Dataset Information

PAT1-type GRAS-domain proteins control regeneration following wounding by transcriptional activation of DOF3.4 driving cell proliferation

ABSTRACT: Plant roots possess a remarkable regenerative potential owing to the presence of stem cells that constantly generate new tissues. Key molecular mechanisms have been linked to this potential, among which the ETHYLENE RESPONSE FACTOR 115 (ERF115) that plays a predominant role in the activation of regenerative cell divisions. However, the downstream operating molecular machinery driving wound-activated cell divisions is largely unknown. Here, we biochemically and genetically identified the GRAS-domain transcription factor protein SCARECROW-LIKE 5 (SCL5) as an interaction partner of ERF115. Although being non-essential under control growth conditions, SCL5 drives redundantly with the related PAT1 and SCL21 transcription factors the expression of the DNA-BINDING ONE FINGER 3.4 (DOF3;4) transcription factor gene. DOF3.4 expression is wound inducible and ERF115 dependent, and in turn activates D3-type cyclin expression. Accordingly, ectopic DOF3.4 expression drives periclinal cell division, whereas its downstream D3-type cyclins are essential for regeneration. The data highlight the importance of the PAT1-branch of GRAS-domain transcription factors for wound activated regeneration processes and pinpoint the DOF3.4 transcription factor as a key element driving regenerative cell divisions.

ORGANISM(S): Arabidopsis thaliana

PROVIDER: GSE200500 | GEO | 2023/04/26

REPOSITORIES: GEO

ACCESS DATA

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Project description:In eukaryotes, chromosomal DNA is equally distributed to daughter cells during mitosis, whereas the number of chromosomes is halved during meiosis. Despite considerable progress in understanding the molecular mechanisms that regulate mitosis, there is currently a lack of complete understanding of the molecular mechanisms regulating meiosis. Here, we took advantage of the fission yeast Schizosaccharomyces pombe, for which highly synchronous meiosis can be induced, and performed quantitative proteomics and phosphoproteomics analyses to track changes in protein expression and phosphorylation during meiotic cell divisions. We compared the proteomes and phosphoproteomes of mitotic cells with cells harvested around meiosis I, or meiosis II in strains bearing either the temperature-sensitive pat1-114 allele or conditional ATP analog-sensitive pat1-as2 allele of the Pat1 kinase. Comparing pat1-114 with pat1-as2 also allowed us to investigate the impact of elevated temperature (25°C versus 34°C) on meiosis, an issue that sexually reproducing organisms face due to climate change. Using TMTpro 18plex labeling and phosphopeptide enrichment strategies, we performed quantification of a total of 4673 proteins and 7172 phosphosites in S. pombe. We found that the protein level of 2680 proteins and the rate of phosphorylation of 4005 phosphosites significantly changed during progression of S. pombe cells through meiosis. The proteins exhibiting changes in expression and phosphorylation during meiotic cell divisions were represented mainly by those involved in the meiotic cell cycle, meiotic recombination, meiotic nuclear division, meiosis I, centromere clustering, microtubule cytoskeleton organization, ascospore formation, organonitrogen compound biosynthetic process, carboxylic acid metabolic process, gene expression, and ncRNA processing, among others. In summary, our findings provide global overview of changes in the levels and phosphorylation of proteins during progression of S. pombe cells through meiosis at normal and elevated temperatures, laying the groundwork for further elucidation of the functions and importance of specific proteins and their phosphorylation in regulating meiotic cell divisions in this yeast.

Dataset Information

PAT1-type GRAS-domain proteins control regeneration following wounding by transcriptional activation of DOF3.4 driving cell proliferation

Dataset's files

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets