CB5C affects the glucosinolate profile in Arabidopsis thaliana

Daniel Vik; Christoph Crocoll; Tonni Grube Andersen; Meike Burow; Barbara Ann Halkier

doi:10.1080/15592324.2016.1160189

CB5C affects the glucosinolate profile in Arabidopsis thaliana

Daniel Vik, Christoph Crocoll, Tonni Grube Andersen, Meike Burow, Barbara Ann Halkier

Section for Molecular Plant Biology

4 Citations (Scopus)

44 Downloads (Pure)

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 2 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 2 analyzed alleles show different phenotypes.

Original language	English
Article number	e1160189
Journal	Plant Signalling & Behavior
Volume	11
Issue number	8
Number of pages	6
ISSN	1559-2316
DOIs	https://doi.org/10.1080/15592324.2016.1160189
Publication status	Published - 2 Aug 2016

Access to Document

10.1080/15592324.2016.1160189Licence: CC BY

CB5C affects the glucosinolate profile in Arabidopsis thalianaFinal published version, 1.26 MBLicence: CC BY

Cite this

@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 2 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 2 analyzed alleles show different phenotypes.",

author = "Daniel Vik and Christoph Crocoll and Andersen, {Tonni Grube} and Meike Burow and Halkier, {Barbara Ann}",

year = "2016",

month = aug,

day = "2",

doi = "10.1080/15592324.2016.1160189",

language = "English",

volume = "11",

journal = "Plant Signalling & Behavior",

issn = "1559-2316",

publisher = "Taylor & Francis",

number = "8",

}

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 - 2016/8/2

Y1 - 2016/8/2

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 2 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 2 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 2 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 2 analyzed alleles show different phenotypes.

U2 - 10.1080/15592324.2016.1160189

DO - 10.1080/15592324.2016.1160189

M3 - Journal article

C2 - 27454255

SN - 1559-2316

VL - 11

JO - Plant Signalling & Behavior

JF - Plant Signalling & Behavior

IS - 8

M1 - e1160189

ER -

CB5C affects the glucosinolate profile in Arabidopsis thaliana

Abstract

Access to Document

Fingerprint

Cite this