations of c‐subunits from other organisms, we propose that c‐subunits follow different membrane insertion pathways.

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Identification of Proteolipid from an Extremely Halophilic ArchaeonHalobacterium salinarumas anN,N′-Dicyclohexyl-carbodiimide Binding Subunit of ATP Synthase

Cited by 20 publications

References 30 publications

Filming Biomolecular Processes by High-Speed Atomic Force Microscopy

Filming Biomolecular Processes by High-Speed Atomic Force Microscopy

The a subunit of the A1AO ATP synthase of Methanosarcina mazei Gö1 contains two conserved arginine residues that are crucial for ATP synthesis

Role of the N‐terminal signal peptide in the membrane insertion of Aquifex aeolicus F₁F₀ATP synthase c‐subunit

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Identification of Proteolipid from an Extremely Halophilic ArchaeonHalobacterium salinarumas anN,N′-Dicyclohexyl-carbodiimide Binding Subunit of ATP Synthase

Cited by 20 publications

References 30 publications

Filming Biomolecular Processes by High-Speed Atomic Force Microscopy

Filming Biomolecular Processes by High-Speed Atomic Force Microscopy

The a subunit of the A1AO ATP synthase of Methanosarcina mazei Gö1 contains two conserved arginine residues that are crucial for ATP synthesis

Role of the N‐terminal signal peptide in the membrane insertion of Aquifex aeolicus F1F0ATP synthase c‐subunit

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Role of the N‐terminal signal peptide in the membrane insertion of Aquifex aeolicus F₁F₀ATP synthase c‐subunit