Information on EC 2.4.1.12 - cellulose synthase (UDP-forming)

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
2.4.1.12
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RECOMMENDED NAME
GeneOntology No.
cellulose synthase (UDP-forming)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-glucose + [(1->4)-beta-D-glucosyl]n = UDP + [(1->4)-beta-D-glucosyl]n+1
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
cellulose biosynthesis
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Metabolic pathways
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Starch and sucrose metabolism
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:(1->4)-beta-D-glucan 4-beta-D-glucosyltransferase
Involved in the synthesis of cellulose. A similar enzyme utilizes GDP-glucose [EC 2.4.1.29 cellulose synthase (GDP-forming)].
CAS REGISTRY NUMBER
COMMENTARY hide
9027-19-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
ixr1-1, ixr1-2
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Manually annotated by BRENDA team
Gloeocapsa sp.
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
several CesA and Csl genes
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Manually annotated by BRENDA team
several cesA genes
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Manually annotated by BRENDA team
several cesA genes
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Manually annotated by BRENDA team
several cesA genes
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Manually annotated by BRENDA team
several cesA genes
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Manually annotated by BRENDA team
several cesA genes
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Manually annotated by BRENDA team
several cesA genes
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Manually annotated by BRENDA team
several cesA genes
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Manually annotated by BRENDA team
several cesA genes
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Manually annotated by BRENDA team
a hybrid of Populus alba x Populus tremula, several cesA genes
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Manually annotated by BRENDA team
several cesA genes
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Manually annotated by BRENDA team
several cesA genes
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Manually annotated by BRENDA team
a hybrid of Populus deltoides x Populus nigra, several cesA genes
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Manually annotated by BRENDA team
several CesA and Csl genes
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Manually annotated by BRENDA team
spp. parvifolia, collected in Semengoh Forest Reservat, Kuching, Sarawak, Malaysia, gene SpcesA1
UniProt
Manually annotated by BRENDA team
genes csr2 and csr4
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Manually annotated by BRENDA team
several CesA and Csl genes
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Manually annotated by BRENDA team
several CesA and Csl genes
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
SmCesA2PH shares the PPBM motif with several PH domains of human proteins, the SmCesA2 PH domain is similar to the C-terminal PH domain of the human protein TAPP1
malfunction
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the naturally occuring irx3-1 and irx5-2 mutations are caused by premature stop codons that result in protein truncation of CESA7 and CESA4,respectively. In the naturally occuring irx3-1 background, interaction between CESA4 and CESA8 is greatly reduced, and the proteins fail to localize to the plasma membrane
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-glucose + [(1->4)-beta-D-glucosyl]n
UDP + [(1->4)-beta-D-glucosyl]n+1
show the reaction diagram
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-glucose + [(1->4)-beta-D-glucosyl]n
UDP + [(1->4)-beta-D-glucosyl]n+1
show the reaction diagram
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CDP
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enhances activity
CTP
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enhances activity
GDP
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enhances activity
GMP
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enhances activity
TDP
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inhibits at low concentrations, stimulates at high concentrations
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
the cotton fiber zinc-binding domain of cellulose synthase A1 displays rapid turnover in vitro and in vivo
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,6-dichlorobenzonitrile
affects mycelial growth; affects mycelial growth
Amphomycin
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in presence of 0.1% digitonin
bacitracin
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in presence of 0.1% digitonin
Congo red
isoxaben
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reduces cellulose synthesis in wild-type but not ixr1-1 seedlings
nucleoside phosphates
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degree of inhibition in decreasing order: nucleoside-triphosphate, nucleoside-diphosphate, nucleoside-monophosphate
TDP
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inhibits at low concentrations, stimulates at high concentrations
tunicamycin
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in presence of 0.1% digitonin
UDP-alpha-D-xylose
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strong inhibition
additional information
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no inhibition by guanosine and adenosine diphosphates
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3',5'-cGMP
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cellobiose
Cellodextrins
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stimulate cellulose synthesis, cellulose synthesis is dependent on presence of a soluble primer
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Cyclic diguanylic acid
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stimulation
cyclic-3',5'-diguanylate
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activates cellulose synthesis allosterically and binds BcsA-B with high affinity. The tight association of BcsA's PilZ and GT domains suggests that cyclic-3',5'-diguanylate controls the accessibility of the GT active site. Titrating UDP-Glc at different cyclic-3',5'-diguanylate concentrations shows that the maximum catalytic activity achieved depends on the overall c-di-GMP concentration, whereas the apparent affinity for UDP-Glc remains within 0.1-1.0 mM, comparable with the Km of 0.5 mM for UDP-Glc determined in the presence of 0.030 mM cyclic-3',5'-diguanylate. The cyclic-3',5'-diguanylate binding PilZ domain of cellulose synthase is a part of the catalytic BcsA subunit. Cyclic-3',5'-diguanylate does not alter BcsA's apparent affinity for UDP-Glc, yet it increases BcsA's apparent catalytic rate in vitro at least 10fold
cyclic-di-GMP
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BcsA contains a PilZ domain within its C-terminal, intracellular domain and its activity is strongly stimulated by the bacterial secondary messenger cyclic-di-GMP
D-glucose
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1 M, 7fold stimulation
Digitonin
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optimal concentration is 0.05%
methyl-beta-D-glucoside
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1 M, 11fold stimulation
Polyethylene glycol
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activation by polyethylene glycol and GTP is cooperative and involves association of the enzyme with a protein factor essential for high rates of enzyme activity
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004 - 2.5
UDPglucose
additional information
additional information
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monophasic Michaelis-Menten kinetics, kinetic analysis of cellulose synthesis, overview
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 8.5
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7.5
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.3
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pH 6.5: 13% of activity maximum, pH 7.5: 39% of activity maximum, pH 8.3: activity maximum, enzyme is not tested under more alkaline conditions because of instability of UDPglucose
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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assay at
27
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assay at
30
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
comparisons of morphologies of wild-type and mutant plant embryos and seedlings, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
co-localized with F-actin
Manually annotated by BRENDA team
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the cellulose synthase-containing compartment moves rapidly beneath sites of secondary wall synthesis, overview
Manually annotated by BRENDA team
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cortical, the cellulose synthase-containing compartment moves rapidly beneath sites of secondary wall synthesis, overview
Manually annotated by BRENDA team
co-localized with F-actin
Manually annotated by BRENDA team
co-localized with F-actin
Manually annotated by BRENDA team
additional information
CesA2 might co-localize with microtubules in vivo
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Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
83000
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alphabeta, 1 * 83000 + 1 * 93000, SDS-PAGE
93000
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alphabeta, 1 * 83000 + 1 * 93000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
isozyme CESA4
monomer
isozyme CESA7; isozyme CESA8
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
AtCesA7 is phosphorylated in vivo at two serine residues in a region of hyper-variability between the cellulose synthase catalytic subunits. Full length endogenous CesA7 is degraded via a proteasome dependant pathway in whole plant extracts. Phosphorylation of the catalytic subunits may target them for degradation via a proteasome dependant pathway. This is a possible mechanism by which plants regulate the relative levels of the three proteins whose specific interaction are required to form an active cellulose synthase complex
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
solution X-ray scattering of monomeric and dimeric catalytic subunits with or without bound substrate UDP-glucose
purified recombinant native and selenomethionine -labeled complex of BcsA and BcsB containing a translocating polysaccharide, from 30% PEG 200, 0.1 M MES, pH 6.5, and 50 mM NaCl at 4C, 7 days, X-ray diffraction structure determination and analysis, modeling, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
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after 16 h more than half of activity of the solubilized form is lost
25
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after 1 h more than half of activity of the solubilized form is lost
30
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rather labile
35
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quickly loses its in vitro activity beyond 35C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
BcsA-B is catalytically active in a detergent-solubilized state
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full length endogenous CesA7 is degraded via a proteasome dependant pathway in whole plant extracts. Phosphorylation of the catalytic subunits may target them for degradation via a proteasome dependant pathway. This is a possible mechanism by which plants regulate the relative levels of the three proteins whose specific interaction are required to form an active cellulose synthase complex
repeated freezing and thawing, substantial loss of activity
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when the protein is boiled in lithium dodecyl sulfate there is no detection of the 83000 Da polypeptide on the polyacrylamide gel, so the sample has to be incubated on ice
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, in liquid N2, stable
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0C, stable for several days
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4C, 1% digitonin, solubilized enzyme is stable for at least several h
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
IRX3 ist tightly bound to the cell wall and can only be released using very harsh conditions. Triton X-100 and NP40 are most effective. No effect: Triton X-114, Tween 80, Brij 35, Brij 58, CHAPS, octyl beta-glucoside, octyl beta-thioglucopyranoside
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native oligomers partially from microsomes as fragments of the cellulose synthase complex by dual epitope tagging of the CESA7 protein, selection for CESA multimers, overview. Recombinant His- and STREP-tagged CESA4, CESA7, and CESA8, as well as double mutant irx3-1:STREP-CESA7-irx3-1:His/FLAG-CESA7 from Arabidopsis thaliana irx1-1, irx3-1, and irx5-2 mutant plants by nickel and streptavidin affinity chromatography
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recombinant His-tagged native and selenomethionine -labeled subunits BcsA and B from Escherichia coli strain C43 by nickel affinity chromatography and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CesA and Csl genes, detailed phylogenetic analysis, overview
CesA2, expression in Escherichia coli strain BL21(DE3) and in human U2OS osteosarcoma cells as GFP-tagged enzyme using the pCDNA6.2/GW/C-EmGFP vector
construction of a phylogeny-based CesA nomenclature for the Populus CesA gene family, aligning it with the enzyme family from Arabidopsis thaliana, phylogenetic analysis, overview
expression in Arabidopsis Col-0
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expression in Escherichia coli
expression of a PtCesAP-GUS fusion protein in Agrobacterium tumefaciens C58/pMP90; expression of DNA in lambda phage
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expression of His- and STREP-tagged CESA4, CESA7, and CESA8 in Arabidopsis thaliana using the Agrobacterium tumefaciens transfection nethod in the mutant lines are irx1-1, irx3-1, and irx5-2
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gene cesA, genotyping, quantitative real-time PCR assays, overview
gene cesA2, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis; gene cesA4, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis
gene EgraCesA1, DNA and amino acid sequence determination and analysis, gene structure and genomic organization; gene EgraCesA1, DNA and amino acid sequence determination and analysis, gene structure and genomic organization; gene EgraCesA2, DNA and amino acid sequence determination and analysis, gene expression directed by the EgraCesA2 promoter or its deletions reveal several negative and positive regulatory regions controlling gene expression in xylem or phloem, a region is likely to contain mechanical stress-responsive elements, gene structure and genomic organization, overview; gene EgraCesA2, DNA and amino acid sequence determination and analysis, gene expression directed by the EgraCesA2 promoter or its deletions reveal several negative and positive regulatory regions controlling gene expression in xylem or phloem, a region is likely to contain mechanical stress-responsive elements, gene structure and genomic organization, overview; gene EgraCesA3, DNA and amino acid sequence determination and analysis, gene expression directed by the EgraCesA3 promoter or its deletions reveal several negative and positive regulatory regions controlling gene expression in xylem or phloem, a region is likely to contain mechanical stress-responsive elements, gene structure and genomic organization, overview
gene SpCesa1, from developing xylem, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis
genes cslF and cslH, native expression under the control of a constitutive promoter, recombinant expression of Hordeum vulgare CslH gene in Arabidopsis thaliana leads to the deposition of mixed-linked beta-glucan in the cell wall, which do not contains this polysaccharide in Arabidopsis thaliana
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genes cslF and cslH, native expression under the control of a constitutive promoter, the genome contains a cluster of rice CslF genes, recombinant expression of Oryza sativa CslF genes in Arabidopsis thaliana leads to the deposition of mixed-linked beta-glucan in the cell wall, which do not contains this polysaccharide in Arabidopsis thaliana
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genes csr2 and csr4, quantitative real-time RT-PCR assays with four CesA gene transcripts, CesA1, 2, 3, and 4, in the wild-type genetic background, and on the two antisense CesA gene transcripts, CesA2 and 4. The two CesA genes show different expression patterns in tubers, overview
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interaction analysis between membrane-bound cellulose synthases using the yeast two-hybrid expression system in strain NMY51, confirmed by in planta by bimolecular fluorescence complementation assay, overview; interaction analysis between membrane-bound cellulose synthases using the yeast two-hybrid expression system in strain NMY51, confirmed by in planta by bimolecular fluorescence complementation assay, overview; interaction analysis between membrane-bound cellulose synthases using the yeast two-hybrid expression system in strain NMY51, confirmed by in planta by bimolecular fluorescence complementation assay, overview
recombinant expression of His-tagged subunits BcsA and B in Escherichia coli strain C43
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recombinant expression of subunits BcsA and B in Escherichia coli strain C43
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usage of the CesA enzyme family from Arabidopsis thaliana for construction of a phylogeny-based CesA nomenclature for the Populus CesA gene family, aligning it with the enzyme family from Arabidopsis thaliana, phylogenetic analysis, overview
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CesA inhibition by 2,6-dichlorobenzonitrile or Congo Red results in increased expression of all CesA genes, overview; CesA inhibition by 2,6-dichlorobenzonitrile or Congo Red results in increased expression of all CesA genes, overview
EgraCesA1 gene expression is not upregulated in tension-stressed eucalyptus xylem cells, transcriptional regulation mechanisms of each EgraCesA genes, overview; EgraCesA1 gene expression is not upregulated in tension-stressed eucalyptus xylem cells, transcriptional regulation mechanisms of each EgraCesA genes, overview; transcriptional regulation mechanisms of each EgraCesA genes, overview; transcriptional regulation mechanisms of each EgraCesA genes, overview; transcriptional regulation mechanisms of each EgraCesA genes, overview
EgraCesA2 gene expression is upregulated in tension-stressed eucalyptus xylem cells; EgraCesA2 gene expression is upregulated in tension-stressed eucalyptus xylem cells; EgraCesA3 gene expression is upregulated in tension-stressed eucalyptus xylem cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G998B
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stable to the inhibitors: isoxaben and 5-tert-butyl-carbamoyloxy-3-(3-trifluormethyl)phenyl-4-thiazolidinone
T942I
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stable to the inhibitors: isoxaben and 5-tert-butyl-carbamoyloxy-3-(3-trifluormethyl)phenyl-4-thiazolidinone
G998B
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stable to the inhibitors: isoxaben and 5-tert-butyl-carbamoyloxy-3-(3-trifluormethyl)phenyl-4-thiazolidinone
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T942I
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stable to the inhibitors: isoxaben and 5-tert-butyl-carbamoyloxy-3-(3-trifluormethyl)phenyl-4-thiazolidinone
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C37A
site-directed mutagenesis of the RING-motif leading to slightly decreased interaction with other CESA proteins, overview
C37A/C56A
site-directed mutagenesis of the RING-motif leading to decreased interaction with other CESA proteins, overview
C37A/C64A C37A/C79A
site-directed mutagenesis of the RING-motif leading to decreased interaction with other CESA proteins, overview
C56A
site-directed mutagenesis of the RING-motif leading to slightly decreased interaction with other CESA proteins, overview
C56A/C64A
site-directed mutagenesis of the RING-motif leading to decreased interaction with other CESA proteins, overview
C56A/C79A C64A/C79A
site-directed mutagenesis of the RING-motif leading to decreased interaction with other CESA proteins, overview
C64A
site-directed mutagenesis of the RING-motif leading to slightly decreased interaction with other CESA proteins, overview
C79A
site-directed mutagenesis of the RING-motif leading to slightly decreased interaction with other CESA proteins, overview
P578S
identification of thanatos, a semidominant mutant of Arabidopsis thaliana with impaired growth of seedlings due to a mutation in the catalytic domain of cellulose synthase 3, homozygous seedlings of than germinate and grow but do not survive, while heterozygous plants are dwarfed and display a radially swollen root phenotype, cellulose content is reduced by approximately one-fifth in heterozygous and by two-fifths in homozygous plants, overview. Gene dosage-dependent expression of the AtCesA3 mutant gene in wild-type Arabidopsis thaliana plants results in a than dominant-negative phenotype. The mutation alters the structure of the CESA3 catalytic domain
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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