NDLI: Cd2+ extrusion by P-type Cd2+-ATPase of Staphylococcus aureus 17810R via energy-dependent Cd2+/H+ exchange mechanism

Content Provider	Springer Nature Link
Author	Tynecka, Zofia Malm, Anna Goś Szcześniak, Zofia
Copyright Year	2016
Abstract	Cd2+ is highly toxic to Staphylococcus aureus since it blocks dithiols in cytoplasmic 2-oxoglutarate dehydrogenase complex (ODHC) participating in energy conservation process. However, S. aureus 17810R is Cd2+-resistant due to possession of cadA-coded Cd2+ efflux system, recognized here as P-type Cd2+-ATPase. This Cd2+ pump utilizing cellular energy—ATP, ∆μ H + (electrochemical proton potential) and respiratory protons, extrudes Cd2+ from cytoplasm to protect dithiols in ODHC, but the mechanism of Cd2+ extrusion remains unknown. Here we propose that two Cd2+ taken up by strain 17810R via Mn2+ uniporter down membrane potential (∆ψ) generated during glutamate oxidation in 100 mM phosphate buffer (high PiB) are trapped probably by high affinity sites in cytoplasmic domain of Cd2+-ATPase, forming SCdS. This stops Cd2+ transport towards dithiols in ODHC, allowing undisturbed NADH production, its oxidation and energy conservation, while ATP could change orientation of SCdS towards facing transmembrane channel. Now, increased number of Pi-dependent protons pumped electrogenically via respiratory chain and countertransported through the channel down ∆ψ, extrude two trapped cytoplasmic Cd2+, which move to low affinity sites, being then extruded into extracellular space via ∆ψ-dependent Cd2+/H+ exchange. In 1 mM phosphate buffer (low PiB), external Cd2+ competing with decreased number of Pi-dependent protons, binds to ψs of Cd2+-ATPase channel, enters cytoplasm through the channel down ∆ψ via Cd2+/Cd2+ exchange and blocks dithiols in ODHC. However, Mg2+ pretreatment preventing external Cd2+ countertransport through the channel down ∆ψ, allowed undisturbed NADH production, its oxidation and extrusion of two cytoplasmic Cd2+ via Cd2+/H+ exchange, despite low PiB.
Starting Page	651
Ending Page	663
Page Count	13
File Format	PDF
ISSN	09660844
Journal	BioMetals
Volume Number	29
Issue Number	4
e-ISSN	15728773
Language	English
Publisher	Springer Netherlands
Publisher Date	2016-06-21
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Cd2+ resistance Cd2+-ATPase Energy dependent Cd2+/H+ exchange Staphylococcus aureus Biochemistry Pharmacology/Toxicology Microbiology Cell Biology Plant Physiology Medicine/Public Health
Content Type	Text
Resource Type	Article
Subject	Metals and Alloys Biochemistry, Genetics and Molecular Biology Biomaterials Agricultural and Biological Sciences

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Cd2+ extrusion by P-type Cd2+-ATPase of Staphylococcus aureus 17810R via energy-dependent Cd2+/H+ exchange mechanism

Mechanism of action of the tri-hybrid antimicrobial peptide LHP7 from lactoferricin, HP and plectasin on Staphylococcus aureus

Energetics of Cd2+ efflux system in cadmium-resistant Staphylococcus aureus 17810R.

Mutations in the ArsA ATPase that restore interaction with the ArsD metallochaperone

Exposure of Staphylococcus aureus to silver(I) induces a short term protective response

CtpA, a putative Mycobacterium tuberculosis P-type ATPase, is stimulated by copper (I) in the mycobacterial plasma membrane

The multi-layered regulation of copper translocating P-type ATPases

Iron Acquisition and Transport in Staphylococcus aureus

Antibacterial effect of silver nanoparticles on Staphylococcus aureus

Cd2+ extrusion by P-type Cd2+-ATPase of Staphylococcus aureus 17810R via energy-dependent Cd2+/H+ exchange mechanism

Similar Documents

Cd2+ extrusion by P-type Cd2+-ATPase of Staphylococcus aureus 17810R via energy-dependent Cd2+/H+ exchange mechanism

Mechanism of action of the tri-hybrid antimicrobial peptide LHP7 from lactoferricin, HP and plectasin on Staphylococcus aureus

Energetics of Cd2+ efflux system in cadmium-resistant Staphylococcus aureus 17810R.

Mutations in the ArsA ATPase that restore interaction with the ArsD metallochaperone

Exposure of Staphylococcus aureus to silver(I) induces a short term protective response

CtpA, a putative Mycobacterium tuberculosis P-type ATPase, is stimulated by copper (I) in the mycobacterial plasma membrane

The multi-layered regulation of copper translocating P-type ATPases

Iron Acquisition and Transport in Staphylococcus aureus

Antibacterial effect of silver nanoparticles on Staphylococcus aureus

Cd2+ extrusion by P-type Cd2+-ATPase of Staphylococcus aureus 17810R via energy-dependent Cd2+/H+ exchange mechanism