Metal Response in Cupriavidus metallidurans

Vandenbussche, Guy; Mergeay, Max

doi:10.1007/978-3-319-20624-0

SpringerBriefs in Molecular Science

2015

DOI: 10.1007/978-3-319-20624-0

|View full text |Cite

Metal Response in Cupriavidus metallidurans

Guy Vandenbussche

Max Mergeay

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

2016

2021

Publication Types

Select...

Article5

Relationship

Self Cite1

Independent4

Authors

Journals

Cited by 5 publications

References 243 publications

(605 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

Structural and Functional Investigation of the Ag⁺/Cu⁺ Binding Domains of the Periplasmic Adaptor Protein SilB from Cupriavidus metallidurans CH34

et al. 2016

Self Cite

View full text Add to dashboard Cite

Silver ion resistance in bacteria mainly relies on efflux systems, and notably on tripartite efflux complexes involving a transporter from the resistance-nodulation-cell division (RND) superfamily, such as the SilCBA system from Cupriavidus metallidurans CH34. The periplasmic adaptor protein SilB hosts two specific metal coordination sites, located in the N-terminal and C-terminal domains, respectively, that are believed to play a different role in the efflux mechanism and the trafficking of metal ions from the periplasm to the RND transporter. On the basis of the known domain structure of periplasmic adaptor proteins, we designed different protein constructs derived from SilB domains with either one or two metal binding sites per protein chain. ITC data acquired on proteins with single metal sites suggest a slightly higher affinity of Ag(+) for the N-terminal metal site, compared to that for the C-terminal one. Remarkably, via the study of a protein construct featuring both metal sites, nuclear magnetic resonance (NMR) and fluorescence spectroscopies concordantly show that the C-terminal site is saturated prior to the N-terminal one. The C-terminal binding site is supposed to transfer the metal ions to the RND protein, while the transport driven by this latter is activated upon binding of the metal ion to the N-terminal site. Our results suggest that the filling of the C-terminal metal site is a key prerequisite for preventing futile activation of the transport system. Exhaustive NMR studies reveal for the first time the structure and dynamics of the functionally important N-terminal domain connected to the membrane proximal domain as well as of its Ag(+) binding site.

show abstract

Structural and Functional Investigation of the Ag⁺/Cu⁺ Binding Domains of the Periplasmic Adaptor Protein SilB from Cupriavidus metallidurans CH34

et al. 2016

Self Cite

View full text Add to dashboard Cite

show abstract

Cupriavidus metallidurans CH34, a historical perspective on its discovery, characterization and metal resistance

Mergeay

2020

FEMS Microbiology Ecology

View full text Add to dashboard Cite

Cupriavidus metallidurans, and in particular type strain CH34, became a model bacterium to study bacterial resistance to metals. Although nowadays the routine use of a wide variety of omics and molecular techniques allow refining, deepening and expanding our knowledge on adaptation and resistance to metals, these were not available at the onset of C. metallidurans research starting from its isolation in 1976. This minireview describes the early research and legacy tools used to study its metal resistance determinants, characteristic megaplasmids, ecological niches and environmental applications.

show abstract

Cupriavidus metallidurans Strains with Different Mobilomes and from Distinct Environments Have Comparable Phenomes

Provoost

Assche

Leys

et al. 2018

Genes

View full text Add to dashboard Cite

Cupriavidus metallidurans has been mostly studied because of its resistance to numerous heavy metals and is increasingly being recovered from other environments not typified by metal contamination. They host a large and diverse mobile gene pool, next to their native megaplasmids. Here, we used comparative genomics and global metabolic comparison to assess the impact of the mobilome on growth capabilities, nutrient utilization, and sensitivity to chemicals of type strain CH34 and three isolates (NA1, NA4 and H1130). The latter were isolated from water sources aboard the International Space Station (NA1 and NA4) and from an invasive human infection (H1130). The mobilome was expanded as prophages were predicted in NA4 and H1130, and a genomic island putatively involved in abietane diterpenoids metabolism was identified in H1130. An active CRISPR-Cas system was identified in strain NA4, providing immunity to a plasmid that integrated in CH34 and NA1. No correlation between the mobilome and isolation environment was found. In addition, our comparison indicated that the metal resistance determinants and properties are conserved among these strains and thus maintained in these environments. Furthermore, all strains were highly resistant to a wide variety of chemicals, much broader than metals. Only minor differences were observed in the phenomes (measured by phenotype microarrays), despite the large difference in mobilomes and the variable (shared by two or three strains) and strain-specific genomes.

show abstract

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

customersupport@researchsolutions.com

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Metal Response in Cupriavidus metallidurans

Cited by 5 publications

References 243 publications

Structural and Functional Investigation of the Ag⁺/Cu⁺ Binding Domains of the Periplasmic Adaptor Protein SilB from Cupriavidus metallidurans CH34

Structural and Functional Investigation of the Ag⁺/Cu⁺ Binding Domains of the Periplasmic Adaptor Protein SilB from Cupriavidus metallidurans CH34

Cupriavidus metallidurans CH34, a historical perspective on its discovery, characterization and metal resistance

Cupriavidus metallidurans Strains with Different Mobilomes and from Distinct Environments Have Comparable Phenomes

Contact Info

Product

Resources

About

Metal Response in Cupriavidus metallidurans

Cited by 5 publications

References 243 publications

Structural and Functional Investigation of the Ag+/Cu+ Binding Domains of the Periplasmic Adaptor Protein SilB from Cupriavidus metallidurans CH34

Structural and Functional Investigation of the Ag+/Cu+ Binding Domains of the Periplasmic Adaptor Protein SilB from Cupriavidus metallidurans CH34

Cupriavidus metallidurans CH34, a historical perspective on its discovery, characterization and metal resistance

Cupriavidus metallidurans Strains with Different Mobilomes and from Distinct Environments Have Comparable Phenomes

Contact Info

Product

Resources

About

Structural and Functional Investigation of the Ag⁺/Cu⁺ Binding Domains of the Periplasmic Adaptor Protein SilB from Cupriavidus metallidurans CH34

Structural and Functional Investigation of the Ag⁺/Cu⁺ Binding Domains of the Periplasmic Adaptor Protein SilB from Cupriavidus metallidurans CH34