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酿酒酵母α-葡萄糖苷酶突变体中游离N-聚糖的结构分析：缺乏作用于N-聚糖的分解代谢α-葡萄糖苷酶存在的证据

Structural Analysis of Free N-Glycans in α-Glucosidase Mutants of Saccharomyces cerevisiae: Lack of the Evidence for the Occurrence of Catabolic α-Glucosidase Acting on the N-Glycans.

作者信息

Hossain Tanim Jabid, Harada Yoichiro, Hirayama Hiroto, Tomotake Haruna, Seko Akira, Suzuki Tadashi

机构信息

Glycometabolome Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center for Systems Chemical Biology, RIKEN Global Research Cluster, Wako, Saitama, Japan.

Graduate School of Science and Engineering, Saitama University, Sakura, Saitama, Japan.

出版信息

PLoS One. 2016 Mar 24;11(3):e0151891. doi: 10.1371/journal.pone.0151891. eCollection 2016.

DOI:10.1371/journal.pone.0151891
PMID:27010459
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4807098/
Abstract

Saccharomyces cerevisiae produces two different α-glucosidases, Glucosidase 1 (Gls1) and Glucosidase 2 (Gls2), which are responsible for the removal of the glucose molecules from N-glycans (Glc3Man9GlcNAc2) of glycoproteins in the endoplasmic reticulum. Whether any additional α-glucosidases playing a role in catabolizing the glucosylated N-glycans are produced by this yeast, however, remains unknown. We report herein on a search for additional α-glucosidases in S. cerevisiae. To this end, the precise structures of cytosolic free N-glycans (FNGs), mainly derived from the peptide:N-glycanase (Png1) mediated deglycosylation of N-glycoproteins were analyzed in the endoplasmic reticulum α-glucosidase-deficient mutants. 12 new glucosylated FNG structures were successfully identified through 2-dimentional HPLC analysis. On the other hand, non-glucosylated FNGs were not detected at all under any culture conditions. It can therefore be safely concluded that no catabolic α-glucosidases acting on N-glycans are produced by this yeast.

摘要

酿酒酵母会产生两种不同的α-葡萄糖苷酶，即葡萄糖苷酶1（Gls1）和葡萄糖苷酶2（Gls2），它们负责在内质网中从糖蛋白的N-聚糖（Glc3Man9GlcNAc2）上移除葡萄糖分子。然而，这种酵母是否会产生其他在代谢糖基化N-聚糖中起作用的α-葡萄糖苷酶仍不清楚。我们在此报告了对酿酒酵母中其他α-葡萄糖苷酶的搜索。为此，在内质网α-葡萄糖苷酶缺陷型突变体中分析了主要源自肽：N-聚糖酶（Png1）介导的N-糖蛋白去糖基化的胞质游离N-聚糖（FNG）的精确结构。通过二维高效液相色谱分析成功鉴定出12种新的糖基化FNG结构。另一方面，在任何培养条件下都完全未检测到非糖基化的FNG。因此，可以有把握地得出结论，这种酵母不会产生作用于N-聚糖的分解代谢α-葡萄糖苷酶。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd3c/4807098/c96fe9a6bc98/pone.0151891.g010.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd3c/4807098/f084dd049345/pone.0151891.g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd3c/4807098/fdd156ba349b/pone.0151891.g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd3c/4807098/a98946431de3/pone.0151891.g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd3c/4807098/55b039192be0/pone.0151891.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd3c/4807098/7362a916e978/pone.0151891.g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd3c/4807098/c9de97d0a98e/pone.0151891.g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd3c/4807098/b6dbcd8bf8c6/pone.0151891.g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd3c/4807098/464230221042/pone.0151891.g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd3c/4807098/8f3f853f8870/pone.0151891.g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd3c/4807098/c96fe9a6bc98/pone.0151891.g010.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd3c/4807098/f084dd049345/pone.0151891.g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd3c/4807098/fdd156ba349b/pone.0151891.g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd3c/4807098/a98946431de3/pone.0151891.g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd3c/4807098/55b039192be0/pone.0151891.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd3c/4807098/7362a916e978/pone.0151891.g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd3c/4807098/c9de97d0a98e/pone.0151891.g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd3c/4807098/b6dbcd8bf8c6/pone.0151891.g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd3c/4807098/464230221042/pone.0151891.g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd3c/4807098/8f3f853f8870/pone.0151891.g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd3c/4807098/c96fe9a6bc98/pone.0151891.g010.jpg

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