Dataset for: Enhanced glycosylation of S-layer protein enables a psychrophilic methanogenic archaeon to adapt to elevated temperatures in abundant substrates

Adaptation to higher temperatures would increase the environmental competitiveness of psychrophiles. Methanolobus psychrophilus, a cold wetland methanogen, “evolved” as a mesophile growing optimally at 30°C after subculturings, and cells grown with ample substrates exhibited higher integrity. This work investigated N-glycosylation of S-layer proteins, the major archaeal envelope component, with respect to mesophilic adaptation. Lectin affinity enriched a glycoprotein from 30°C and ample substrates-grown cells, which was identified as S-layer protein Mpsy_1486. Four N-glycosylation sites were identified, which exhibited different glycosylation profiles with N94 only found in 30°C-culutred cells. An N-linked glycosylation inhibitor, tunicamycin, reduced glycosylation levels of Mpsy_1486 and growth at 30°C, thus establishing a link between S-layer protein glycosylation and higher temperature adaptation of the psychrophilic archaeon M. psychrophilus.