作者: Sune Lobedanz , Lotte Søgaard-Andersen
DOI: 10.1101/GAD.274203
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摘要: The regulated accumulation of the contact-dependent extracellular C-signal morphogen in bacterium Myxococcus xanthus ensures temporal and spatial coordination multicellular morphogenesis cellular differentiation during fruiting bodyformation. Synthesis depends on csgA gene. CsgA protein exists two forms, full-length 25-kD (p25), which is homologous to short-chain alcohol dehydrogenases, a 17-kD (p17). molecular nature has remained elusive. Here we show that p25 p17 are associated with outer membrane copurifies activityfrom M. cells. corresponds C-terminal part p25. A recombinant protein, lacks N-terminal coenzyme binding pocket fails bind NAD+ vitro, activity. These data provide evidence active species C-signaling does not act as dehydrogenase generate C-signal. We further synthesized by proteolytic processing serine protease. Compared other bacterial signaling molecules, unusual respect size cell-surface association. In these regards, functionally analogous eukaryotic proteins.