Molecular mechanisms of glycogen particle assembly in Escherichia coli.
Escherichia coli
Glycogen debranching enzyme
Glycogen phosphorylase
Glycogen α particle
Structural fragility
Journal
Carbohydrate polymers
ISSN: 1879-1344
Titre abrégé: Carbohydr Polym
Pays: England
ID NLM: 8307156
Informations de publication
Date de publication:
01 Jan 2023
01 Jan 2023
Historique:
received:
14
09
2022
revised:
02
10
2022
accepted:
05
10
2022
entrez:
6
3
2023
pubmed:
7
3
2023
medline:
8
3
2023
Statut:
ppublish
Résumé
It has been reported that glycogen in Escherichia coli has two structural states, that is, fragility and stability, which alters dynamically. However, molecular mechanisms behind the structural alterations are not fully understood. In this study, we focused on the potential roles of two important glycogen degradation enzymes, glycogen phosphorylase (glgP) and glycogen debranching enzyme (glgX), in glycogen structural alterations. The fine molecular structure of glycogen particles in Escherichia coli and three mutants (ΔglgP, ΔglgX and ΔglgP/ΔglgX) were examined, which showed that glycogen in E. coli ΔglgP and E. coli ΔglgP/ΔglgX were consistently fragile while being consistently stable in E. coli ΔglgX, indicating the dominant role of GP in glycogen structural stability control. In sum, our study concludes that glycogen phosphorylase is essential in glycogen structural stability, leading to molecular insights into structural assembly of glycogen particles in E. coli.
Identifiants
pubmed: 36876811
pii: S0144-8617(22)01105-5
doi: 10.1016/j.carbpol.2022.120200
pii:
doi:
Substances chimiques
Glycogen
9005-79-2
Glycogen Debranching Enzyme System
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
120200Informations de copyright
Copyright © 2022 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare no competing financial interest.