Organellar Proton-ATPases by Nathan Nelson

By Nathan Nelson

THE global OF PROTON PUMPS Nathan Nelson uite often an observer appears to be like at a lifestyles phenomenon and asks ~himself why nature took this path out of numerous different on hand mec anisms. in an effort to comprehend this problem he may well first try and reconstruct the evolution of the method bearing in mind the most riding forces that have been assumed to exist over the last three. five billion years in the world. Now we all know that the electrochemical gradient of protons is the common high-energy intermediate produced and uti­ lized by means of each residing phone in nature. This excessive strength intermediate is an expression of other concentrations of lively protons within the faces of organic membranes. Why then did nature go with to make use of a pre­ dominantly electrochemical gradient of protons and no different ion? the reply to this question could lie within the surroundings within which the 1st dwelling creatures developed. a few of them could have been challenged through an acidic atmosphere that reduced their inner pH (by a proton leak via their membranes) to deadly degrees. To counteract those inci­ dents proton pumps advanced. self sustaining platforms have been devel­ oped. One used to be a proton pump coupled to energetically downhill vectorial electron delivery throughout membranes and the second one used to be an ATP-dependent proton pump. either one of them pump protons outward from the cells producing an electrochemical gradient of protons.

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As in the case of the cation antiport, anion exchange is driven by the concentration gradients of the substrate ions. In most cell types, the intracellular concentrations of Cl- and HC0 3- are lower than those in the external medium, due in part to the electronegativity of the cell interior. However, the inward concentration gradient of Cl- is generally greater than that of HC0 3-. This imbalance is predicted to drive the net influx of Cl- simultaneously with net HC0 3- efflux. Because HC0 3- is a base equivalent, this is anticipated to result in cytosolic acidification.

88. Hanada H, Hasebe M, Moriyama Y, et al. Molecular cloning of cDNA encoding the 16 kDa subunit of vacuolar H+-ATPase from mouse cerebellum. Biochem. Biophys, Res. Commun. 1991; 176:1062-1076. 89. Meagher L, McLean P, Finbow ME. Sequence of a cDNA from Drosophila coding for the 16 kD proteolipid component of the vacuolar H+ATPase. Nucleic Acids Res. 1990; 18:6712. 90. Lai S, Watson, ]C, Hansen ]N. Molecular cloning and sequencing of cDNAs encoding the proteolipid subunit of the vacuolar H+-ATPase from a higher plant.

In: Scarpa A, Carafoli E, Papa S. eds. Ion-Motive ATPases: Structure, Function, and Regulation (Vol. 671). New York: The New York Academy of Sciences, 1992:293309. 17. Moriyama Y, Nelson N. Nucleotide binding sites and chemical modification of the chromaffin granule proton ATPase. J Bioi Chern 1987; 262: 14723-14729. 18. Bowman EJ, Tenney K, Bowman BJ. Isolation of genes encoding the Neurospora vacuolar ATPase. J Bioi Chern 1988; 263:13994-14001. 19. Zimniak L, Dittrich P, Gogarten JP, et al. The cDNA sequence of the 69 kDa subunit of the carrot vacuolar H'-ATPase.

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