Refereed review article in scientific journal (A2)
Pyrophosphate-Fueled Na+ and H+ Transport in Prokaryotes
List of Authors: Baykov AA, Malinen AM, Luoto HH, Lahti R
Publisher: AMER SOC MICROBIOLOGY
Publication year: 2013
Journal: Microbiology and Molecular Biology Reviews
Journal name in source: MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS
Journal acronym: MICROBIOL MOL BIOL R
Number in series: 2
Volume number: 77
Issue number: 2
Start page: 267
End page: 276
Number of pages: 10
ISSN: 1092-2172
DOI: http://dx.doi.org/10.1128/MMBR.00003-13
Abstract
In its early history, life appeared to depend on pyrophosphate rather than ATP as the source of energy. Ancient membrane pyrophosphatases that couple pyrophosphate hydrolysis to active H+ transport across biological membranes (H+-pyrophosphatases) have long been known in prokaryotes, plants, and protists. Recent studies have identified two evolutionarily related and widespread prokaryotic relics that can pump Na+ (Na+-pyrophosphatase) or both Na+ and H+ (Na+,H+-pyrophosphatase). Both these transporters require Na+ for pyrophosphate hydrolysis and are further activated by K+. The determination of the three-dimensional structures of H+- and Na+-pyrophosphatases has been another recent breakthrough in the studies of these cation pumps. Structural and functional studies have highlighted the major determinants of the cation specificities of membrane pyrophosphatases and their potential use in constructing transgenic stress-resistant organisms.
In its early history, life appeared to depend on pyrophosphate rather than ATP as the source of energy. Ancient membrane pyrophosphatases that couple pyrophosphate hydrolysis to active H+ transport across biological membranes (H+-pyrophosphatases) have long been known in prokaryotes, plants, and protists. Recent studies have identified two evolutionarily related and widespread prokaryotic relics that can pump Na+ (Na+-pyrophosphatase) or both Na+ and H+ (Na+,H+-pyrophosphatase). Both these transporters require Na+ for pyrophosphate hydrolysis and are further activated by K+. The determination of the three-dimensional structures of H+- and Na+-pyrophosphatases has been another recent breakthrough in the studies of these cation pumps. Structural and functional studies have highlighted the major determinants of the cation specificities of membrane pyrophosphatases and their potential use in constructing transgenic stress-resistant organisms.
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