J 2023

Characteristics of N-Glycosylation and Its Impact on the Molecular Behavior of Lupinus angustifolius ?-Conglutin

CZUBINSKI, Jaroslaw, Erika LATTOVÁ, Zbyněk ZDRÁHAL and Richard STRASSER

Basic information

Original name

Characteristics of N-Glycosylation and Its Impact on the Molecular Behavior of Lupinus angustifolius ?-Conglutin

Authors

CZUBINSKI, Jaroslaw (616 Poland), Erika LATTOVÁ (703 Slovakia, guarantor, belonging to the institution), Zbyněk ZDRÁHAL (203 Czech Republic, belonging to the institution) and Richard STRASSER (40 Austria)

Edition

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, UNITED STATES, AMER CHEMICAL SOC, 2023, 0021-8561

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

40500 4.5 Other agricultural sciences

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

Impact factor

Impact factor: 6.100 in 2022

RIV identification code

RIV/00216224:14740/23:00131565

Organization unit

Central European Institute of Technology

UT WoS

000986537100001

Keywords in English

lupin seed;gamma-conglutin;N-glycosylation;mass spectrometry;post-translational modification;thermal stability

Tags

Tags

International impact, Reviewed
Změněno: 2/11/2024 21:14, Ing. Martina Blahová

Abstract

V originále

a-Conglutin, a lupin seed protein, is an intriguing protein both in terms of the complexity of its molecular structure and a broad spectrum of unique health-promoting properties manifested in animal and human trials. Moreover, this protein is an evolutionary cornerstone whose physiological significance for the plant has not been determined yet. Herein, a comprehensive characterization of a-conglutin glycosylation is presented and includes the identification of the N-glycan-bearing site, the qualitative and quantitative composition of glycan-building saccharides, as well as the effect of oligosaccharide removal on structural and thermal stability. The obtained results indicate the presence of glycans belonging to different classes attached to the Asn98 residue. In addition, the detachment of the oligosaccharide significantly affects secondary structure composition, which disturbs the oligomerization process. The structural changes were also reflected in biophysical parameters, i.e., at a pH value of 4.5, an increase in a-conglutin thermal stability was observed for the deglycosylated monomeric form. Collectively, the presented results provide evidence of the high complexity of the post-translational maturation and suggest the possibility of a functional effect that glycosylation might have on a-conglutin structure integrity.

Links

EF16_026/0008446, research and development project
Name: Integrace signálu a epigenetické reprogramování pro produktivitu rostlin
90242, large research infrastructures
Name: CIISB III