Gibberellin (GA) regulates plant development primarily by triggering the degradation/deactivation of the DELLA proteins. However, it remains unclear whether all GA responses are regulated by DELLAs. Tomato (Solanum lycopersicum) has a single DELLA gene named PROCERA (PRO), and its recessive pro allele exhibits constitutive GA activity but retains responsiveness to external GA. In the loss-of-function mutant pro DGRAS , all examined GA developmental responses were considerably enhanced relative to pro and a defect in seed desiccation tolerance was uncovered. As pro, but not pro DGRAS , elongation was promoted by GA treatment, pro may retain residual DELLA activity. In agreement with homeostatic feedback regulation of the GA biosynthetic pathway, we found that GA20oxidase1 expression was suppressed in pro DGRAS and was not affected by exogenous GA 3 . In contrast, expression of GA2oxidase4 was not affected by the elevated GA signaling in pro DGRAS but was strongly induced by exogenous GA 3 . Since a similar response was found in Arabidopsis thaliana plants with impaired activity of all five DELLA genes, we suggest that homeostatic GA responses are regulated by both DELLA-dependent and -independent pathways. Transcriptome analysis of GA-treated pro DGRAS leaves suggests that 5% of all GA-regulated genes in tomato are DELLA independent.
INTRODUCTIONThe phytohormone gibberellin (GA) regulates numerous developmental processes throughout the plant life cycle, including seed germination, stem elongation, flowering, and fruit set (Yamaguchi, 2008). The signaling pathway from GA perception to transcriptional activation has been intensively studied over the past two decades and its major components have been identified. The nuclear DELLA proteins, a subgroup of the GRAS transcription factors family, suppress GA signaling (Locascio et al., 2013). GA binding to the soluble GIBBERELLIN INSENSITIVE DWARF1 (GID1) receptor triggers GID1 interaction with the DELLA proteins (Ueguchi-Tanaka et al., 2005;Nakajima et al., 2006;Griffiths et al., 2006), which then stimulates assembly of the DELLA proteins into an SCF E3 ubiquitin ligase complex via the GID2/SLEEPY1 F-box proteins. The SCF complex polyubiquitinates the DELLA proteins, targeting them for destruction by the 26S proteosome (Sasaki et al., 2003;Dill et al., 2004;Griffiths et al., 2006;Harberd et al., 2009;Hauvermale et al., 2012). GA, via GID1, can also reduce DELLA activity through a degradation-independent mechanism (Ariizumi et al., , 2013Ueguchi-Tanaka et al., 2008).Despite the central role of DELLAs in GA signaling, the mechanism underlying this regulation is not fully understood. Several studies have shown that protein-protein interactions play a major role in DELLA function. DELLAs bind to various transcription factors and proteins affecting transcription, including PHYTOCHROME-INTERACTING FACTORs (PIFs), ALCATRAZ, MYC2, JASMONATE-ZIM-DOMAIN PROTEIN9, SCARECROW LIKE3 (SCL3), and TCP transcription factors (de Lucas et al., 2008;Feng et al., 2008;Arnaud et al., 2010;Ga...