J 2023

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

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

Základní údaje

Originální název

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

Autoři

CZUBINSKI, Jaroslaw (616 Polsko), Erika LATTOVÁ (703 Slovensko, garant, domácí), Zbyněk ZDRÁHAL (203 Česká republika, domácí) a Richard STRASSER (40 Rakousko)

Vydání

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

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

40500 4.5 Other agricultural sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

Impakt faktor

Impact factor: 6.100 v roce 2022

Kód RIV

RIV/00216224:14740/23:00131565

Organizační jednotka

Středoevropský technologický institut

UT WoS

000986537100001

Klíčová slova anglicky

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

Štítky

Příznaky

Mezinárodní význam, Recenzováno
Změněno: 2. 11. 2024 21:14, Ing. Martina Blahová

Anotace

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.

Návaznosti

EF16_026/0008446, projekt VaV
Název: Integrace signálu a epigenetické reprogramování pro produktivitu rostlin
90242, velká výzkumná infrastruktura
Název: CIISB III