Cadaverine covalently linked to the peptidoglycan serves as the correct constituent for the anchoring mechanism between the outer membrane and peptidoglycan in Selenomonas ruminantium

Seiji Kojima, Jun Kaneko, Naoki Abe, Yumiko Takatsuka, Yoshiyuki Kamio

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)

Abstract

In Selenomonas ruminantium, a strictly anaerobic and Gram-negative bacterium, cadaverine covalently linked to the peptidoglycan is required for the interaction between the peptidoglycan and the S-layer homologous (SLH) domain of the major outer membrane protein Mep45. Here, using a series of diamines with a general structure of NH3+(CH2)nNH3+ (n = 3 to 6), we found that cadaverine (n = 5) specifically serves as the most efficient constituent of the peptidoglycan in acquiring the high resistance of the cell to external damage agents and is required for effective interaction between the SLH domain of Mep45 and the peptidoglycan, facilitating the correct anchoring of the outer membrane to the peptidoglycan.

Original languageEnglish
Pages (from-to)2347-2350
Number of pages4
JournalJournal of bacteriology
Volume193
Issue number9
DOIs
Publication statusPublished - 2011 May

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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