RESUMEN
Plant organs often grow into a genetically determined size and shape. How organ growth is finely regulated to achieve a well defined pattern is a fascinating, but largely unresolved, question in plant research. We utilised the Arabidopsis petal to study the genetic control of plant organ growth, and identify two closely related U-box E3 ligases PUB25 and PUB26 as important growth regulators by screening the targets of the petal-specific growth-promoting transcription factor RABBIT EARS (RBE). We showed that PUB25 is directly controlled by RBE in petal development in a spatial- and temporal-specific manner and acts as a major target to mediate RBE's function in petal growth. We also showed that PUB25 and PUB26 repress petal growth by restricting the period of cell proliferation, and their regulation appears to be independent of other plant E3 ligase genes implicated in growth control. PUB25 and PUB26 are among the first U-box E3 ligases shown to function in plant growth control. Furthermore, as they were also found to play a vital role in plant stress responses, PUB25 and PUB26 may act as a key hub to integrate developmental and environmental signals for balancing growth and defence in plants.
Asunto(s)
Proteínas de Arabidopsis , Arabidopsis , Arabidopsis/genética , Arabidopsis/metabolismo , Proteínas de Arabidopsis/genética , Proteínas de Arabidopsis/metabolismo , Regulación de la Expresión Génica de las Plantas , Factores de Transcripción/metabolismo , Ubiquitina-Proteína Ligasas/genética , Ubiquitina-Proteína Ligasas/metabolismoRESUMEN
The actin cytoskeleton plays pivotal roles in pollen tube growth by regulating organelle movement, cytoplasmic streaming, and vesicle trafficking. Previous studies have reported that plasma membrane-localized phospholipase Dδ (PLDδ) binds to cortical microtubules and negatively regulates plant stress tolerance. However, it remains unknown whether or how PLDδ regulates microfilament organization. In this study, we found that loss of PLDδ function led to a significant increase in pollen tube growth, whereas PLDδ overexpression resulted in pollen tube growth inhibition. We also found that wild-type PLDδ, rather than Arg 622-mutated PLDδ, complemented the pldδ phenotype in pollen tubes. In vitro biochemical assays demonstrated that PLDδ binds directly to F-actin, and immunofluorescence assays revealed that PLDδ in pollen tubes influences actin organization. Together, these results suggest that PLDδ participates in the development of pollen tube growth by organizing actin filaments.