Specific protein interactions between rice members of the GT43 and GT47 families form various central cores of putative xylan synthase complexes.

NAPPA Oryza sativa confocal microscopy heteroxylan protein-protein interaction

Journal

The Plant journal : for cell and molecular biology
ISSN: 1365-313X
Titre abrégé: Plant J
Pays: England
ID NLM: 9207397

Informations de publication

Date de publication:
23 Jan 2024
Historique:
revised: 04 01 2024
received: 29 08 2023
accepted: 08 01 2024
medline: 23 1 2024
pubmed: 23 1 2024
entrez: 23 1 2024
Statut: aheadofprint

Résumé

Members of the glycosyltransferase (GT)43 and GT47 families have been associated with heteroxylan synthesis in both dicots and monocots and are thought to assemble into central cores of putative xylan synthase complexes (XSCs). Currently, it is unknown whether protein-protein interactions within these central cores are specific, how many such complexes exist, and whether these complexes are functionally redundant. Here, we used gene association network and co-expression approaches in rice to identify four OsGT43s and four OsGT47s that assemble into different GT43/GT47 complexes. Using two independent methods, we showed that (i) these GTs assemble into at least six unique complexes through specific protein-protein interactions and (ii) the proteins interact directly in vitro. Confocal microscopy showed that, when alone, all OsGT43s were retained in the endoplasmic reticulum (ER), while all OsGT47s were localized in the Golgi. co-expression of OsGT43s and OsGT47s displayed complexes that form in the ER but accumulate in Golgi. ER-to-Golgi trafficking appears to require interactions between OsGT43s and OsGT47s. Comparison of the central cores of the three putative rice OsXSCs to wheat, asparagus, and Arabidopsis XSCs, showed great variation in GT43/GT47 combinations, which makes the identification of orthologous central cores between grasses and dicots challenging. However, the emerging picture is that all central cores from these species seem to have at least one member of the IRX10/IRX10-L clade in the GT47 family in common, suggesting greater functional importance for this family in xylan synthesis. Our findings provide a new framework for future investigation of heteroxylan biosynthesis and function in monocots.

Identifiants

pubmed: 38261531
doi: 10.1111/tpj.16640
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : Ohio University

Informations de copyright

© 2024 The Authors. The Plant Journal published by Society for Experimental Biology and John Wiley & Sons Ltd.

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Auteurs

Tasleem Javaid (T)

Department of Environmental and Plant Biology, Ohio University, Athens, Ohio, 45701, USA.

Matrika Bhattarai (M)

Department of Environmental and Plant Biology, Ohio University, Athens, Ohio, 45701, USA.

Akshayaa Venkataraghavan (A)

Department of Environmental and Plant Biology, Ohio University, Athens, Ohio, 45701, USA.

Michael Held (M)

Department of Chemistry and Biochemistry, Ohio University, Athens, Ohio, 45701, USA.

Ahmed Faik (A)

Department of Environmental and Plant Biology, Ohio University, Athens, Ohio, 45701, USA.

Classifications MeSH