Showing papers on "Polyamine binding published in 2018"
TL;DR: The three-dimensional structure of McpU-LBD in complex with putrescine is reported at a resolution of 2.4 Å, which fitted well a solution structure generated by small-angle X-ray scattering and enhances the understanding of CACHE domains, which are the most abundant sensor domains in bacterial chemoreceptors and sensor kinases.
26 citations
TL;DR: An approach employing quantitative western blot analyses that provides in vivo evidence for cotranslational polyamine-sensing by nascent OAZ in yeast is described and an in vitro method to detect polyamine binding by antizyme is described.
Abstract: Polyamines are essential poly-cations with vital functions in all cellular systems. Their levels are controlled by intricate regulatory feedback mechanisms. Abnormally high levels of polyamines have been linked to cancer. A rate-limiting enzyme in the biosynthesis of polyamines in fungi and higher eukaryotes is ornithine-decarboxylase (ODC). Its levels are largely controlled posttranslationally via ubiquitin-independent degradation mediated by ODC antizyme (OAZ). The latter is a critical polyamine sensor in a feedback control mechanism that adjusts cellular polyamine levels. Here, we describe an approach employing quantitative western blot analyses that provides in vivo evidence for cotranslational polyamine-sensing by nascent OAZ in yeast. In addition, we describe an in vitro method to detect polyamine binding by antizyme.
2 citations