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CtpB is a plasma membrane copper (I) transporting P-type ATPase of Mycobacterium tuberculosis
by
Soto, Carlos Y.
, Castillo, Eliana
, León-Torres, Andrés
, Arango, Epifania
in
Adenosine triphosphatase
/ Amino acids
/ ATPases
/ BCG
/ Binding sites
/ BIOLOGY
/ Biomedical and Life Sciences
/ Cations
/ Cell Biology
/ Cell culture
/ Cell Membrane - metabolism
/ Cell membranes
/ Copper
/ Copper transport
/ Copper-Transporting ATPases - metabolism
/ CtpB
/ Detoxification
/ Developmental Biology
/ Enzymes
/ Genes
/ Homeostasis
/ Hypoxia
/ Infections
/ Life Sciences
/ Macrophages
/ Membranes
/ Metal ions
/ Metals
/ Microbiology
/ Mutants
/ Mycobacterium tuberculosis
/ Mycobacterium tuberculosis - chemistry
/ Mycobacterium tuberculosis - metabolism
/ Neurosciences
/ Nickel
/ Nickel (Metal)
/ Oxidative stress
/ P-type ATPase
/ Pathogens
/ Phosphorylation
/ Plant Sciences
/ Plasma membrane
/ Proteins
/ Research Article
/ Transcription
/ Transcription (Genetics)
/ Tuberculosis
2020
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CtpB is a plasma membrane copper (I) transporting P-type ATPase of Mycobacterium tuberculosis
by
Soto, Carlos Y.
, Castillo, Eliana
, León-Torres, Andrés
, Arango, Epifania
in
Adenosine triphosphatase
/ Amino acids
/ ATPases
/ BCG
/ Binding sites
/ BIOLOGY
/ Biomedical and Life Sciences
/ Cations
/ Cell Biology
/ Cell culture
/ Cell Membrane - metabolism
/ Cell membranes
/ Copper
/ Copper transport
/ Copper-Transporting ATPases - metabolism
/ CtpB
/ Detoxification
/ Developmental Biology
/ Enzymes
/ Genes
/ Homeostasis
/ Hypoxia
/ Infections
/ Life Sciences
/ Macrophages
/ Membranes
/ Metal ions
/ Metals
/ Microbiology
/ Mutants
/ Mycobacterium tuberculosis
/ Mycobacterium tuberculosis - chemistry
/ Mycobacterium tuberculosis - metabolism
/ Neurosciences
/ Nickel
/ Nickel (Metal)
/ Oxidative stress
/ P-type ATPase
/ Pathogens
/ Phosphorylation
/ Plant Sciences
/ Plasma membrane
/ Proteins
/ Research Article
/ Transcription
/ Transcription (Genetics)
/ Tuberculosis
2020
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CtpB is a plasma membrane copper (I) transporting P-type ATPase of Mycobacterium tuberculosis
by
Soto, Carlos Y.
, Castillo, Eliana
, León-Torres, Andrés
, Arango, Epifania
in
Adenosine triphosphatase
/ Amino acids
/ ATPases
/ BCG
/ Binding sites
/ BIOLOGY
/ Biomedical and Life Sciences
/ Cations
/ Cell Biology
/ Cell culture
/ Cell Membrane - metabolism
/ Cell membranes
/ Copper
/ Copper transport
/ Copper-Transporting ATPases - metabolism
/ CtpB
/ Detoxification
/ Developmental Biology
/ Enzymes
/ Genes
/ Homeostasis
/ Hypoxia
/ Infections
/ Life Sciences
/ Macrophages
/ Membranes
/ Metal ions
/ Metals
/ Microbiology
/ Mutants
/ Mycobacterium tuberculosis
/ Mycobacterium tuberculosis - chemistry
/ Mycobacterium tuberculosis - metabolism
/ Neurosciences
/ Nickel
/ Nickel (Metal)
/ Oxidative stress
/ P-type ATPase
/ Pathogens
/ Phosphorylation
/ Plant Sciences
/ Plasma membrane
/ Proteins
/ Research Article
/ Transcription
/ Transcription (Genetics)
/ Tuberculosis
2020
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CtpB is a plasma membrane copper (I) transporting P-type ATPase of Mycobacterium tuberculosis
Journal Article
CtpB is a plasma membrane copper (I) transporting P-type ATPase of Mycobacterium tuberculosis
2020
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Overview
Background
The intracellular concentration of heavy-metal cations, such as copper, nickel, and zinc is pivotal for the mycobacterial response to the hostile environment inside macrophages. To date, copper transport mediated by P-type ATPases across the mycobacterial plasma membrane has not been sufficiently explored.
Results
In this work, the ATPase activity of the putative
Mycobacterium tuberculosis
P
1B
-type ATPase CtpB was associated with copper (I) transport from mycobacterial cells. Although CtpB heterologously expressed in
M. smegmatis
induced tolerance to toxic concentrations of Cu
2+
and a metal preference for Cu
+
, the disruption of
ctpB
in
M. tuberculosis
cells did not promote impaired cell growth or heavy-metal accumulation in whole mutant cells in cultures under high doses of copper. In addition, the Cu
+
ATPase activity of CtpB embedded in the plasma membrane showed features of high affinity/slow turnover ATPases, with enzymatic parameters
K
M
0.19 ± 0.04 µM and
V
max
2.29 ± 0.10 nmol/mg min. In contrast, the
ctpB
gene transcription was activated in cells under culture conditions that mimicked the hostile intraphagosomal environment, such as hypoxia, nitrosative and oxidative stress, but not under high doses of copper.
Conclusions
The overall results suggest that
M. tuberculosis
CtpB is associated with Cu
+
transport from mycobacterial cells possibly playing a role different from copper detoxification.
Publisher
BioMed Central,BioMed Central Ltd,Springer Nature B.V,Sociedad de Biología de Chile,BMC
Subject
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