N-linked glycans confer protein stability and modulate multidrug efflux pump assembly in Campylobacter jejuni
It is now apparent that nearly all bacteria species have at least a single glycosylation system, but the direct effect(s) of these protein post translational modifications are unresolved. In this study, we used the general N-linked glycosylation pathway from Campylobacter jejuni to investigate the biophysical roles of protein modification on the CmeABC multidrug efflux pump complex. The study reveals the multifunctional role of N-linked glycans in enhancing protein thermostability, stabilising protein complexes and the promotion of protein-protein interaction. Our findings demonstrate, for the first time, that regardless of glycan diversification among domains of life, N-linked glycans confer a common evolutionary intrinsic role.
biochemistry↗