Structural basis for the presence of a monoglucosylated oligosaccharide in mature glycoproteins

Hyo Il Jung; Young Hwan Kim; Soohyun Kim

doi:10.1016/j.bbrc.2005.02.192

Structural basis for the presence of a monoglucosylated oligosaccharide in mature glycoproteins

Hyo Il Jung, Young Hwan Kim, Soohyun Kim

Department of Mechanical Engineering

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

Abstract

Arylphorin is an insect hexameric storage protein. The structures of the oligosaccharides attached to this protein have recently been determined. However, their precise functions remain to be established. Proteolysis and MALDI MS studies disclose that the amino acid residues Asn196 and Asn344 are N-glycosylated with Glc₁Man₉GlcNAc₂ and Man_5-6GlcNAc₂ oligosaccharides, respectively. Interestingly, significant variations in the amounts of glycans involving Glc₁Man₉GlcNAc₂ are evident in arylphorins purified from larvae reared at different seasons. The data suggest that the metabolism of larvae and local protein structure contribute to glycan development. Three-dimensional model of the protein speculated that N-glycosidic linkage to Asn196 in the Glc₁Man₉GlcNAc₂ structure was buried inside the twofold axis of the hexamer, whereas oligosaccharide linkages to Asn344 were completely exposed to solvent. This finding is in agreement with previous biochemical data showing that limited Glc₁Man₉GlcNAc₂ was released by protein-N-glycosidase F under non-denaturing conditions, in contrast to Man _5-6GlcNAc₂ oligosaccharides.

Original language	English
Pages (from-to)	100-106
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	331
Issue number	1
DOIs	https://doi.org/10.1016/j.bbrc.2005.02.192
Publication status	Published - 2005 May 27

Bibliographical note

Funding Information:
This work was supported by a grant, R01-2002-000-00224-0 (to S.K.), from the Basic Research Program and National Core Research Center for Nanomedical Technology Center (to H.J.) of the Korea Science and Engineering Foundation. The authors thank K.I. Kim for excellent MS operation and Dr. S.M. Lee for generously supplying larval hemolymph.

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2005.02.192

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title = "Structural basis for the presence of a monoglucosylated oligosaccharide in mature glycoproteins",

abstract = "Arylphorin is an insect hexameric storage protein. The structures of the oligosaccharides attached to this protein have recently been determined. However, their precise functions remain to be established. Proteolysis and MALDI MS studies disclose that the amino acid residues Asn196 and Asn344 are N-glycosylated with Glc1Man9GlcNAc2 and Man5-6GlcNAc2 oligosaccharides, respectively. Interestingly, significant variations in the amounts of glycans involving Glc1Man9GlcNAc2 are evident in arylphorins purified from larvae reared at different seasons. The data suggest that the metabolism of larvae and local protein structure contribute to glycan development. Three-dimensional model of the protein speculated that N-glycosidic linkage to Asn196 in the Glc1Man9GlcNAc2 structure was buried inside the twofold axis of the hexamer, whereas oligosaccharide linkages to Asn344 were completely exposed to solvent. This finding is in agreement with previous biochemical data showing that limited Glc1Man9GlcNAc2 was released by protein-N-glycosidase F under non-denaturing conditions, in contrast to Man 5-6GlcNAc2 oligosaccharides.",

author = "Jung, {Hyo Il} and Kim, {Young Hwan} and Soohyun Kim",

note = "Funding Information: This work was supported by a grant, R01-2002-000-00224-0 (to S.K.), from the Basic Research Program and National Core Research Center for Nanomedical Technology Center (to H.J.) of the Korea Science and Engineering Foundation. The authors thank K.I. Kim for excellent MS operation and Dr. S.M. Lee for generously supplying larval hemolymph.",

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N2 - Arylphorin is an insect hexameric storage protein. The structures of the oligosaccharides attached to this protein have recently been determined. However, their precise functions remain to be established. Proteolysis and MALDI MS studies disclose that the amino acid residues Asn196 and Asn344 are N-glycosylated with Glc1Man9GlcNAc2 and Man5-6GlcNAc2 oligosaccharides, respectively. Interestingly, significant variations in the amounts of glycans involving Glc1Man9GlcNAc2 are evident in arylphorins purified from larvae reared at different seasons. The data suggest that the metabolism of larvae and local protein structure contribute to glycan development. Three-dimensional model of the protein speculated that N-glycosidic linkage to Asn196 in the Glc1Man9GlcNAc2 structure was buried inside the twofold axis of the hexamer, whereas oligosaccharide linkages to Asn344 were completely exposed to solvent. This finding is in agreement with previous biochemical data showing that limited Glc1Man9GlcNAc2 was released by protein-N-glycosidase F under non-denaturing conditions, in contrast to Man 5-6GlcNAc2 oligosaccharides.

AB - Arylphorin is an insect hexameric storage protein. The structures of the oligosaccharides attached to this protein have recently been determined. However, their precise functions remain to be established. Proteolysis and MALDI MS studies disclose that the amino acid residues Asn196 and Asn344 are N-glycosylated with Glc1Man9GlcNAc2 and Man5-6GlcNAc2 oligosaccharides, respectively. Interestingly, significant variations in the amounts of glycans involving Glc1Man9GlcNAc2 are evident in arylphorins purified from larvae reared at different seasons. The data suggest that the metabolism of larvae and local protein structure contribute to glycan development. Three-dimensional model of the protein speculated that N-glycosidic linkage to Asn196 in the Glc1Man9GlcNAc2 structure was buried inside the twofold axis of the hexamer, whereas oligosaccharide linkages to Asn344 were completely exposed to solvent. This finding is in agreement with previous biochemical data showing that limited Glc1Man9GlcNAc2 was released by protein-N-glycosidase F under non-denaturing conditions, in contrast to Man 5-6GlcNAc2 oligosaccharides.

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Structural basis for the presence of a monoglucosylated oligosaccharide in mature glycoproteins

Abstract

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