SUMO proteases ULP1c and ULP1d are required for development and osmotic stress responses in Arabidopsis thaliana View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2016-09

AUTHORS

Pedro Humberto Castro, Daniel Couto, Sara Freitas, Nuno Verde, Alberto P. Macho, Stéphanie Huguet, Miguel Angel Botella, Javier Ruiz-Albert, Rui Manuel Tavares, Eduardo Rodríguez Bejarano, Herlânder Azevedo

ABSTRACT

Sumoylation is an essential post-translational regulator of plant development and the response to environmental stimuli. SUMO conjugation occurs via an E1-E2-E3 cascade, and can be removed by SUMO proteases (ULPs). ULPs are numerous and likely to function as sources of specificity within the pathway, yet most ULPs remain functionally unresolved. In this report we used loss-of-function reverse genetics and transcriptomics to functionally characterize Arabidopsis thaliana ULP1c and ULP1d SUMO proteases. GUS reporter assays implicated ULP1c/d in various developmental stages, and subsequent defects in growth and germination were uncovered using loss-of-function mutants. Microarray analysis evidenced not only a deregulation of genes involved in development, but also in genes controlled by various drought-associated transcriptional regulators. We demonstrated that ulp1c ulp1d displayed diminished in vitro root growth under low water potential and higher stomatal aperture, yet leaf transpirational water loss and whole drought tolerance were not significantly altered. Generation of a triple siz1 ulp1c ulp1d mutant suggests that ULP1c/d and the SUMO E3 ligase SIZ1 may display separate functions in development yet operate epistatically in response to water deficit. We provide experimental evidence that Arabidopsis ULP1c and ULP1d proteases act redundantly as positive regulators of growth, and operate mainly as isopeptidases downstream of SIZ1 in the control of water deficit responses. More... »

PAGES

143-159

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s11103-016-0500-9

DOI

http://dx.doi.org/10.1007/s11103-016-0500-9

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1051834832

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27325215


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