Identification of a novel endo-O-mannosidases for developing a new tool for de-glycosylation of O-glycans

2017 Fiscal Year Final Research Report

• Project/Area Number: 16K18521
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Functional biochemistry
• Research Institution: Institute of Physical and Chemical Research
• Principal Investigator: Hirayama Hiroto 国立研究開発法人理化学研究所, 糖鎖代謝学研究チーム, 客員研究員 (50525847)
• Project Period (FY): 2016-04-01 – 2018-03-31
• Keywords: 糖鎖 / 代謝 / 遊離糖鎖 / 出芽酵母

Outline of Final Research Achievements

Glycosylation for the nascent proteins are one of the most common co- and post- translational modifications. This modification is well known to play a critical role in the various biological processes . It is known that free-formed N-glycans, designated as free N-glycans (fNgs), which are liberated from glycans on the glycoproteins, are accumulated in the cytosol. However biological meaning of the accumulation of fNgs is unclear. Unexpectedly, we found that under specific culture condition, yeast cells generate novel free glycans derived from O-linked sugar chains on the glycoproteins, suggesting yeast cells possess a novel endo O-mannosidase (EOM). Our goal of this study, therefore, is not only identification of the gene coding EOM and gain deeper insight into biological and physiological meaning of the generation of the free glycans derived from O-glycans(fOGs) but also providing this enzyme as a tool for structural/functional analysis of O-glycan on glycoproteins.

Free Research Field

糖鎖生物学