Structural insights into homotrimeric assembly of cellulose synthase CesA7 from Gossypium hirsutum.
GhCesA
cellulose synthase
cotton fibres
homotrimer
Journal
Plant biotechnology journal
ISSN: 1467-7652
Titre abrégé: Plant Biotechnol J
Pays: England
ID NLM: 101201889
Informations de publication
Date de publication:
08 2021
08 2021
Historique:
revised:
05
02
2021
received:
15
12
2020
accepted:
16
02
2021
pubmed:
28
2
2021
medline:
4
9
2021
entrez:
27
2
2021
Statut:
ppublish
Résumé
Cellulose is one of the most abundant organic polymers in nature. It contains multiple β-1,4-glucan chains synthesized by cellulose synthases (CesAs) on the plasma membrane of higher plants. CesA subunits assemble into a pseudo-sixfold symmetric cellulose synthase complex (CSC), known as a 'rosette complex'. The structure of CesA remains enigmatic. Here, we report the cryo-EM structure of the homotrimeric CesA7 from Gossypium hirsutum at 3.5-angstrom resolution. The GhCesA7 homotrimer shows a C3 symmetrical assembly. Each protomer contains seven transmembrane helices (TMs) which form a channel potentially facilitating the release of newly synthesized glucans. The cytoplasmic glycosyltransferase domain (GT domain) of GhCesA7 protrudes from the membrane, and its catalytic pocket is directed towards the TM pore. The homotrimer GhCesA7 is stabilized by the transmembrane helix 7 (TM7) and the plant-conserved region (PCR) domains. It represents the building block of CSCs and facilitates microfibril formation. This structure provides insight into how eukaryotic cellulose synthase assembles and provides a mechanistic basis for the improvement of cotton fibre quality in the future.
Identifiants
pubmed: 33638282
doi: 10.1111/pbi.13571
pmc: PMC8384604
doi:
Substances chimiques
Cellulose
9004-34-6
Glucosyltransferases
EC 2.4.1.-
cellulose synthase
EC 2.4.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1579-1587Informations de copyright
© 2021 The Authors. Plant Biotechnology Journal published by Society for Experimental Biology and The Association of Applied Biologists and John Wiley & Sons Ltd.
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