Characterization of a Listeria monocytogenes Ca(2+) pump : a SERCA-type ATPase with only one Ca(2+)-binding site
(2011) In Journal of Biological Chemistry 286(2). p.17-1609- Abstract
We have characterized a putative Ca(2+)-ATPase from the pathogenic bacterium Listeria monocytogenes with the locus tag lmo0841. The purified and detergent-solubilized protein, which we have named Listeria monocytogenes Ca(2+)-ATPase 1 (LMCA1), performs a Ca(2+)-dependent ATP hydrolysis and actively transports Ca(2+) after reconstitution in dioleoylphosphatidyl-choline vesicles. Despite a high sequence similarity to the sarcoplasmic reticulum Ca(2+)-ATPase (SERCA1a) and plasma membrane Ca(2+)-ATPase (PMCA), LMCA1 exhibits important biochemical differences such as a low Ca(2+) affinity (K(0.5) ∼80 μm) and a high pH optimum (pH ∼9). Mutational studies indicate that the unusually high pH optimum can be partially ascribed to the presence of... (More)
We have characterized a putative Ca(2+)-ATPase from the pathogenic bacterium Listeria monocytogenes with the locus tag lmo0841. The purified and detergent-solubilized protein, which we have named Listeria monocytogenes Ca(2+)-ATPase 1 (LMCA1), performs a Ca(2+)-dependent ATP hydrolysis and actively transports Ca(2+) after reconstitution in dioleoylphosphatidyl-choline vesicles. Despite a high sequence similarity to the sarcoplasmic reticulum Ca(2+)-ATPase (SERCA1a) and plasma membrane Ca(2+)-ATPase (PMCA), LMCA1 exhibits important biochemical differences such as a low Ca(2+) affinity (K(0.5) ∼80 μm) and a high pH optimum (pH ∼9). Mutational studies indicate that the unusually high pH optimum can be partially ascribed to the presence of an arginine residue (Arg-795), corresponding in sequence alignments to the Glu-908 position at Ca(2+) binding site I of rabbit SERCA1a, but probably with an exposed position in LMCA1. The arginine is characteristic of a large group of putative bacterial Ca(2+)-ATPases. Moreover, we demonstrate that H(+) is countertransported with a transport stoichiometry of 1 Ca(2+) out and 1 H(+) in per ATP hydrolyzed. The ATPase may serve an important function by removing Ca(2+) from the microorganism in environmental conditions when e.g. stressed by high Ca(2+) and alkaline pH.
(Less)
- author
- Faxén, Kristina ; Andersen, Jacob Lauwring ; Gourdon, Pontus LU ; Fedosova, Natalya ; Morth, Jens Preben ; Nissen, Poul and Møller, Jesper Vuust
- publishing date
- 2011-01-14
- type
- Contribution to journal
- publication status
- published
- keywords
- Adenosine Triphosphate, Alkalies, Amino Acid Sequence, Animals, Binding Sites, Biological Transport, Active, Calcium, Electrochemical Techniques, Hydrogen-Ion Concentration, Listeria monocytogenes, Molecular Sequence Data, Muscle, Skeletal, Protein Structure, Tertiary, Rabbits, Sarcoplasmic Reticulum Calcium-Transporting ATPases, Journal Article, Research Support, Non-U.S. Gov't
- in
- Journal of Biological Chemistry
- volume
- 286
- issue
- 2
- pages
- 17 - 1609
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:21047776
- scopus:78651394444
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.M110.176784
- language
- English
- LU publication?
- no
- id
- 4a6564be-279d-4d66-8502-b967dba89ebf
- date added to LUP
- 2017-04-29 15:31:54
- date last changed
- 2024-04-14 09:34:00
@article{4a6564be-279d-4d66-8502-b967dba89ebf,
abstract = {{<p>We have characterized a putative Ca(2+)-ATPase from the pathogenic bacterium Listeria monocytogenes with the locus tag lmo0841. The purified and detergent-solubilized protein, which we have named Listeria monocytogenes Ca(2+)-ATPase 1 (LMCA1), performs a Ca(2+)-dependent ATP hydrolysis and actively transports Ca(2+) after reconstitution in dioleoylphosphatidyl-choline vesicles. Despite a high sequence similarity to the sarcoplasmic reticulum Ca(2+)-ATPase (SERCA1a) and plasma membrane Ca(2+)-ATPase (PMCA), LMCA1 exhibits important biochemical differences such as a low Ca(2+) affinity (K(0.5) ∼80 μm) and a high pH optimum (pH ∼9). Mutational studies indicate that the unusually high pH optimum can be partially ascribed to the presence of an arginine residue (Arg-795), corresponding in sequence alignments to the Glu-908 position at Ca(2+) binding site I of rabbit SERCA1a, but probably with an exposed position in LMCA1. The arginine is characteristic of a large group of putative bacterial Ca(2+)-ATPases. Moreover, we demonstrate that H(+) is countertransported with a transport stoichiometry of 1 Ca(2+) out and 1 H(+) in per ATP hydrolyzed. The ATPase may serve an important function by removing Ca(2+) from the microorganism in environmental conditions when e.g. stressed by high Ca(2+) and alkaline pH.</p>}},
author = {{Faxén, Kristina and Andersen, Jacob Lauwring and Gourdon, Pontus and Fedosova, Natalya and Morth, Jens Preben and Nissen, Poul and Møller, Jesper Vuust}},
issn = {{1083-351X}},
keywords = {{Adenosine Triphosphate; Alkalies; Amino Acid Sequence; Animals; Binding Sites; Biological Transport, Active; Calcium; Electrochemical Techniques; Hydrogen-Ion Concentration; Listeria monocytogenes; Molecular Sequence Data; Muscle, Skeletal; Protein Structure, Tertiary; Rabbits; Sarcoplasmic Reticulum Calcium-Transporting ATPases; Journal Article; Research Support, Non-U.S. Gov't}},
language = {{eng}},
month = {{01}},
number = {{2}},
pages = {{17--1609}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{Characterization of a Listeria monocytogenes Ca(2+) pump : a SERCA-type ATPase with only one Ca(2+)-binding site}},
url = {{http://dx.doi.org/10.1074/jbc.M110.176784}},
doi = {{10.1074/jbc.M110.176784}},
volume = {{286}},
year = {{2011}},
}