Evolution of A bHLH Interaction Motif

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Evolution of A bHLH Interaction Motif. / Millard, Peter S.; Kragelund, Birthe B.; Burow, Meike.

I: International Journal of Molecular Sciences, Bind 22, Nr. 1, 447, 2021.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Millard, PS, Kragelund, BB & Burow, M 2021, 'Evolution of A bHLH Interaction Motif', International Journal of Molecular Sciences, bind 22, nr. 1, 447. https://doi.org/10.3390/ijms22010447

APA

Millard, P. S., Kragelund, B. B., & Burow, M. (2021). Evolution of A bHLH Interaction Motif. International Journal of Molecular Sciences, 22(1), [447]. https://doi.org/10.3390/ijms22010447

Vancouver

Millard PS, Kragelund BB, Burow M. Evolution of A bHLH Interaction Motif. International Journal of Molecular Sciences. 2021;22(1). 447. https://doi.org/10.3390/ijms22010447

Author

Millard, Peter S. ; Kragelund, Birthe B. ; Burow, Meike. / Evolution of A bHLH Interaction Motif. I: International Journal of Molecular Sciences. 2021 ; Bind 22, Nr. 1.

Bibtex

@article{7afacaaf8f934864b2f46bf09615b77f,
title = "Evolution of A bHLH Interaction Motif",
abstract = "Intrinsically disordered proteins and regions with their associated short linear motifs play key roles in transcriptional regulation. The disordered MYC-interaction motif (MIM) mediates interactions between MYC and MYB transcription factors in Arabidopsis thaliana that are critical for constitutive and induced glucosinolate (GLS) biosynthesis. GLSs comprise a class of plant defense compounds that evolved in the ancestor of the Brassicales order. We used a diverse set of search strategies to discover additional occurrences of the MIM in other proteins and in other organisms and evaluate the findings by means of structural predictions, interaction assays, and biophysical experiments. Our search revealed numerous MIM instances spread throughout the angiosperm lineage. Experiments verify that several of the newly discovered MIM-containing proteins interact with MYC TFs. Only hits found within the same transcription factor family and having similar characteristics could be validated, indicating that structural predictions and sequence similarity are good indicators of whether the presence of a MIM mediates interaction. The experimentally validated MIMs are found in organisms outside the Brassicales order, showing that MIM function is broader than regulating GLS biosynthesis.",
keywords = "MYB, bHLH, MYC, transcription factor, short linear motif (SLiM), intrinsically disordered protein (IDP), protein interaction, interaction motif, plant defense metabolism, jasmonate signaling",
author = "Millard, {Peter S.} and Kragelund, {Birthe B.} and Meike Burow",
year = "2021",
doi = "10.3390/ijms22010447",
language = "English",
volume = "22",
journal = "International Journal of Molecular Sciences (Online)",
issn = "1661-6596",
publisher = "MDPI AG",
number = "1",

}

RIS

TY - JOUR

T1 - Evolution of A bHLH Interaction Motif

AU - Millard, Peter S.

AU - Kragelund, Birthe B.

AU - Burow, Meike

PY - 2021

Y1 - 2021

N2 - Intrinsically disordered proteins and regions with their associated short linear motifs play key roles in transcriptional regulation. The disordered MYC-interaction motif (MIM) mediates interactions between MYC and MYB transcription factors in Arabidopsis thaliana that are critical for constitutive and induced glucosinolate (GLS) biosynthesis. GLSs comprise a class of plant defense compounds that evolved in the ancestor of the Brassicales order. We used a diverse set of search strategies to discover additional occurrences of the MIM in other proteins and in other organisms and evaluate the findings by means of structural predictions, interaction assays, and biophysical experiments. Our search revealed numerous MIM instances spread throughout the angiosperm lineage. Experiments verify that several of the newly discovered MIM-containing proteins interact with MYC TFs. Only hits found within the same transcription factor family and having similar characteristics could be validated, indicating that structural predictions and sequence similarity are good indicators of whether the presence of a MIM mediates interaction. The experimentally validated MIMs are found in organisms outside the Brassicales order, showing that MIM function is broader than regulating GLS biosynthesis.

AB - Intrinsically disordered proteins and regions with their associated short linear motifs play key roles in transcriptional regulation. The disordered MYC-interaction motif (MIM) mediates interactions between MYC and MYB transcription factors in Arabidopsis thaliana that are critical for constitutive and induced glucosinolate (GLS) biosynthesis. GLSs comprise a class of plant defense compounds that evolved in the ancestor of the Brassicales order. We used a diverse set of search strategies to discover additional occurrences of the MIM in other proteins and in other organisms and evaluate the findings by means of structural predictions, interaction assays, and biophysical experiments. Our search revealed numerous MIM instances spread throughout the angiosperm lineage. Experiments verify that several of the newly discovered MIM-containing proteins interact with MYC TFs. Only hits found within the same transcription factor family and having similar characteristics could be validated, indicating that structural predictions and sequence similarity are good indicators of whether the presence of a MIM mediates interaction. The experimentally validated MIMs are found in organisms outside the Brassicales order, showing that MIM function is broader than regulating GLS biosynthesis.

KW - MYB

KW - bHLH

KW - MYC

KW - transcription factor

KW - short linear motif (SLiM)

KW - intrinsically disordered protein (IDP)

KW - protein interaction

KW - interaction motif

KW - plant defense metabolism

KW - jasmonate signaling

U2 - 10.3390/ijms22010447

DO - 10.3390/ijms22010447

M3 - Journal article

C2 - 33466276

VL - 22

JO - International Journal of Molecular Sciences (Online)

JF - International Journal of Molecular Sciences (Online)

SN - 1661-6596

IS - 1

M1 - 447

ER -

ID: 255692230