Sulfite both stimulates and inhibits the yeast vacuolar H(+)-ATPase.

Kibak, Henrik; Eeckhout, D Van; Cutler, T; Taiz, Saundra Lee; Taiz, Lincoln

doi:10.1016/s0021-9258(19)49466-0

Cited by 22 publications

(2 citation statements)

References 37 publications

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“…The clathrin-coated vesicle ATPase has been shown to have a low K m site of 80 µM and a high K m site of 800 µM ATP (Arai et al, 1989), but most other V-type ATPases appear to exhibit a single apparent K m falling between these two values (Bowman & Bowman, 1982;Wang & Gluck, 1990;Randall & Sze, 1986). Reported apparent K m values for the purified yeast vacuolar H + -ATPase range from approximately 250 µM ATP (Kibak et al, 1993;Uchida et al, 1985) up to 1.3 mM ATP in the presence of sulfite (Kibak et al, 1993). The single apparent K m value (528 ( 54 µM ATP) reported here for the membrane-bound yeast 10946 Biochemistry, Vol.…”

Section: Discussionmentioning

confidence: 99%

Mutational Analysis of the Catalytic Subunit of the Yeast Vacuolar Proton-Translocating ATPase

Liu

Kane

1996

Biochemistry

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In order to generate a set of tools for probing structure-function relationships in the catalytic subunit of the yeast vacuolar H(+)-ATPase, the gene encoding this subunit (VMA1) was randomly mutagenized. Mutant plasmids unable to complement the growth defects of yeast cells lacking an intact VMA1 gene were isolated and sequenced. Eight different mutant alleles of VMA1 were examined for levels of the catalytic subunit and other subunits of the enzyme, assembly of the ATPase complex, targeting to the vacuolar membrane, and concanamycin A-sensitive ATPase activity. The mutations S811P and E740D resulted in mutant enzymes that assembled fully but were incapable of ATP hydrolysis, and the mutation E785G generated a similar but somewhat less severe phenotype (17% of the ATPase activity of wild-type vacuoles). When MgATP-dependent stripping of the peripheral subunits by 100 mM KNO3 was examined in these three mutants, only the E785G mutant exhibited significant stripping, suggesting that ATP hydrolysis, even at relatively low levels, generates a conformation susceptible to dissociation. Plasmids containing the mutations E751G and F752S partially complemented the growth defects and resulted in partial defects in ATPase activity that appear to reflect reduced catalytic efficiency. Partial defects in growth and ATPase activity were also seen in the Y797H mutant, but this mutation caused an assembly defect manifested as a preferential loss of two of the peripheral subunits of the enzyme. The phenotypes of these mutants are interpreted in the context of homologies with other V-type and F-type ATPases.

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Section: Discussionmentioning

confidence: 99%

Mutational Analysis of the Catalytic Subunit of the Yeast Vacuolar Proton-Translocating ATPase

Liu

Kane

1996

Biochemistry

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“…While the presence of ATP could slowly release the tightly bound ADP during catalysis, the presence of sulfite significantly accelerated the ATP-dependent reactivation of the ADP-inhibited complex. However, sulfite was shown to inhibit ATP synthesis, in a way not readily explained by competition with Pi ( Pacheco-Moisés et al, 2002 ) and, consistently with the latter inhibition, was also shown to decrease the H + /ATP coupling ratio, as measured in the hydrolysis direction, both in the V-type ATPase ( Kibak et al, 1993 ), and in the ATP synthase ( Cappellini et al, 1997 ). The sulfite-activated hydrolysis was still completely inhibited by F O inhibitors, such as oligomycin, venturicidin, DCCD ( Moyle and Mitchell, 1975 ; Zhang et al, 1993 ; Cappellini et al, 1997 ; Pacheco-Moisés et al, 2000 ; Pacheco-Moisés et al, 2002 ).…”

Section: Nucleotide- and Ligand-induced Changes In The H + ...mentioning

confidence: 75%

Modulation of the H+/ATP coupling ratio by ADP and ATP as a possible regulatory feature in the F-type ATP synthases

Turina

2022

Front. Mol. Biosci.

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F-type ATP synthases are transmembrane enzymes, which play a central role in the metabolism of all aerobic and photosynthetic cells and organisms, being the major source of their ATP synthesis. Catalysis occurs via a rotary mechanism, in which the free energy of a transmembrane electrochemical ion gradient is converted into the free energy of ATP phosphorylation from ADP and Pi, and vice versa. An ADP, tightly bound to one of the three catalytic sites on the stator head, is associated with catalysis inhibition, which is relieved by the transmembrane proton gradient and by ATP. By preventing wasteful ATP hydrolysis in times of low osmotic energy and low ATP/ADP ratio, such inhibition constitutes a classical regulatory feedback effect, likely to be an integral component of in vivo regulation. The present miniview focuses on an additional putative regulatory phenomenon, which has drawn so far little attention, consisting in a substrate-induced tuning of the H+/ATP coupling ratio during catalysis, which might represent an additional key to energy homeostasis in the cell. Experimental pieces of evidence in support of such a phenomenon are reviewed.

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Sulfite Interacts with the ATP Synthase from Chloroplasts and Cyanobacteria by Competition with Phosphate

Bakels¹,

Wielink²,

Krab³

et al. 1995

Photosynthesis: From Light to Biosphere

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Sulfite both stimulates and inhibits the yeast vacuolar H(+)-ATPase.

Cited by 22 publications

References 37 publications

Mutational Analysis of the Catalytic Subunit of the Yeast Vacuolar Proton-Translocating ATPase

Mutational Analysis of the Catalytic Subunit of the Yeast Vacuolar Proton-Translocating ATPase

Modulation of the H+/ATP coupling ratio by ADP and ATP as a possible regulatory feature in the F-type ATP synthases

Sulfite Interacts with the ATP Synthase from Chloroplasts and Cyanobacteria by Competition with Phosphate

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