A2 Vertaisarvioitu katsausartikkeli tieteellisessä lehdessä
Pyrophosphate-Fueled Na+ and H+ Transport in Prokaryotes
Tekijät: Baykov AA, Malinen AM, Luoto HH, Lahti R
Kustantaja: AMER SOC MICROBIOLOGY
Julkaisuvuosi: 2013
Journal: Microbiology and Molecular Biology Reviews
Tietokannassa oleva lehden nimi: MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS
Lehden akronyymi: MICROBIOL MOL BIOL R
Numero sarjassa: 2
Vuosikerta: 77
Numero: 2
Aloitussivu: 267
Lopetussivu: 276
Sivujen määrä: 10
ISSN: 1092-2172
DOI: https://doi.org/10.1128/MMBR.00003-13
Tiivistelmä
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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