Dynamic interactions of CbiN and CbiM trigger activity of a cobalt energy-coupling-factor transporter

Finkenwirth, Friedrich; Sippach, Michael; Pecina, Sinah N.; Gäde, Mario; Ruta, Julia; Ricke, Adrian; Bondarenko, Elena; Klare, Johann P.; Zinke, Maximilian; Lange, Adam; Steinhoff, Heinz‐Jürgen; Eitinger, Thomas

doi:10.1016/j.bbamem.2019.183114

Cited by 6 publications

(3 citation statements)

References 59 publications

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“…CbiN has a short flexible extracytoplasmic loop between its two transmembrane helices that lies on top of the metal binding pocket of CbiM. It has been shown that truncations or modifications to this loop severely impair cobalt transport though the mechanism behind their interactions is still not well understood [ 67 ]. It is understood that CbiM provides ATPase activity to the complex without the presence of CbiN, and that CbiO units undergo ATP binding and product release-induced conformational change, but the full transport cycle is yet to be elucidated [ 65 ].…”

Section: The Components Of Cobalt Homeostasismentioning

confidence: 99%

The requirement for cobalt in vitamin B12: A paradigm for protein metalation

Osman

Cooke

Young

et al. 2021

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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Vitamin B 12 , cobalamin, is a cobalt-containing ring-contracted modified tetrapyrrole that represents one of the most complex small molecules made by nature. In prokaryotes it is utilised as a cofactor, coenzyme, light sensor and gene regulator yet has a restricted role in assisting only two enzymes within specific eukaryotes including mammals. This deployment disparity is reflected in another unique attribute of vitamin B 12 in that its biosynthesis is limited to only certain prokaryotes, with synthesisers pivotal in establishing mutualistic microbial communities. The core component of cobalamin is the corrin macrocycle that acts as the main ligand for the cobalt. Within this review we investigate why cobalt is paired specifically with the corrin ring, how cobalt is inserted during the biosynthetic process, how cobalt is made available within the cell and explore the cellular control of cobalt and cobalamin levels. The partitioning of cobalt for cobalamin biosynthesis exemplifies how cells assist metalation.

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Section: The Components Of Cobalt Homeostasismentioning

confidence: 99%

The requirement for cobalt in vitamin B12: A paradigm for protein metalation

Osman

Cooke

Young

et al. 2021

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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“… 2006 ; Finkenwirth et al . 2020 ). The final mode of uptake falls to nonspecific divalent metal permeases, which have been shown to transport cobalt with relatively lower affinities, such as CorA (see Mg section) (Guskov and Eshaghi 2012 ), ZupT (see Zn section) (Grass et al .…”

Section: Introductionmentioning

confidence: 99%

An overview ofSalmonella entericametal homeostasis pathways during infection

Cunrath

Palmer

2021

microLife

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Nutritional immunity is a powerful strategy at the core of the battlefield between host survival and pathogen proliferation. A host can prevent pathogens from accessing biological metals such as Mg, Fe, Zn, Mn, Cu, Co or Ni, or actively intoxicate them with metal overload. While the importance of metal homeostasis for the enteric pathogen Salmonella enterica Typhimurium was demonstrated many decades ago, inconsistent results across various mouse models, diverse Salmonella genotypes, and differing infection routes challenge aspects of our understanding of this phenomenon. With expanding access to CRISPR-Cas9 for host genome manipulation, it is now pertinent to re-visit past results in the context of specific mouse models, identify gaps and incongruities in current knowledge landscape of Salmonella homeostasis, and recommend a straight path forward towards a more universal understanding of this historic host-microbe relationship.

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“…Pathogenic bacteria display nutrient deprivation strategies to obtain dietary elements essential for growth, such as metal ions, amino acids, vitamins, and oligopeptides, and respond to hardship by releasing stress proteins and via immune evasion mechanisms. Several ABC-type transporters are involved in virulence, playing a role in bacterial propagation during infection [72][73][74][75]. The LC-ESI-MS/MS analyses carried out in Streptococcus spp.…”

Section: Transporters Associated To Virulence Factorsmentioning

confidence: 99%

Proteomic Characterization of Antibiotic Resistance, and Production of Antimicrobial and Virulence Factors in Streptococcus Species Associated with Bovine Mastitis. Could Enzybiotics Represent Novel Therapeutic Agents Against These Pathogens?

Abril

Carrera

Böhme³

et al. 2020

Antibiotics

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Streptococcus spp. are major mastitis pathogens present in dairy products, which produce a variety of virulence factors that are involved in streptococcal pathogenicity. These include neuraminidase, pyrogenic exotoxin, and M protein, and in addition they might produce bacteriocins and antibiotic-resistance proteins. Unjustifiable misuse of antimicrobials has led to an increase in antibiotic-resistant bacteria present in foodstuffs. Identification of the mastitis-causing bacterial strain, as well as determining its antibiotic resistance and sensitivity is crucial for effective therapy. The present work focused on the LC–ESI–MS/MS (liquid chromatography–electrospray ionization tandem mass spectrometry) analysis of tryptic digestion peptides from mastitis-causing Streptococcus spp. isolated from milk. A total of 2706 non-redundant peptides belonging to 2510 proteins was identified and analyzed. Among them, 168 peptides were determined, representing proteins that act as virulence factors, toxins, anti-toxins, provide resistance to antibiotics that are associated with the production of lantibiotic-related compounds, or play a role in the resistance to toxic substances. Protein comparisons with the NCBI database allowed the identification of 134 peptides as specific to Streptococcus spp., while two peptides (EATGNQNISPNLTISNAQLNLEDKNK and DLWC*NM*IIAAK) were found to be species-specific to Streptococcus dysgalactiae. This proteomic repository might be useful for further studies and research work, as well as for the development of new therapeutics for the mastitis-causing Streptococcus strains.

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Dynamic interactions of CbiN and CbiM trigger activity of a cobalt energy-coupling-factor transporter

Cited by 6 publications

References 59 publications

The requirement for cobalt in vitamin B12: A paradigm for protein metalation

The requirement for cobalt in vitamin B12: A paradigm for protein metalation

An overview ofSalmonella entericametal homeostasis pathways during infection

Proteomic Characterization of Antibiotic Resistance, and Production of Antimicrobial and Virulence Factors in Streptococcus Species Associated with Bovine Mastitis. Could Enzybiotics Represent Novel Therapeutic Agents Against These Pathogens?

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