CB5C affects the glucosinolate profile in Arabidopsis thaliana

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

CB5C affects the glucosinolate profile in Arabidopsis thaliana. / Vik, Daniel; Crocoll, Christoph; Andersen, Tonni Grube; Burow, Meike; Halkier, Barbara Ann.

In: Plant Signalling & Behavior, Vol. 11, No. 8, e1160189, 2016.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Vik, D, Crocoll, C, Andersen, TG, Burow, M & Halkier, BA 2016, 'CB5C affects the glucosinolate profile in Arabidopsis thaliana', Plant Signalling & Behavior, vol. 11, no. 8, e1160189. https://doi.org/10.1080/15592324.2016.1160189

APA

Vik, D., Crocoll, C., Andersen, T. G., Burow, M., & Halkier, B. A. (2016). CB5C affects the glucosinolate profile in Arabidopsis thaliana. Plant Signalling & Behavior, 11(8), [e1160189]. https://doi.org/10.1080/15592324.2016.1160189

Vancouver

Vik D, Crocoll C, Andersen TG, Burow M, Halkier BA. CB5C affects the glucosinolate profile in Arabidopsis thaliana. Plant Signalling & Behavior. 2016;11(8). e1160189. https://doi.org/10.1080/15592324.2016.1160189

Author

Vik, Daniel ; Crocoll, Christoph ; Andersen, Tonni Grube ; Burow, Meike ; Halkier, Barbara Ann. / CB5C affects the glucosinolate profile in Arabidopsis thaliana. In: Plant Signalling & Behavior. 2016 ; Vol. 11, No. 8.

Bibtex

@article{cd061d1d6422415ab8907703f0da4c24,
title = "CB5C affects the glucosinolate profile in Arabidopsis thaliana",
abstract = "Cytochrome b5 (CB5) proteins are small heme-binding proteins, that influence cytochrome P450 activity. While only one CB5 isoform is found in mammals, higher plants have several isoforms of these proteins. The roles of the many CB5 isoforms in plants remain unknown. We hypothesized that CB5 proteins support the cytochrome P450 enzymes of plant specialized metabolism and found CB5C from Arabidopsis thaliana to co-express with glucosinolate biosynthetic genes. We characterized the glucosinolate profiles of two T-DNA insertion mutants of CB5C, and found that long-chained aliphatic glucosinolates were reduced in one of the mutant lines - a phenotype that was exaggerated upon methyl-jasmonate treatment. These results support the hypothesis, that CB5C influences glucosinolate biosynthesis, however, the mode of action remains unknown. Furthermore, the mutants differed in their biomass response to methyl jasmonate treatment. Thereby, our results highlight the varying effects of T-DNA insertion sites, as the two analyzed alleles show different phenotypes.",
author = "Daniel Vik and Christoph Crocoll and Andersen, {Tonni Grube} and Meike Burow and Halkier, {Barbara Ann}",
year = "2016",
doi = "10.1080/15592324.2016.1160189",
language = "English",
volume = "11",
journal = "Plant Signalling & Behavior",
issn = "1559-2316",
publisher = "Taylor & Francis",
number = "8",

}

RIS

TY - JOUR

T1 - CB5C affects the glucosinolate profile in Arabidopsis thaliana

AU - Vik, Daniel

AU - Crocoll, Christoph

AU - Andersen, Tonni Grube

AU - Burow, Meike

AU - Halkier, Barbara Ann

PY - 2016

Y1 - 2016

N2 - Cytochrome b5 (CB5) proteins are small heme-binding proteins, that influence cytochrome P450 activity. While only one CB5 isoform is found in mammals, higher plants have several isoforms of these proteins. The roles of the many CB5 isoforms in plants remain unknown. We hypothesized that CB5 proteins support the cytochrome P450 enzymes of plant specialized metabolism and found CB5C from Arabidopsis thaliana to co-express with glucosinolate biosynthetic genes. We characterized the glucosinolate profiles of two T-DNA insertion mutants of CB5C, and found that long-chained aliphatic glucosinolates were reduced in one of the mutant lines - a phenotype that was exaggerated upon methyl-jasmonate treatment. These results support the hypothesis, that CB5C influences glucosinolate biosynthesis, however, the mode of action remains unknown. Furthermore, the mutants differed in their biomass response to methyl jasmonate treatment. Thereby, our results highlight the varying effects of T-DNA insertion sites, as the two analyzed alleles show different phenotypes.

AB - Cytochrome b5 (CB5) proteins are small heme-binding proteins, that influence cytochrome P450 activity. While only one CB5 isoform is found in mammals, higher plants have several isoforms of these proteins. The roles of the many CB5 isoforms in plants remain unknown. We hypothesized that CB5 proteins support the cytochrome P450 enzymes of plant specialized metabolism and found CB5C from Arabidopsis thaliana to co-express with glucosinolate biosynthetic genes. We characterized the glucosinolate profiles of two T-DNA insertion mutants of CB5C, and found that long-chained aliphatic glucosinolates were reduced in one of the mutant lines - a phenotype that was exaggerated upon methyl-jasmonate treatment. These results support the hypothesis, that CB5C influences glucosinolate biosynthesis, however, the mode of action remains unknown. Furthermore, the mutants differed in their biomass response to methyl jasmonate treatment. Thereby, our results highlight the varying effects of T-DNA insertion sites, as the two analyzed alleles show different phenotypes.

U2 - 10.1080/15592324.2016.1160189

DO - 10.1080/15592324.2016.1160189

M3 - Journal article

C2 - 27454255

VL - 11

JO - Plant Signalling & Behavior

JF - Plant Signalling & Behavior

SN - 1559-2316

IS - 8

M1 - e1160189

ER -

ID: 164887255