원문정보
초록
영어
The cell envelope of a gram-negative bacterium is unique from several respects, and it consists of a number of layers whose chemical compositions and physical natures differ markedly. In this study, it was found that the outer membrane of Selenomonas ruminantium subsp. lactilytica contained a major protein with an apparent molecular weight of 45 kDa by using SDS-PAGE. The outer membrane protein was purified and then its gene (Mep45) was cloned. The N-terminal region for Mep45 had a high identity with the S-layer protein of various prokaryotes. The homologous regions of the N-terminal and C-terminal correspond to a SLH (surface layer-like homologous) domain and a porin. The negatively charged amino acids are candidates for an interaction with a positively charged cadaverine for linking it to peptidoglycan in S. ruminantium. We propose that the Mep45 itself associates with the cadaverine in the peptidoglycan by an ionic interaction. We could hypothesize that cadaverine interacts with Mep45 and the outer membrane of a cell envelope in S. ruminantium.