Regulatory protein complexes

We visualize the sub-cellular localization of proteins by transiently expressing fluorophore fusion proteins in tobacco.

Transcription factors regulate most cellular processes, a function they typically perform in protein complexes. The composition of these complexes determines their specificity towards defined sets of genes which are then coordinately transcribed and translated to proteins. To gain novel insight into the biological roles of transcription factors, it is crucial to understand the dynamics of transcription factor complexes their protein interaction networks.

Regulation of glucosinolate production from the amino acids methionine and tryptophan is controlled by six closely related and inter-dependent R2R3 MYB transcription factors. All of them can physically interact with three member s of the bHLH transcription factor family and the formation of these heterodimers is critical for the biosynthesis of glucosinolates.

We investigate the stoichiometry of the protein complexes that bind the promoters of glucosinolate biosynthetic genes to learn more about the impact of transcription factor complex composition on transcriptional regulation. In combination with these studies, we also explore the mechanisms underlying the sub-cellular localizations of glucosinolate regulatory proteins.


Millard PS, Weber K, Kragelund BB, Burow M (2019) Specificity of MYB interactions relies on motifs in ordered and disordered contexts. Nucleic Acid Research. DOI:10.1093/nar/gkz691.

Millard PS, Kragelund BB, Burow M (2019) R2R3 MYB Transcription Factors – Functions outside the DNA-Binding Domain. Trends in Plant Science. DOI:10.1016/j.tplants.2019.07.003.

Burow M, Atwell S, Francisco M, Kerwin RE, Halkier BA, Kliebenstein DJ (2015) The glucosinolate biosynthetic Gene AOP2 mediates feed-back regulation of jasmonic acid signaling in Arabidopsis. Mol Plant 8: 1201–1212. DOI:10.1016/j.molp.2015.03.001

Pireyre M, Burow M (2015) Regulation of MYB and bHLH transcription factors: a glance at the protein level. Mol Plant 8: 378–388. DOI:10.1016/j.molp.2014.11.022