The ALOG domain defines a family of plant-specific transcription factors acting during Arabidopsis flower development

Author:

Rieu Philippe1ORCID,Beretta Veronica Maria2ORCID,Caselli Francesca2ORCID,Thévénon Emmanuel1,Lucas Jérémy1ORCID,Rizk Mahmoud3ORCID,Franchini Emanuela2,Caporali Elisabetta2,Paleni Chiara2ORCID,Nanao Max H.3,Kater Martin M.2ORCID,Dumas Renaud1ORCID,Zubieta Chloe1,Parcy François1ORCID,Gregis Veronica2ORCID

Affiliation:

1. Laboratoire Physiologie Cellulaire et Végétale, Université Grenoble Alpes, Centre national de la recherche scientifique, Commissariat à l’énergie atomique et aux énergies alternatives, Institut national de recherche pour l’agriculture, l’alimentation et l’environnement, Département de Biologie Structurale et Cellulaire intégrée, Grenoble F-38054, France

2. Dipartimento di Bioscienze, Università degli Studi di Milano, Milano 20133, Italy

3. Structural Biology Group, European Synchrotron Radiation Facility, Grenoble 38000, France

Abstract

The ALOG (Arabidopsis LIGHT-DEPENDENT SHORT HYPOCOTYLS 1 (LSH1) and Oryza G1) proteins are conserved plant-specific Transcription Factors (TFs). They play critical roles in the development of various plant organs (meristems, inflorescences, floral organs, and nodules) from bryophytes to higher flowering plants. Despite the fact that the first members of this family were originally discovered in Arabidopsis, their role in this model plant has remained poorly characterized. Moreover, how these transcriptional regulators work at the molecular level is unknown. Here, we study the redundant function of the ALOG proteins LSH1,3,4 from Arabidopsis. We uncover their role in the repression of bract development and position them within a gene regulatory network controlling this process and involving the floral regulators LEAFY, BLADE-ON-PETIOLE, and PUCHI. Next, using in vitro genome-wide studies, we identified the conserved DNA motif bound by ALOG proteins from evolutionarily distant species (the liverwort Marchantia polymorpha and the flowering plants Arabidopsis, tomato, and rice). Resolution of the crystallographic structure of the ALOG DNA-binding domain in complex with DNA revealed the domain is a four-helix bundle with a disordered NLS and a zinc ribbon insertion between helices 2 and 3. The majority of DNA interactions are mediated by specific contacts made by the third alpha helix and the NLS. Taken together, this work provides the biochemical and structural basis for DNA-binding specificity of an evolutionarily conserved TF family and reveals its role as a key player in Arabidopsis flower development.

Funder

Agence Nationale de la Recherche

Ministero dell'Università e della Ricerca

Publisher

Proceedings of the National Academy of Sciences

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