Abstract
The plasma membrane H+‐ATPase of fungi and plants is a single polypeptide of fewer than 1,000 residues that extrudes protons from the cell against a large electric and concentration gradient. The minimalist structure of this nanomachine is in stark contrast to that of the large multi‐subunit FOF1 ATPase of mitochondria, which is also a proton pump, but under physiological conditions runs in the reverse direction to act as an ATP synthase. The plasma membrane H+‐ATPase is a P‐type ATPase, defined by having an obligatory phosphorylated reaction cycle intermediate, like cation pumps of animal membranes, and thus, this pump has a completely different mechanism to that of FOF1 ATPases, which operates by rotary catalysis. The work that led to these insights in plasma membrane H+‐ATPases of fungi and plants has a long history, which is briefly summarized in this review.
Highlights
It has been known since ancient times that yeast secretes acid during glucose fermentation without this phenomenon being connected with any essential process in yeast
This review recapitulates the discovery of the plasma membrane proton pump (H+‐ATPase) and will highlight recent advances in our understanding of the function, regulation, and structure of this pump, so surprisingly different from other proton pumps that it caused eyebrows to rise
An important discovery that demonstrated that the plasma membrane H+‐ATPase is under tight metabolic control came when it was shown that the enzyme is posttranslationally activated by glucose metabolism in a way that increases proton pumping tenfold (Serrano, 1983)
Summary
It has been known since ancient times that yeast secretes acid during glucose fermentation without this phenomenon being connected with any essential process in yeast. Why are the two presumed proton pumps of the yeast cell, the mitochondrial and the plasma membrane ATPases, so different in their structure and mechanism?
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