The cDNA sequence of the 69-kDa subunit of the carrot vacuolar H+-ATPase. Homology to the beta-chain of F0F1-ATPases.

Zimniak, Ludwika; Dittrich, P.; Gogarten, J. Peter; Kibak, Henrik; Taiz, Lincoln

doi:10.1016/s0021-9258(19)76514-4

Cited by 268 publications

(23 citation statements)

References 67 publications

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“…Functionally, however, the A and F types show more similarities-for instance, the ability to synthesize ATP in vivo (Iwabe et al, 1989;Ihara et al, 1992;Müller et al, 1999;Schäfer et al, 1999). These similarities in sequence, structure, and function point to the existence of a shared common ancestor, which underwent a series of changes to arrive at the three modern ATPase classes (Imamura et al, 2003;Zimniak et al, 1988). Due to the conservation of their basic structure and function across biological kingdoms, the ATP synthases are an intriguing framework within which to study several major events in the evolution of life, from its origin and the rooting of the tree of life (Mulkidjanian et al, 2009) to the prokaryoteeukaryote transition (Hilario and Gogarten, 1998), among others.…”

Section: Introductionmentioning

confidence: 99%

ATP synthase: Evolution, energetics, and membrane interactions

Nirody

Budin

Rangamani

2020

Journal of General Physiology

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The synthesis of ATP, life’s “universal energy currency,” is the most prevalent chemical reaction in biological systems and is responsible for fueling nearly all cellular processes, from nerve impulse propagation to DNA synthesis. ATP synthases, the family of enzymes that carry out this endless task, are nearly as ubiquitous as the energy-laden molecule they are responsible for making. The F-type ATP synthase (F-ATPase) is found in every domain of life and has facilitated the survival of organisms in a wide range of habitats, ranging from the deep-sea thermal vents to the human intestine. Accordingly, there has been a large amount of work dedicated toward understanding the structural and functional details of ATP synthases in a wide range of species. Less attention, however, has been paid toward integrating these advances in ATP synthase molecular biology within the context of its evolutionary history. In this review, we present an overview of several structural and functional features of the F-type ATPases that vary across taxa and are purported to be adaptive or otherwise evolutionarily significant: ion channel selectivity, rotor ring size and stoichiometry, ATPase dimeric structure and localization in the mitochondrial inner membrane, and interactions with membrane lipids. We emphasize the importance of studying these features within the context of the enzyme’s particular lipid environment. Just as the interactions between an organism and its physical environment shape its evolutionary trajectory, ATPases are impacted by the membranes within which they reside. We argue that a comprehensive understanding of the structure, function, and evolution of membrane proteins—including ATP synthase—requires such an integrative approach.

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Section: Introductionmentioning

confidence: 99%

ATP synthase: Evolution, energetics, and membrane interactions

Nirody

Budin

Rangamani

2020

Journal of General Physiology

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“…The soluble portions of both ATPases have a sixfold symmetry created by the alternation of A and B subunits in V 1 and the ␤ and ␣ subunits in F 1 . A and B share 25% sequence identity with ␤ and ␣, respectively (Bowman et al, 1988a, b;Zimniak et al, 1988). In addition, each hexamer contains three catalytic sites capable of ATP hydrolysis (Arai et al, 1988).…”

Section: Introductionmentioning

confidence: 99%

The Mechanochemistry of V-ATPase Proton Pumps

Grabe

Wang

Oster

2000

Biophysical Journal

110

104

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The vacuolar H(+)-ATPases (V-ATPases) are a universal class of proton pumps that are structurally similar to the F-ATPases. Both protein families are characterized by a membrane-bound segment (V(o), F(o)) responsible for the translocation of protons, and a soluble portion, (V(1), F(1)), which supplies the energy for translocation by hydrolyzing ATP. Here we present a mechanochemical model for the functioning of the V(o) ion pump that is consistent with the known structural features and biochemistry. The model reproduces a variety of experimental measurements of performance and provides a unified view of the many mechanisms of intracellular pH regulation.

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“…They induce self-excision and subsequent ligation of two flanking sequences, named exteins, by the formation of a native peptide bond. Protein splicing was first observed in 1988 in yeast trifluoperazine-resistant TFP1-408 gene [64][65][66], and was confirmed in the yeast vacuolar membrane ATPase VMA-1 gene [67] and yeast TFP-1 gene in 1990 [68]. Up to date, there are more than three hundred inteins identified with wide occurrence in all three domains of living organisms [69].…”

Section: Inteinmentioning

confidence: 98%

Making Circles: Recent Advance in Chemical and Enzymatic Approaches in Peptide Macrocyclization

2018

JCAR

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Macrocyclic peptides have emerged as an important class of molecules for drug discovery due to their enhanced stability and bioavailability. Since the 1990s, ligation chemistries have been extensively studied for preparing peptide macrocycles. The ligation chemistries usually go through an energetically favored capture coupled with an acyl transfer reaction to overcome the disfavored entropy ring formation and facilitate the formation of the cyclic amide bond. Concurrently with chemical methods, several enzymatic approaches utilizing peptide ligases have also been explored. These peptide ligases are enzymes that involve in the production of naturally-occurring cyclic peptides in diverse organisms. Many enzymes have been isolated and proved to be highly efficient in the production of cyclic peptides. Here, we review the recent advance in chemical ligation and enzymatic approaches in making cycles.NorCal Open Access Publications . 01 .

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The cDNA sequence of the 69-kDa subunit of the carrot vacuolar H+-ATPase. Homology to the beta-chain of F0F1-ATPases.

Cited by 268 publications

References 67 publications

ATP synthase: Evolution, energetics, and membrane interactions

ATP synthase: Evolution, energetics, and membrane interactions

The Mechanochemistry of V-ATPase Proton Pumps

Making Circles: Recent Advance in Chemical and Enzymatic Approaches in Peptide Macrocyclization

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