AglB, catalyzing the oligosaccharyl transferase step of the archaeal N‐glycosylation process, is essential in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius

MicrobiologyOpen

Benjamin H. Meyer¹ 

[1] Molecular Biology of Archaea, Max-Planck Institute for terrestrial Microbiology, Marburg

关键词: AglB;    Archaea;    Crenarchaeota;    N‐glycosylation;    Sulfolobus;   

DOI  :  10.1002/mbo3.185

来源: Wiley

【 摘 要 】

Abstract

Sulfolobus acidocaldarius, a thermo-acidophilic crenarchaeon which grows optimally at 76°C and pH 3, exhibits an astonishing high number of N-glycans linked to the surface (S-) layer proteins. The S-layer proteins as well as other surface-exposed proteins are modified via N-glycosylation, in which the oligosaccharyl transferase AglB catalyzes the final step of the transfer of the glycan tree to the nascent protein. In this study, we demonstrated that AglB is essential for the viability of S. acidocaldarius. Different deletion approaches, that is, markerless in-frame deletion as well as a marker insertion were unsuccessful to create an aglB deletion mutant. Only the integration of a second aglB gene copy allowed the successful deletion of the original aglB.

【 授权许可】

CC BY   
© 2014 The Authors. MicrobiologyOpen published by John Wiley & Sons Ltd.

Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.