A thermostable K+-stimulated vacuolar-type pyrophosphatase from the hyperthermophilic bacterium Thermotoga maritima

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A thermostable K+-stimulated vacuolar-type pyrophosphatase from the hyperthermophilic bacterium Thermotoga maritima. / Pérez-Castiñeira, José R.; López-Marqués, Rosa L.; Losada, Manuel; Serrano, Aurelio.

In: FEBS Letters, Vol. 496, No. 1, 04.05.2001, p. 6-11.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Pérez-Castiñeira, JR, López-Marqués, RL, Losada, M & Serrano, A 2001, 'A thermostable K+-stimulated vacuolar-type pyrophosphatase from the hyperthermophilic bacterium Thermotoga maritima', FEBS Letters, vol. 496, no. 1, pp. 6-11. https://doi.org/10.1016/S0014-5793(01)02390-0

APA

Pérez-Castiñeira, J. R., López-Marqués, R. L., Losada, M., & Serrano, A. (2001). A thermostable K+-stimulated vacuolar-type pyrophosphatase from the hyperthermophilic bacterium Thermotoga maritima. FEBS Letters, 496(1), 6-11. https://doi.org/10.1016/S0014-5793(01)02390-0

Vancouver

Pérez-Castiñeira JR, López-Marqués RL, Losada M, Serrano A. A thermostable K+-stimulated vacuolar-type pyrophosphatase from the hyperthermophilic bacterium Thermotoga maritima. FEBS Letters. 2001 May 4;496(1):6-11. https://doi.org/10.1016/S0014-5793(01)02390-0

Author

Pérez-Castiñeira, José R. ; López-Marqués, Rosa L. ; Losada, Manuel ; Serrano, Aurelio. / A thermostable K+-stimulated vacuolar-type pyrophosphatase from the hyperthermophilic bacterium Thermotoga maritima. In: FEBS Letters. 2001 ; Vol. 496, No. 1. pp. 6-11.

Bibtex

@article{4d185d0e8d084d53ba97f10075ac599a,
title = "A thermostable K+-stimulated vacuolar-type pyrophosphatase from the hyperthermophilic bacterium Thermotoga maritima",
abstract = "Current evidence suggests the occurrence of two classes of vacuolar-type H+-translocating inorganic pyrophosphatases (V-PPases): K+-insensitive proteins, identified in eukaryotes, bacteria and archaea, and K+-stimulated V-PPases, identified to date only in eukaryotes. Here, we describe the functional characterization of a thermostable V-PPase from the anaerobic hyperthermophilic bacterium Thermotoga maritima by heterologous expression in Saccharomyces cerevisiae. The activity of this 71-kDa membrane-embedded polypeptide has a near obligate requirement for K+, like the plant V-PPase, and its thermostability depends on the binding of Mg2+. Phylogenetic analysis of protein sequences consistently assigned the T. maritima V-PPase to the K+-sensitive class of V-PPases so far only known for eukaryotes. The finding of a K+-stimulated V-PPase also in a member of a primitive eubacterial lineage strongly supports an ancient evolutionary origin of this group of pyrophosphate-energized proton pumps.",
keywords = "Heterologous expression, K-stimulation, Saccharomyces cerevisiae, Thermotoga maritima, Vacuolar-type H-pyrophosphatase",
author = "P{\'e}rez-Casti{\~n}eira, {Jos{\'e} R.} and L{\'o}pez-Marqu{\'e}s, {Rosa L.} and Manuel Losada and Aurelio Serrano",
note = "Funding Information: Preliminary genome sequence data were obtained from TIGR and JGI websites http://tigr.org and http://spider.jgi-psf.org/JGI_microbial/html/ , respectively. We gratefully thank Prof. R. Serrano for providing yeast strains and plasmids. We are also indebted to Prof. P.A. Rea for the generous gift of antibody PAB HK and to Prof. M. Baltcheffsky for providing the RVP gene and antibody against the protein. T. maritima genomic DNA was obtained from Dr. C. Bouthier de la Tour, which is also gratefully acknowledged. J.R. P.-C. and R.L. L.-M. were supported by a postdoctoral contract from the Spanish Research Council (CSIC) and by a Ph.D. studentship from MEC-CSIC, respectively. This work was supported by DGICYT Grant PB97-1135 from the Spanish Government and Grant PAI CVI-261 from the Andalusian Regional Government (Spain).",
year = "2001",
month = may,
day = "4",
doi = "10.1016/S0014-5793(01)02390-0",
language = "English",
volume = "496",
pages = "6--11",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "1",

}

RIS

TY - JOUR

T1 - A thermostable K+-stimulated vacuolar-type pyrophosphatase from the hyperthermophilic bacterium Thermotoga maritima

AU - Pérez-Castiñeira, José R.

AU - López-Marqués, Rosa L.

AU - Losada, Manuel

AU - Serrano, Aurelio

N1 - Funding Information: Preliminary genome sequence data were obtained from TIGR and JGI websites http://tigr.org and http://spider.jgi-psf.org/JGI_microbial/html/ , respectively. We gratefully thank Prof. R. Serrano for providing yeast strains and plasmids. We are also indebted to Prof. P.A. Rea for the generous gift of antibody PAB HK and to Prof. M. Baltcheffsky for providing the RVP gene and antibody against the protein. T. maritima genomic DNA was obtained from Dr. C. Bouthier de la Tour, which is also gratefully acknowledged. J.R. P.-C. and R.L. L.-M. were supported by a postdoctoral contract from the Spanish Research Council (CSIC) and by a Ph.D. studentship from MEC-CSIC, respectively. This work was supported by DGICYT Grant PB97-1135 from the Spanish Government and Grant PAI CVI-261 from the Andalusian Regional Government (Spain).

PY - 2001/5/4

Y1 - 2001/5/4

N2 - Current evidence suggests the occurrence of two classes of vacuolar-type H+-translocating inorganic pyrophosphatases (V-PPases): K+-insensitive proteins, identified in eukaryotes, bacteria and archaea, and K+-stimulated V-PPases, identified to date only in eukaryotes. Here, we describe the functional characterization of a thermostable V-PPase from the anaerobic hyperthermophilic bacterium Thermotoga maritima by heterologous expression in Saccharomyces cerevisiae. The activity of this 71-kDa membrane-embedded polypeptide has a near obligate requirement for K+, like the plant V-PPase, and its thermostability depends on the binding of Mg2+. Phylogenetic analysis of protein sequences consistently assigned the T. maritima V-PPase to the K+-sensitive class of V-PPases so far only known for eukaryotes. The finding of a K+-stimulated V-PPase also in a member of a primitive eubacterial lineage strongly supports an ancient evolutionary origin of this group of pyrophosphate-energized proton pumps.

AB - Current evidence suggests the occurrence of two classes of vacuolar-type H+-translocating inorganic pyrophosphatases (V-PPases): K+-insensitive proteins, identified in eukaryotes, bacteria and archaea, and K+-stimulated V-PPases, identified to date only in eukaryotes. Here, we describe the functional characterization of a thermostable V-PPase from the anaerobic hyperthermophilic bacterium Thermotoga maritima by heterologous expression in Saccharomyces cerevisiae. The activity of this 71-kDa membrane-embedded polypeptide has a near obligate requirement for K+, like the plant V-PPase, and its thermostability depends on the binding of Mg2+. Phylogenetic analysis of protein sequences consistently assigned the T. maritima V-PPase to the K+-sensitive class of V-PPases so far only known for eukaryotes. The finding of a K+-stimulated V-PPase also in a member of a primitive eubacterial lineage strongly supports an ancient evolutionary origin of this group of pyrophosphate-energized proton pumps.

KW - Heterologous expression

KW - K-stimulation

KW - Saccharomyces cerevisiae

KW - Thermotoga maritima

KW - Vacuolar-type H-pyrophosphatase

UR - http://www.scopus.com/inward/record.url?scp=0035805112&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(01)02390-0

DO - 10.1016/S0014-5793(01)02390-0

M3 - Journal article

C2 - 11343697

AN - SCOPUS:0035805112

VL - 496

SP - 6

EP - 11

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 1

ER -

ID: 272654340