scholarly journals Correction: Rational design of a stapled JAZ9 peptide inhibiting protein–protein interaction of a plant transcription factor

2021 ◽  
Author(s):  
Kaho Suzuki ◽  
Yousuke Takaoka ◽  
Minoru Ueda
Keyword(s):  
Transcription Factor ◽  
Protein Interaction ◽  
Rational Design ◽  
Protein Protein Interaction ◽  
Inhibiting Protein

Correction for ‘Rational design of a stapled JAZ9 peptide inhibiting protein–protein interaction of a plant transcription factor’ by Kaho Suzuki et al., RSC Chem. Biol., 2021, DOI: 10.1039/d0cb00204f.

scholarly journals Rational design of a stapled JAZ9 peptide inhibiting protein–protein interaction of a plant transcription factor

2021 ◽  
Author(s):  
Kaho Suzuki ◽  
Yousuke Takaoka ◽  
Minoru Ueda
Keyword(s):  
Arabidopsis Thaliana ◽  
Transcription Factor ◽  
Protein Interaction ◽  
Rational Design ◽  
Master Regulators ◽  
Jasmonate Signaling ◽  
Protein Protein Interaction ◽  
Inhibiting Protein

A rationally designed stapled JAZ peptide selectively inhibited MYCs, master-regulators of the jasmonate signaling in Arabidopsis thaliana. It is proposed as a novel chemical tool for the analysis of MYC related jasmonate signaling.

In Silico Approaches Assisting the Rational Design of Low Molecular Weight Protein–Protein Interaction Modulators

2015 ◽  
pp. 441-482
Author(s):  
Bruno Villoutreix ◽  
Melaine Kuenemann ◽  
David Lagorce ◽  
Olivier Sperandio ◽  
Maria Miteva
Keyword(s):  
Molecular Weight ◽  
Protein Interaction ◽  
In Silico ◽  
Rational Design ◽  
Low Molecular Weight ◽  
Molecular Weight Protein ◽  
Protein Protein Interaction ◽  
Weight Protein ◽  
Low Molecular Weight Protein

The activated glucocorticoid receptor inhibits the transcription factor T‐bet by direct protein‐protein interaction

2007 ◽  
Vol 21 (4) ◽  
pp. 1177-1188 ◽  
Author(s):  
Ana C. Liberman ◽  
Damian Refojo ◽  
Jimena Druker ◽  
Marta Toscano ◽  
Theo Rein ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Glucocorticoid Receptor ◽  
Protein Interaction ◽  
Protein Protein Interaction

Rational Design, Synthesis and Evaluation of Coumarin Derivatives as Protein-protein Interaction Inhibitors

2016 ◽  
Vol 35 (8-9) ◽  
pp. 460-473 ◽  
Author(s):  
Laura De Luca ◽  
Fatima E. Agharbaoui ◽  
Rosaria Gitto ◽  
Maria Rosa Buemi ◽  
Frauke Christ ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Rational Design ◽  
Coumarin Derivatives ◽  
Design Synthesis ◽  
Protein Protein Interaction

scholarly journals The TCP transcription factor HvTB2 heterodimerizes with VRS5(HvTB1) and controls spike architecture in barley

2021 ◽  
Author(s):  
Tatiana de Souza Moraes ◽  
Sam W. van Es ◽  
Inmaculada Hernández-Pinzón ◽  
Gwendolyn K. Kirschner ◽  
Froukje van der Wal ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Protein Interaction ◽  
Protein Interactions ◽  
Plant Architecture ◽  
Transcriptional Regulators ◽  
Class Ii ◽  
Barley Plant ◽  
Cereal Crop ◽  
Protein Protein Interactions ◽  
Protein Protein Interaction

AbstractBarley is the fourth largest cereal crop grown worldwide, and essential for food and feed production. Phenotypically, the barley spike, which is unbranched, occurs in two main architectural shapes: two-rowed or six-rowed. In the 6-rowed cultivars, all three florets of the triple floret meristem develop into seeds while in 2-rowed lines only the central floret forms a seed. VRS5(HvTB1), act as inhibitor of lateral seed outgrowth and vrs5(hvtb1) mutants display a six-rowed spike architecture. VRS5(HvTB1) is a member of the TCP transcription factor (TF) family, which often form protein-protein interactions with other transcriptional regulators to modulate the expression of their target genes.Despite the key role of VRS5(HvTB1) in regulating barley plant architecture, there is hardly any knowledge on its molecular mode-of-action. We performed an extensive phylogenetic analysis of the TCP transcription factor family, followed by an in-vitro protein-protein interaction study using yeast-two-hybrid. Our analysis shows that VRS5(HvTB1) has a diverse interaction capacity, interacting with class II TCP’s, NF-Y TF, but also chromatin modellers. Further analysis of the interaction capacity of VRS5(HvTB1) with other TCP TFs shows that VRS5(HvTB1) preferably interacts with other class II TCP TFs within the TB1 clade. One of these interactors, encoded by HvTB2, shows a similar expression pattern when compared to VRS5(HvTB1). Haplotype analysis of HvTB2 suggest that this gene is highly conserved and shows hardly any variation in cultivars or wild barley. Induced mutations in HvTB2 trough CRISPR-CAS9 mutagenesis in cv. Golden Promise resulted in barley plants that lost their characteristic unbranched spike architecture. hvtb2 mutants exhibited branches arising at the main spike, suggesting that, similar to VRS5(HvTB1), HvTB2 act as inhibitor of branching. Taken together, our protein-protein interaction studies of VRS5(HvTB1) resulted in the identification of HvTB2, another key regulator of spike architecture in barley. Understanding the molecular network, including protein-protein interactions, of key regulators of plant architecture such as VRS5(HvTB1) provide new routes towards the identification of other key regulators of plant architecture in barley.Author summaryTranscriptional regulation is one of the basic molecular processes that drives plant growth and development. The key TCP transcriptional regulator TEOSINTE BRANCHED 1 (TB1) is one of these key regulators that has been targeted during domestication of several crops for its role as modulator of branching. Also in barley, a key cereal crop, HvTB1 (also referred to as VRS5), inhibits the outgrowth or side shoots, or tillers, and seeds. Despite its key role in barley development, there is hardly any knowledge on the molecular network that is utilized by VRS5(HvTB1). Transcriptional regulators form homo- and heterodimers to regulate the expression of their downstream targets. Here, we performed an extensive phylogenetic analysis of TCP transcription factors (TFs) in barley, followed by protein-protein interaction studies of VRS5(HvTB1). Our analysis indicates, that VRS5(HvTB1) has a diverse capacity of interacting with class II TCPs, NF-Y TF, but also chromatin modellers. Induced mutagenesis trough CRISPR-CAS mutagenesis of one of the putative VRS5(HvTB1) interactors, HvTB2, resulted in barley plants with branched spikes. This shows that insight into the VRS5(HvTB1) interactome, followed by detailed functional analysis of potential interactors is essential to truly understand how TCPs modulate plant architecture. The study presented here provides a first step to underpin the protein-protein interactome of VRS5(HvTB1) and identify other, yet unknown, key regulators of barley plant architecture.

A direct protein‐protein interaction is involved in the cooperation between thyroid hormone and retinoic acid receptors and the transcription factor GHF‐1

1998 ◽  
Vol 12 (12) ◽  
pp. 1201-1209 ◽  
Author(s):  
Teresa Palomino ◽  
Aurora Sánchez‐Pacheco ◽  
Pilar Peña ◽  
Ana Aranda
Keyword(s):  
Transcription Factor ◽  
Retinoic Acid ◽  
Thyroid Hormone ◽  
Protein Interaction ◽  
Retinoic Acid Receptors ◽  
Protein Protein Interaction

Functional interference between the ubiquitous and constitutive octamer transcription factor 1 (OTF-1) and the glucocorticoid receptor by direct protein-protein interaction involving the homeo subdomain of OTF-1

1992 ◽  
Vol 12 (11) ◽  
pp. 4960-4969
Author(s):  
E Kutoh ◽  
P E Strömstedt ◽  
L Poellinger
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Glucocorticoid Receptor ◽  
Protein Interaction ◽  
Binding Activity ◽  
Dependent Manner ◽  
Protein Protein Interaction ◽  
Dna Binding Activity ◽  
Functional Interference

The ubiquitous and constitutive octamer transcription factor OTF-1 (Oct 1) is the target of positive regulation by the potent herpes simplex virus trans-activator VP16, which forms a complex with the homeodomain of OTF-1. Here we present evidence that the glucocorticoid receptor can negatively regulate OTF-1 function by a mechanism that is independent of DNA binding. In vivo-expressed glucocorticoid receptor inhibited in a hormone-dependent manner activation of a minimal promoter construct carrying a functional octamer site. Moreover, expression of the receptor in vivo resulted in hormone-dependent repression of OTF-1-dependent DNA-binding activity in nuclear extract. In vitro, the DNA-binding activity of partially purified OTF-1 was repressed following incubation with purified glucocorticoid receptor. Cross-linking and immunoprecipitation experiments indicated that the functional interference may be due to a strong association between these two proteins in solution. Finally, preliminary evidence indicates that the homeo subdomain of OTF-1 that directs formation of a complex with VP16 may also be critical for interaction with the glucocorticoid receptor. Thus, OTF-1 is a target for both positive and negative regulation by protein-protein interaction. Moreover, the functional interference between OTF-1 and the glucocorticoid receptor represents a novel regulatory mechanism in the cross-coupling of signal transduction pathways of nuclear receptors and constitutive transcription factors.

Transcription Factor E2 Regulates BPV-1 DNA Replication In Vitro by Direct Protein-Protein Interaction

1991 ◽  
Vol 56 (0) ◽  
pp. 335-346 ◽  
Author(s):  
L. Yang ◽  
I. Mohr ◽  
R. Li ◽  
T. Nottoli ◽  
S. Sun ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Dna Replication ◽  
Protein Interaction ◽  
Protein Protein Interaction
Sign in / Sign up

Export Citation Format

Share Document