Organization of cellulose synthase complexes involved in primary cell wall synthesis in Arabidopsis thaliana
0301 basic medicine
Arabidopsis thaliana
MESH: Plant Shoots
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Arabidopsis
CESA
MESH: Plant Roots
plant
MESH: Protein Isoforms
cellulose synthase
Plant Roots
catalytic subunit
Cell Wall
Gene Expression Regulation, Plant
MESH: Models
MESH: Genes, Plant
Protein Isoforms
MESH: Arabidopsis
MESH: Models, Genetic
MESH: Cellulose
Cell wall
isoform
MESH: Gene Expression Regulation
ARABIDOPSIS THALIANA;PROTEIN;CELLULOSE;MUTANT
MESH: Genes
cellulose
MESH: Microfibrils
Glucosyltransferases
Plant Shoots
570
MESH: Arabidopsis Proteins
Genes, Plant
03 medical and health sciences
MESH: Cell Wall
Genetic
SDV:BBM
[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology
MESH: Gene Expression Regulation, Plant
Cellulose
Molecular Biology
MESH: Glucosyltransferases
Models, Genetic
Arabidopsis Proteins
540
plant;Arabidopsis thaliana;Cell wall;cellulose;biosynthesis;enzyme;cellulose synthase;isoform;catalytic subunit;gene expression;CESA;Arabidopsis;Arabidopsis Proteins;Cell Wall;Cellulose;Gene Expression Regulation;Plant;Genes;Glucosyltransferases;Microfibrils;Models;Genetic;Plant Roots;Plant Shoots;Protein Isoforms
enzyme
Microfibrils
gene expression
biosynthesis
DOI:
10.1073/pnas.0706569104
Publication Date:
2007-09-19T01:04:45Z
AUTHORS (9)
ABSTRACT
In all land plants, cellulose is synthesized from hexameric plasma membrane complexes. Indirect evidence suggests that in vascular plants the complexes involved in primary wall synthesis contain three distinct cellulose synthase catalytic subunits (CESAs). In this study, we show that CESA3 and CESA6 fused to GFP are expressed in the same cells and at the same time in the hypocotyl of etiolated seedlings and migrate with comparable velocities along linear trajectories at the cell surface. We also show that CESA3 and CESA6 can be coimmunoprecipitated from detergent-solubilized extracts, their protein levels decrease in mutants for either
CESA3
,
CESA6
, or
CESA1
and CESA3, CESA6 and also CESA1 can physically interact
in vivo
as shown by bimolecular fluorescence complementation. We also demonstrate that CESA6-related CESA5 and CESA2 are partially, but not completely, redundant with CESA6 and most likely compete with CESA6 for the same position in the cellulose synthesis complex. Using promoter-β-glucuronidase fusions we show that
CESA5
,
CESA6
, and
CESA2
have distinct overlapping expression patterns in hypocotyl and root corresponding to different stages of cellular development. Together, these data provide evidence for the existence of binding sites for three distinct CESA subunits in primary wall cellulose synthase complexes, with two positions being invariably occupied by CESA1 and CESA3, whereas at least three isoforms compete for the third position. Participation of the latter three isoforms might fine-tune the CESA complexes for the deposition of microfibrils at distinct cellular growth stages.
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