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Yeast N-glycanase distinguishes between native and non-native glycoproteins.酵母N-聚糖酶能够区分天然糖蛋白和非天然糖蛋白。
EMBO Rep. 2004 Feb;5(2):201-6. doi: 10.1038/sj.embor.7400066. Epub 2004 Jan 9.
2
Free oligosaccharides to monitor glycoprotein endoplasmic reticulum-associated degradation in Saccharomyces cerevisiae.监测酿酒酵母糖蛋白内质网相关降解的游离寡糖。
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3
Influence of substrate conformation on the deglycosylation of ribonuclease B by recombinant yeast peptide:N-glycanase.底物构象对重组酵母肽:N-聚糖酶催化核糖核酸酶B去糖基化的影响
Acta Biochim Biophys Sin (Shanghai). 2007 Jan;39(1):8-14. doi: 10.1111/j.1745-7270.2007.00244.x.
4
N-terminal deletion of peptide:N-glycanase results in enhanced deglycosylation activity.肽:N-糖基水解酶的 N 端缺失导致去糖基化活性增强。
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Physiological and molecular functions of the cytosolic peptide:N-glycanase.细胞质肽:N-糖基酶的生理和分子功能。
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Structure of a peptide:N-glycanase-Rad23 complex: insight into the deglycosylation for denatured glycoproteins.一种肽:N-聚糖酶-Rad23复合物的结构:对变性糖蛋白去糖基化作用的深入了解。
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7
The Png1-Rad23 complex regulates glycoprotein turnover.Png1-Rad23复合物调节糖蛋白周转。
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8
Identification of PNGase-dependent ERAD substrates in Saccharomyces cerevisiae.酿酒酵母中依赖肽-N-糖苷酶的内质网相关蛋白降解底物的鉴定。
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Wild type RTA and less toxic variants have distinct requirements for Png1 for their depurination activity and toxicity in Saccharomyces cerevisiae.野生型RTA和毒性较低的变体在酿酒酵母中进行脱嘌呤活性和毒性时,对Png1有不同的要求。
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Endoplasmic reticulum-associated SKN-1A/Nrf1 mediates a cytoplasmic unfolded protein response and promotes longevity.内质网相关 SKN-1A/Nrf1 介导细胞质未折叠蛋白反应并促进长寿。
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Inhibition of NGLY1 Inactivates the Transcription Factor Nrf1 and Potentiates Proteasome Inhibitor Cytotoxicity.NGLY1的抑制使转录因子Nrf1失活并增强蛋白酶体抑制剂的细胞毒性。
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Glycosylation-directed quality control of protein folding.糖基化定向的蛋白质折叠质量控制。
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Wild type RTA and less toxic variants have distinct requirements for Png1 for their depurination activity and toxicity in Saccharomyces cerevisiae.野生型RTA和毒性较低的变体在酿酒酵母中进行脱嘌呤活性和毒性时,对Png1有不同的要求。
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Derlin-1 is a rhomboid pseudoprotease required for the dislocation of mutant α-1 antitrypsin from the endoplasmic reticulum.Derlin-1 是一种菱形假蛋白酶,对于突变型α-1 抗胰蛋白酶从内质网的易位是必需的。
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Deglycosylated milin unfolds via inactive monomeric intermediates.去糖基化的 milin 通过非活性单体中间产物展开。
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本文引用的文献

1
The preparation of subtilisn-modified ribonuclease and the separation of the peptide and protein components.枯草杆菌蛋白酶修饰的核糖核酸酶的制备以及肽和蛋白质成分的分离。
J Biol Chem. 1959 Jun;234(6):1459-65.
2
Enhancement of endoplasmic reticulum (ER) degradation of misfolded Null Hong Kong alpha1-antitrypsin by human ER mannosidase I.人内质网甘露糖苷酶I增强对错误折叠的香港α1-抗胰蛋白酶的内质网降解作用
J Biol Chem. 2003 Jul 11;278(28):26287-94. doi: 10.1074/jbc.M303395200. Epub 2003 May 6.
3
Glycopeptide specificity of the secretory protein folding sensor UDP-glucose glycoprotein:glucosyltransferase.分泌性蛋白质折叠传感器UDP-葡萄糖糖蛋白:葡糖基转移酶的糖肽特异性
EMBO Rep. 2003 Apr;4(4):405-11. doi: 10.1038/sj.embor.embor797.
4
A role for N-glycanase in the cytosolic turnover of glycoproteins.N-聚糖酶在糖蛋白胞质周转中的作用。
EMBO J. 2003 Mar 3;22(5):1036-46. doi: 10.1093/emboj/cdg107.
5
UDP-Glc:glycoprotein glucosyltransferase recognizes structured and solvent accessible hydrophobic patches in molten globule-like folding intermediates.UDP-葡萄糖:糖蛋白葡糖基转移酶识别类熔球折叠中间体中的结构化且溶剂可及的疏水区域。
Proc Natl Acad Sci U S A. 2003 Jan 7;100(1):86-91. doi: 10.1073/pnas.262661199. Epub 2002 Dec 23.
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PNG1, a yeast gene encoding a highly conserved peptide:N-glycanase.PNG1,一种编码高度保守的肽:N-聚糖酶的酵母基因。
J Cell Biol. 2000 May 29;149(5):1039-52. doi: 10.1083/jcb.149.5.1039.
7
Recognition of local glycoprotein misfolding by the ER folding sensor UDP-glucose:glycoprotein glucosyltransferase.内质网折叠传感器UDP-葡萄糖:糖蛋白葡糖基转移酶对局部糖蛋白错误折叠的识别。
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8
Conformational requirements for glycoprotein reglucosylation in the endoplasmic reticulum.内质网中糖蛋白再糖基化的构象要求。
J Cell Biol. 2000 Mar 20;148(6):1123-29. doi: 10.1083/jcb.148.6.1123.
9
A superfamily of archaeal, bacterial, and eukaryotic proteins homologous to animal transglutaminases.一个与动物转谷氨酰胺酶同源的古菌、细菌和真核生物蛋白质超家族。
Protein Sci. 1999 Aug;8(8):1714-9. doi: 10.1110/ps.8.8.1714.
10
Crystal structures of ribonuclease A complexes with 5'-diphosphoadenosine 3'-phosphate and 5'-diphosphoadenosine 2'-phosphate at 1.7 A resolution.核糖核酸酶A与5'-二磷酸腺苷3'-磷酸和5'-二磷酸腺苷2'-磷酸复合物在1.7埃分辨率下的晶体结构。
Biochemistry. 1997 May 6;36(18):5578-88. doi: 10.1021/bi9700330.

酵母N-聚糖酶能够区分天然糖蛋白和非天然糖蛋白。

Yeast N-glycanase distinguishes between native and non-native glycoproteins.

作者信息

Hirsch Christian, Misaghi Shahram, Blom Daniël, Pacold Michael E, Ploegh Hidde L

机构信息

Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115, USA.

出版信息

EMBO Rep. 2004 Feb;5(2):201-6. doi: 10.1038/sj.embor.7400066. Epub 2004 Jan 9.

DOI:10.1038/sj.embor.7400066
PMID:14726951
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1298977/
Abstract

N-glycanase from Saccharomyces cerevisiae (Png1) preferentially removes N-glycans from misfolded proteins. The ability of Png1 to distinguish between folded and misfolded glycoproteins is reminiscent of substrate recognition by UDP-glucose glycoprotein glucosyl transferase, an enzyme that possesses this trait. The only known in vivo substrates of Png1 are aberrant glycoproteins that originate in the endoplasmic reticulum, and arrive in the cytoplasm for proteasomal degradation. The substrate specificity of Png1 is admirably suited for this task.

摘要

来自酿酒酵母的N-聚糖酶(Png1)优先从错误折叠的蛋白质中去除N-聚糖。Png1区分折叠和错误折叠糖蛋白的能力让人联想到UDP-葡萄糖糖蛋白葡糖基转移酶对底物的识别,后者是一种具有这种特性的酶。Png1唯一已知的体内底物是起源于内质网、到达细胞质进行蛋白酶体降解的异常糖蛋白。Png1的底物特异性非常适合这项任务。