Novel pore-forming colicin FY identified in the genus Yersinia

BOSÁK, Juraj, Radovan FIŠER, Ivo KONOPÁSEK a David ŠMAJS. Novel pore-forming colicin FY identified in the genus Yersinia. In How bugs kill bugs: progress and challenges in bacteriocin research. 2012.

Základní údaje

Originální název

Novel pore-forming colicin FY identified in the genus Yersinia

Autoři

BOSÁK, Juraj, Radovan FIŠER, Ivo KONOPÁSEK a David ŠMAJS

Vydání

How bugs kill bugs: progress and challenges in bacteriocin research, 2012

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Další údaje

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Obor

10600 1.6 Biological sciences

Utajení

není předmětem státního či obchodního tajemství

Organizační jednotka

Lékařská fakulta

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Anotace

V originále

In the set of yersinia strains, a novel bacteriocin, produced by Y. frederiksenii 27601, was identified. Its activity spectrum comprises strains of the genus Yersinia, especially strains of Y. enterocolitica. The colicinogenic plasmid pYF27601 (5574 bp) was sequenced and two colicin genes were identified: the colicin FY activity gene (cfyA) and the immunity gene (cfyI). The deduced amino acid sequence of immunity protein and C-terminal sequence of colicin FY revealed high similarity to immunity protein and pore-forming domain of colicin Ib. Colicin FY (54 kDa) was purified and was shown to form a distinct voltage-dependent pore, which is activated by Ca2+ ions. Transposon mutagenesis of susceptible strain Y. kristensenii Y276 revealed the yiuR gene (ykris001_4440) encoding outer membrane protein with siderophore binding function as the colicin FY receptor molecule. Cloning of the gene yiuR to resistant strain Y. kristensenii Y104 resulted in sensitivity to colicin FY. YiuR is similar to Cir protein of Escherichia coli, which is a receptor for colicin Ib. Naturally FY-resistant strains of E. coli acquired susceptibility to colicin FY, when genes yiuR and tonB from the FY-sensitive Y. kristensenii Y276 were introduced. Colicin FY thus belongs to colicin-group B, a group using TonB, ExbB and ExbD proteins to translocate through the bacterial envelope.