Publications by authors named "Claus Schmitz"

Article Synopsis
  • The type IX secretion system (T9SS) helps bacterial pathogens infect hosts, and its activation is regulated by a signaling cascade, with PorX being a key protein that could be targeted for drug development.
  • Structural analysis shows that PorX has a unique enzyme domain similar to alkaline phosphatase, indicating its involvement in previously unlinked nucleotide and lipid signaling pathways.
  • PorX acts as a zinc sensor and is crucial for the secretion of virulence factors in pathogenic bacteria, suggesting it could be an effective target for strategies to disrupt T9SS and reduce virulence.
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Article Synopsis
  • The Type-IX secretion system (T9SS) is a bacterial nanomachinery critical for the infection process, regulated by a signaling cascade led by the protein PorX, making it a potential target for drugs.
  • Research on PorX revealed it has a unique enzymatic domain similar to alkaline phosphatases, indicating it plays a role in nucleotide and lipid signaling that was previously unrecognized in the context of T9SS.
  • PorX exhibits zinc-dependent phosphodiesterase activity and can dimerize through a novel mechanism involving zinc, suggesting it's a cellular zinc sensor and further emphasizing its importance in virulence factor secretion in pathogenic bacteria.
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The PglZ family of proteins belongs to the alkaline phosphatase superfamily, which consists of metallohydrolases with limited sequence identity but similar metal-coordination architectures in otherwise divergent active sites. Proteins with a well-defined PglZ domain are ubiquitous among prokaryotes as essential components of BREX phage defence systems and two-component systems (TCSs). Whereas other members of the alkaline phosphatase superfamily are well characterized, the activity, structure and biological function of PglZ family proteins remain unclear.

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The aminoacylation of tRNAs by aminoacyl-tRNA synthetases (ARSs) is a central reaction in biology. Multiple regulatory pathways use the aminoacylation status of cytosolic tRNAs to monitor and regulate metabolism. The existence of equivalent regulatory networks within the mitochondria is unknown.

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