Potassium- or sodium-efflux ATPase, a key enzyme in the evolution of fungi

被引:85
作者
Benito, B [1 ]
Garciadeblás, B [1 ]
Rodríguez-Navarro, A [1 ]
机构
[1] Univ Politecn Madrid, Escuela Tecn Super Ingn Agron, Dept Biotechnol, E-28040 Madrid, Spain
来源
MICROBIOLOGY-SGM | 2002年 / 148卷
关键词
cation; pump; Schizosaccharomyces pombe; Leishmania; Trypanosoma;
D O I
10.1099/00221287-148-4-933
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Potassium is the most abundant cation in cells. Therefore, plant-associated fungi and intracellular parasites are permanently or circumstantially exposed to high K+ and must avoid excessive K+ accumulation activating K+ efflux systems. Because high K+ and high pH are compatible in natural environments, free-living organisms cannot keep a permanent transmembrane DeltapH and cannot rely only on K+/H+ antiporters, as do mitochondria. This study shows that the Schizosaccharomyces pombe CTA3 is a K+-efflux ATPase, and that other fungi are furnished with Na+-efflux ATPases, which also pump Na+. All these fungal ATPases, including those pumping only Na+, form a phylogenetic group, IID or ENA, among P-type ATPases. By searching in databases and partial cloning of ENA genes in species of Zygomycetes and Basidiomycetes, the authors conclude that probably all fungi have these genes. This study indicates that fungal K+- or Na+-ATPases evolved from an ancestral K+-ATPase, through processes of gene duplication. In yeast hemiascomycetes these duplications have occurred recently and produced bifunctional ATPases, whereas in Neurospora, and probably in other euascomycetes, they occurred earlier in evolution and produced specialized ATPases. In Schizosaccharomyces, adaptation to Na+ did not involve the duplication of the K+-ATPase and thus it retains an enzyme which is probably close to the original one. The parasites Leishmania and Trypanosoma have ATPases phylogenetically related to fungal K+-ATPases, which are probably functional homologues of the fungal enzymes.
引用
收藏
页码:933 / 941
页数:9
相关论文
共 63 条
[52]   The Arabidopsis thaliana salt tolerance gene SOS1 encodes a putative Na+/H+ antiporter [J].
Shi, HZ ;
Ishitani, M ;
Kim, CS ;
Zhu, JK .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (12) :6896-6901
[53]   ORIGIN AND DIVERSIFICATION OF ENDOMYCORRHIZAL FUNGI AND COINCIDENCE WITH VASCULAR LAND PLANTS [J].
SIMON, L ;
BOUSQUET, J ;
LEVESQUE, RC ;
LALONDE, M .
NATURE, 1993, 363 (6424) :67-69
[56]   THE SODIUM-PUMP IN THE EVOLUTION OF ANIMAL-CELLS [J].
STEIN, WD .
PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY OF LONDON SERIES B-BIOLOGICAL SCIENCES, 1995, 349 (1329) :263-269
[57]   Na+ translocation by bacterial NADH:quinone oxidoreductases:: an extension to the complex-I family of primary redox pumps [J].
Steuber, J .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 2001, 1505 (01) :45-56
[58]   Involvement of Nha1 antiporter in regulation of intracellular pH in Saccharomyces cerevisiae [J].
Sychrová, H ;
Ramírez, J ;
Peña, A .
FEMS MICROBIOLOGY LETTERS, 1999, 171 (02) :167-172
[59]   ALLOMYCES IN THE DEVONIAN [J].
TAYLOR, TN ;
REMY, W ;
HASS, H .
NATURE, 1994, 367 (6464) :601-601
[60]   The oldest fossil ascomycetes [J].
Taylor, TN ;
Hass, T ;
Kerp, H .
NATURE, 1999, 399 (6737) :648-648