共查询到20条相似文献,搜索用时 31 毫秒
1.
The Arabidopsis F-box protein SLEEPY1 targets gibberellin signaling repressors for gibberellin-induced degradation 总被引:20,自引:0,他引:20
The nuclear DELLA proteins are highly conserved repressors of hormone gibberellin (GA) signaling in plants. In Arabidopsis thaliana, GA derepresses its signaling pathway by inducing proteolysis of the DELLA protein REPRESSOR OF ga1-3 (RGA). SLEEPY1 (SLY1) encodes an F-box-containing protein, and the loss-of-function sly1 mutant has a GA-insensitive dwarf phenotype and accumulates a high level of RGA. These findings suggested that SLY1 recruits RGA to the SCFSLY1 E3 ligase complex for ubiquitination and subsequent degradation by the 26S proteasome. In this report, we provide new insight into the molecular mechanism of how SLY1 interacts with the DELLA proteins for controlling GA response. By yeast two-hybrid and in vitro pull-down assays, we demonstrated that SLY1 interacts directly with RGA and GA INSENSITIVE (GAI, a closely related DELLA protein) via their C-terminal GRAS domain. The rga and gai null mutations additively suppressed the recessive sly1 mutant phenotype, further supporting the model that SCFSLY1 targets both RGA and GAI for degradation. The N-terminal DELLA domain of RGA previously was shown to be essential for GA-induced degradation. However, we found that this DELLA domain is not required for protein-protein interaction with SLY1 in yeast (Saccharomyces cerevisiae), suggesting that its role is in a GA-triggered conformational change of the DELLA proteins. We also identified a novel gain-of-function sly1-d mutation that increased GA signaling by reducing the levels of the DELLA protein in plants. This effect of sly1-d appears to be caused by an enhanced interaction between sly1-d and the DELLA proteins. 相似文献
2.
Proteolysis-independent downregulation of DELLA repression in Arabidopsis by the gibberellin receptor GIBBERELLIN INSENSITIVE DWARF1 总被引:3,自引:0,他引:3
This article presents evidence that DELLA repression of gibberellin (GA) signaling is relieved both by proteolysis-dependent and -independent pathways in Arabidopsis thaliana. DELLA proteins are negative regulators of GA responses, including seed germination, stem elongation, and fertility. GA stimulates GA responses by causing DELLA repressor degradation via the ubiquitin-proteasome pathway. DELLA degradation requires GA biosynthesis, three functionally redundant GA receptors GIBBERELLIN INSENSITIVE DWARF1 (GID1a, b, and c), and the SLEEPY1 (SLY1) F-box subunit of an SCF E3 ubiquitin ligase. The sly1 mutants accumulate more DELLA proteins but display less severe dwarf and germination phenotypes than the GA biosynthesis mutant ga1-3 or the gid1abc triple mutant. Interestingly, GID1 overexpression rescued the sly1 dwarf and infertility phenotypes without decreasing the accumulation of the DELLA protein REPRESSOR OF ga1-3. GID1 rescue of sly1 mutants was dependent on the level of GID1 protein, GA, and the presence of a functional DELLA motif. Since DELLA shows increasing interaction with GID1 with increasing GA levels, it appears that GA-bound GID1 can block DELLA repressor activity by direct protein-protein interaction with the DELLA domain. Thus, a SLY1-independent mechanism for GA signaling may function without DELLA degradation. 相似文献
3.
The role of two f-box proteins, SLEEPY1 and SNEEZY, in Arabidopsis gibberellin signaling 总被引:4,自引:0,他引:4
The SLEEPY1 (SLY1) F-box gene is a positive regulator of gibberellin (GA) signaling in Arabidopsis (Arabidopsis thaliana). Loss of SLY1 results in GA-insensitive phenotypes including dwarfism, reduced fertility, delayed flowering, and increased seed dormancy. These sly1 phenotypes are partially rescued by overexpression of the SLY1 homolog SNEEZY (SNE)/SLY2, suggesting that SNE can functionally replace SLY1. GA responses are repressed by DELLA family proteins. GA relieves DELLA repression when the SCF(SLY1) (for Skp1, Cullin, F-box) E3 ubiquitin ligase ubiquitinates DELLA protein, thereby targeting it for proteolysis. Coimmunoprecipitation experiments using constitutively expressed 35S:hemagglutinin (HA)-SLY1 and 35S:HA-SNE translational fusions in the sly1-10 background suggest that SNE can function similarly to SLY1 in GA signaling. Like HA-SLY1, HA-SNE interacted with the CULLIN1 subunit of the SCF complex, and this interaction required the F-box domain. Like HA-SLY1, HA-SNE coimmunoprecipitated with the DELLA REPRESSOR OF GA1-3 (RGA), and this interaction required the SLY1 or SNE carboxyl-terminal domain. Whereas HA-SLY1 overexpression resulted in a decrease in both DELLA RGA and RGA-LIKE2 (RGL2) protein levels, HA-SNE caused a decrease in DELLA RGA but not in RGL2 levels. This suggests that one reason HA-SLY1 is able to effect a stronger rescue of sly1-10 phenotypes than HA-SNE is because SLY1 regulates a broader spectrum of DELLA proteins. The FLAG-SLY1 fusion protein was found to coimmunoprecipitate with the GA receptor HA-GA-INSENSITIVE DWARF1b (GID1b), supporting the model that SLY1 regulates DELLA through interaction with the DELLA-GA-GID1 complex. 相似文献
4.
Seed germination of GA-insensitive sleepy1 mutants does not require RGL2 protein disappearance in Arabidopsis
下载免费PDF全文
![点击此处可从《The Plant cell》网站下载免费的PDF全文](/ch/ext_images/free.gif)
We explore the roles of gibberellin (GA) signaling genes SLEEPY1 (SLY1) and RGA-LIKE2 (RGL2) in regulation of seed germination in Arabidopsis thaliana, a plant in which the hormone GA is required for seed germination. Seed germination failure in the GA biosynthesis mutant ga1-3 is rescued by GA and by mutations in the DELLA gene RGL2, suggesting that RGL2 represses seed germination. RGL2 protein disappears before wild-type seed germination, consistent with the model that GA stimulates germination by causing the SCF(SLY1) E3 ubiquitin ligase complex to trigger ubiquitination and destruction of RGL2. Unlike ga1-3, the GA-insensitive sly1 mutants show variable seed dormancy. Seed lots with high seed dormancy after-ripened slowly, with stronger alleles requiring more time. We expected that if RGL2 negatively controls seed germination, sly1 mutant seeds that germinate well should accumulate lower RGL2 levels than those failing to germinate. Surprisingly, RGL2 accumulated at high levels even in after-ripened sly1 mutant seeds with 100% germination, suggesting that RGL2 disappearance is not a prerequisite for seed germination in the sly1 background. Without GA, several GA-induced genes show increased accumulation in sly1 seeds compared with ga1-3. It is possible that the RGL2 repressor of seed germination is inactivated by after-ripening of sly1 mutant seeds. 相似文献
5.
Step-by-step acquisition of the gibberellin-DELLA growth-regulatory mechanism during land-plant evolution 总被引:6,自引:1,他引:5
Angiosperms (flowering plants) evolved relatively recently and are substantially diverged from early land plants (bryophytes, lycophytes, and others [1]). The phytohormone gibberellin (GA) adaptively regulates angiosperm growth via the GA-DELLA signaling mechanism [2-7]. GA binds to GA receptors (GID1s), thus stimulating interactions between GID1s and the growth-repressing DELLAs [8-12]. Subsequent 26S proteasome-mediated destruction of the DELLAs promotes growth [13-17]. Here we outline the evolution of the GA-DELLA mechanism. We show that the interaction between GID1 and DELLA components from Selaginella kraussiana (a lycophyte) is GA stimulated. In contrast, GID1-like (GLP1) and DELLA components from Physcomitrella patens (a bryophyte) do not interact, suggesting that GA-stimulated GID1-DELLA interactions arose in the land-plant lineage after the bryophyte divergence ( approximately 430 million years ago [1]). We further show that a DELLA-deficient P. patens mutant strain lacks the derepressed growth characteristic of DELLA-deficient angiosperms, and that both S. kraussiana and P. patens lack detectable growth responses to GA. These observations indicate that early land-plant DELLAs do not repress growth in situ. However, S. kraussiana and P. patens DELLAs function as growth-repressors when expressed in the angiosperm Arabidopsis thaliana. We conclude that the GA-DELLA growth-regulatory mechanism arose during land-plant evolution and via independent stepwise recruitment of GA-stimulated GID1-DELLA interaction and DELLA growth-repression functions. 相似文献
6.
The Arabidopsis SLEEPY1 gene encodes a putative F-box subunit of an SCF E3 ubiquitin ligase 总被引:19,自引:0,他引:19
下载免费PDF全文
![点击此处可从《The Plant cell》网站下载免费的PDF全文](/ch/ext_images/free.gif)
McGinnis KM Thomas SG Soule JD Strader LC Zale JM Sun TP Steber CM 《The Plant cell》2003,15(5):1120-1130
The Arabidopsis SLY1 (SLEEPY1) gene positively regulates gibberellin (GA) signaling. Positional cloning of SLY1 revealed that it encodes a putative F-box protein. This result suggests that SLY1 is the F-box subunit of an SCF E3 ubiquitin ligase that regulates GA responses. The DELLA domain protein RGA (repressor of ga1-3) is a repressor of GA response that appears to undergo GA-stimulated protein degradation. RGA is a potential substrate of SLY1, because sly1 mutations cause a significant increase in RGA protein accumulation even after GA treatment. This result suggests SCF(SLY1)-targeted degradation of RGA through the 26S proteasome pathway. Further support for this model is provided by the observation that an rga null allele partially suppresses the sly1-10 mutant phenotype. The predicted SLY1 amino acid sequence is highly conserved among plants, indicating a key role in GA response. 相似文献
7.
Sheerin DJ Buchanan J Kirk C Harvey D Sun X Spagnuolo J Li S Liu T Woods VA Foster T Jones WT Rakonjac J 《The Biochemical journal》2011,435(3):629-639
The phytohormone gibberellin and the DELLA proteins act together to control key aspects of plant development. Gibberellin induces degradation of DELLA proteins by recruitment of an F-box protein using a molecular switch: a gibberellin-bound nuclear receptor interacts with the N-terminal domain of DELLA proteins, and this event primes the DELLA C-terminal domain for interaction with the F-box protein. However, the mechanism of signalling between the N- and C-terminal domains of DELLA proteins is unresolved. In the present study, we used in vivo and in vitro approaches to characterize di- and tri-partite interactions of the DELLA protein RGL1 (REPRESSOR OF GA1-3-LIKE 1) of Arabidopsis thaliana with the gibberellin receptor GID1A (GIBBERELLIC ACID-INSENSITIVE DWARF-1A) and the F-box protein SLY1 (SLEEPY1). Deuterium-exchange MS unequivocally showed that the entire N-terminal domain of RGL1 is disordered prior to interaction with the GID1A; furthermore, association/dissociation kinetics, determined by surface plasmon resonance, predicts a two-state conformational change of the RGL1 N-terminal domain upon interaction with GID1A. Additionally, competition assays with monoclonal antibodies revealed that contacts mediated by the short helix Asp-Glu-Leu-Leu of the hallmark DELLA motif are not essential for the GID1A-RGL1 N-terminal domain interaction. Finally, yeast two- and three-hybrid experiments determined that unabated communication between N- and C-terminal domains of RGL1 is required for recruitment of the F-box protein SLY1. 相似文献
8.
The molecular mechanism and evolution of the GA-GID1-DELLA signaling module in plants 总被引:1,自引:0,他引:1
Sun TP 《Current biology : CB》2011,21(9):R338-R345
Bioactive gibberellins (GAs) are diterpene phytohormones that modulate growth and development throughout the whole life cycle of the flowering plant. Impressive advances have been made in elucidating the GA pathway with the cloning and characterization of genes encoding most GA biosynthesis and catabolism enzymes, GA receptors (GIBBERELLIN INSENSITIVE DWARF1, GID1) and early GA signaling components. Recent biochemical, genetic and structural analyses demonstrate that GA de-represses its signaling pathway by GID1-induced degradation of DELLA proteins, which are master growth repressors, via a ubiquitin-proteasome pathway. Multiple endogenous signals and environmental cues also interact with the GA-GID1-DELLA regulatory module by affecting the expression of GA metabolism genes, and hence GA content and DELLA levels. Importantly, DELLA integrates different signaling activities by direct protein-protein interaction with multiple key regulatory proteins from other pathways. Comparative studies suggest that the functional GA-GID1-DELLA module is highly conserved among vascular plants, but not in the bryophytes. Interestingly, differentiation of the moss Physcomitrella patens is regulated by as yet unidentified ent-kaurene-derived diterpenes, which are distinct from the common active GAs in vascular plants. 相似文献
9.
10.
11.
Gibberellins (GAs) play important roles in many essential plant growth and development processes. A family of nuclear growth-repressing DELLA proteins is the key component in GA signaling. GA perception is mediated by GID1, and the key event of GA signaling is the degradation of DELLA proteins via the 26S proteasome pathway. DELLA proteins integrating other plant hormones signaling and environmental cue modulating plant growth and development have been revealed. GA turning on the de-DELLA-repressing system is conserved, and independently establishes step-by-step recruitment of GAstimulated GID1-DELLA interaction and DELLA growth-repression functions during land plant evolution. These discoveries open new prospects for the understanding of GA action and DELLA-mediated signaling in plants. 相似文献
12.
The yeast SLY gene products, suppressors of defects in the essential GTP-binding Ypt1 protein, may act in endoplasmic reticulum-to-Golgi transport. 总被引:25,自引:3,他引:22
下载免费PDF全文
![点击此处可从《Molecular and cellular biology》网站下载免费的PDF全文](/ch/ext_images/free.gif)
R Ossig C Dascher H H Trepte H D Schmitt D Gallwitz 《Molecular and cellular biology》1991,11(6):2980-2993
It has been shown previously that defects in the essential GTP-binding protein, Ypt1p, lead to a block in protein transport from the endoplasmic reticulum (ER) to the Golgi apparatus in the yeast Saccharomyces cerevisiae. Here we report that four newly discovered suppressors of YPT1 deletion (SLY1-20, SLY2, SLY12, and SLY41) to a varying degree restore ER-to-Golgi transport defects in cells lacking Ypt1p. These suppressors also partially complement the sec21-1 and sec22-3 mutants which lead to a defect early in the secretory pathway. Sly1p-depleted cells, as well as a conditional lethal sly2 null mutant at nonpermissive temperatures, accumulate ER membranes and core-glycosylated invertase and carboxypeptidase Y. The sly2 null mutant under restrictive conditions (37 degrees C) can be rescued by the multicopy suppressor SLY12 and the single-copy suppressor SLY1-20, indicating that these three SLY genes functionally interact. Sly2p is shown to be an integral membrane protein. 相似文献
13.
Dissection of the phosphorylation of rice DELLA protein, SLENDER RICE1 总被引:14,自引:0,他引:14
Itoh H Sasaki A Ueguchi-Tanaka M Ishiyama K Kobayashi M Hasegawa Y Minami E Ashikari M Matsuoka M 《Plant & cell physiology》2005,46(8):1392-1399
DELLA proteins are repressors of gibberellin signaling in plants. Our previous studies have indicated that gibberellin signaling is derepressed by SCF(GID2)-mediated proteolysis of the DELLA protein, SLENDER RICE1 (SLR1), in rice. In addition, the gibberellin-dependent increase of phosphorylated SLR1 in the loss-of-function gid2 mutant suggests that the SCF(GID2)-mediated degradation of SLR1 might be initiated by gibberellin-dependent phosphorylation. To confirm the role of phosphorylation of SLR1 in its gibberellin-dependent degradation, we revealed that SLR1 is phosphorylated on an N-terminal serine residue(s) within the DELLA/TVHYNP and polyS/T/V domain. However, gibberellin-induced phosphorylation in these regions was not observed in the gid2 mutant following the constitutive expression of SLR1 under the control of the rice actin1 promoter. Treatment with gibberellin induced both the phosphorylated and non-phosphorylated forms of SLR1 with similar induction kinetics in gid2 mutant cells. Both the phosphorylated and non-phosphorylated SLR1 proteins were degraded by gibberellin treatment with a similar half-life in the rice callus cells, and both proteins interacted with recombinant glutathione S-transferase (GST)-GID2. These results demonstrate that the phosphorylation of SLR1 is independent of its degradation and is dispensable for the interaction of SLR1 with the GID2/F-box protein. 相似文献
14.
Gibberellins (GAs) play important roles in many essential plant growth and development processes. A family of nuclear growth-repressing DELLA proteins is the key component in GA signaling. GA perception is mediated by GID1, and the key event of GA signaling is the degradation of DELLA proteins via the 26S proteasome pathway. DELLA proteins integrating other plant hormones signaling and environmental cue modulating plant growth and development have been revealed. GA turning on the de-DELLA-repressing system is conserved, and independently establishes step-by-step recruitment of GA-stimulated GID1-DELLA interaction and DELLA growth-repression functions during land plant evolution. These discoveries open new prospects for the understanding of GA action and DELLA-mediated signaling in plants. 相似文献
15.
Esther Mirjam Natascha Dohmann Carola Nill Claus Schwechheimer 《European journal of cell biology》2010,89(2-3):163-168
The COP9 signalosome (CSN) is an evolutionarily conserved multiprotein complex with an essential role in the development of higher eukaryotes. CSN deconjugates the ubiquitin-related modifier NEDD8 from the cullin subunit of cullin-RING type E3 ubiquitin ligases (CRLs), and CSN-mediated cullin deneddylation is required for full CRL activity. Although several plant E3 CRL functions have been shown to be compromised in Arabidopsis csn mutants, none of these functions have so far been shown to limit growth in these mutants. Here, we examine the role of CSN in the context of the E3 ubiquitin ligase SCFSLEEPY1 (SLY1), which promotes gibberellic acid (GA)-dependent responses in Arabidopsis thaliana. We show that csn mutants are impaired in GA- and SCFSLY1-dependent germination and elongation growth, and we show that these defects correlate with an accumulation and reduced turnover of an SCFSLY1-degradation target, the DELLA protein REPRESSOR-OF-ga1-3 (RGA). Genetic interaction studies between csn mutants and loss-of-function alleles of RGA and its functional homologue GIBBERELLIC ACID INSENSITIVE (GAI) further reveal that RGA and GAI repress defects of germination in strong csn mutants. In addition, we find that these two DELLA proteins are largely responsible for the elongation defects of a weak csn5 mutant allele. We thus conclude that an impairment of SCFSLY1 is at least in part causative for the germination and elongation defects of csn mutants, and suggest that DELLA proteins are major growth repressors in these mutants. 相似文献
16.
We previously reported that the SLEEPY1 (SLY1) homolog, F-box gene SNEEZY/SLEEPY2 (SNE/SLY2), can partly replace SLY1 in gibberellin (GA) hormone signaling through interaction with DELLAs RGA and GAI. To determine whether SNE normally functions in GA signaling, we characterized the phenotypes of two T-DNA alleles, sne-t2 and sne-t3. These mutations result in no apparent vegetative phenotypes, but do result in increased ABA sensitivity in seed germination. Double mutants sly1-t2 sne-t2 and sly1-t2 sne-t3 result in a significant decrease in plant fertility and final plant height compared to sly1-t2. The fact that sne mutations have an additive effect with sly1 suggests that SNE normally functions as a redundant positive regulator of GA signaling.Key words: gibberellin signaling, GA, SLEEPY1, SNEEZY, DELLA, F-box proteinThis paper describes genetic evidence that the SLEEPY1 (SLY1) homolog SNEEZY/SLEEPY2 (SNE/SLY2) functions redundantly with SLY1 to stimulate gibberellin signaling. GA responses such as seed germination, stem elongation and fertility are promoted by proteolysis of DELLA proteins, negative regulators of the GA signaling.1 In the classic GA signaling model, GA binding to the GA receptor GID1 increases GID1 affinity for DELLA protein. This GID1-GA binding to DELLA causes SLY1, the F-box subunit of an SCF E3 ubiquitin ligase complex, to recognize, bind and ubiquitinate DELLA proteins thereby targeting them for destruction by the 26S proteasome. Thus, loss of SLY1 function results in decreased GA responses, causing dwarfism, delayed flowering, infertility and seed dormancy. The sly1 mutants over-accumulate DELLA proteins due to failure to destroy them through the ubiquitin-proteasome pathway.Overexpression of the SLY1 homolog, SNE, partially rescues the germination, dwarfism and infertility of the sly1-10 mutant.2–4 SNE overexpression in the sly1-10 background is associated with reduced accumulation of DELLA proteins RGA and GAI, but not of DELLA RGL2. Co-immunoprecipitation assays demonstrated that SNE directly binds RGA protein as well as the cullin subunit of the SCF E3 complex. These recently published data suggest that SNE forms a functional SCF E3 ubiquitin ligase complex that negatively regulates a subset of the DELLA proteins regulated by SLY1.4The finding that SNE overexpression rescues sly1-10 phenotypes through down-regulation of DELLA RGA and GAI suggests that SNE is normally a positive regulator of GA signaling. If this is true, then we expect sne mutations to cause phenotypes resulting from reduced GA response including reduced germination, stature and fertility. To examine this hypothesis, three sne T-DNA mutants were identified: sne-t1, sne-t2 and sne-t3. The sne-t1 allele is a SALK line containing a T-DNA insertion 183-bp upstream of the coding region.5 This line showed no apparent phenotype and was not further characterized. The sne-t2 allele is a Sussman T-DNA line4,6 containing a T-DNA insertion immediately before the ATG that is the SNE translational start codon (Fig. 1A). While this insertion does not disrupt the coding region, it likely disrupts SNE protein translation as the T-DNA contains multiple stop codons. The sne-t3 allele contains a T-DNA insertion within the SNE ORF before amino acid 146 of the 157 amino acid predicted protein (FLAG_461E03).7,8 This allele should result in loss of the last 11 SNE amino acids. We know that loss of the last 8 SLY1 amino acids in sly1-10 results in dwarfism, suggesting that loss of the last 11 SNE amino acids may also cause some loss of function in the small F-box protein. When the homozygous sne-t2 and sne-t3 lines were compared to wild-type Ws, no change was observed either in final plant height or fertility measured in seeds/silique (Fig. 1B). An ABA dose-response curve in seed germination detected a small but reproducible increase in ABA sensitivity during seed germination of sne-t2 and sne-t3 (Fig. 1C). The fact that the sne-t2 and sne-t3 mutants, like sly1-2 and sly1-10, show increased ABA sensitivity suggests that SNE and SLY1 may have similar functions in GA signaling during seed germination.2Open in a separate windowFigure 1The phenotypes of sne-t2 and sne-t3 T-DNA mutants. (A) Schematic diagram of the sne-t2 T-DNA insertion at position −1 bp and of sne-t3 at position +435 bp with respect to the translation start site. (B) Final plant height (upper) and fertility (lower) of indicated genotypes. Letters indicate statistically different classes as determine by t-test. Bars represent standard error. (C) sne mutants show increase in ABA sensitivity. Seeds of wild-type Ws, sne-t2 and sne-t3 were after-ripened for 2 weeks then sown on MS-agar containing indicated concentrations of ABA as described by Steber et al.11 Germination was scored based on radical emergence after incubating 3 days at 4°C followed by 14 days at 22°C. (D) Mutations in SNE cause no significant effect on DELLA RGA, GAI and RGL2 protein accumulation. Total protein was extracted from leaves of 12-d-old seedlings (Top) or flower buds (FB, bottom) and detected as described in Ariizumi et al.4One possible explanation for the lack of apparent GA-insensitive phenotypes in sne T-DNA insertion lines, is that SNE function is redundant with SLY1 in GA signaling.9 If so, we would expect sly1 sne double mutants to show stronger GA-insensitive phenotypes than the sly1 single mutation. Double mutants were constructed containing either the sne-t2 or sne-t3 mutation in the sly-t2 null background. The sly1-t2 allele was chosen because sly1-t2, sne-t2 and sne-t3 are all in the Ws ecotype. The sly1-t2 allele contains a T-DNA insertion within the F-box domain resulting in severe GA-insensitive phenotypes including failure to germinate, reduced stature and infertility.10 The sly1-t2 sne-t2 and sly1-t2 sne-t3 double mutants showed a small but significant decrease in final plant height and fertility (seeds/silique) compared to sly1-t2 (Fig. 1B). This increase in phenotype severity was not associated with an apparent increase in DELLA RGA, GAI or RGL2 protein accumulation (Fig. 1D). It could be that DELLA protein levels in sly1-t2 are so high that any slight increase due to sne mutations is undetectable. Our previous study of SNE overexpression lines showed that SNE has the ability to downregulate RGA and GAI protein accumulation. Figure 1 shows that the chromosomal SNE gene contributes to GA signaling presumably through ubiquitination of DELLA protein.Taken together, the fact that sne mutants show only mild GA-insensitive phenotypes and that the natural SNE expression cannot compensate for lack of SLY1, indicate that SLY1 is the main E3 ubiquitin ligase stimulating GA signaling (this study, reviewed in ref. 4). We cannot rule out the possibility that stronger SNE alleles would show either stronger GA response phenotypes or phenotypes that are unrelated to GA signaling. Indeed, there is evidence to suggest that SNE may have unique functions. The sne-t3 (sne-1) allele results in a shortened root phenotype.8 That SNE is expressed in the endodermis and quiescent center of the root whereas SLY1 is expressed in the stele, suggests that SNE may function independently in the root.8 Moreover, SNE overexpression, but not SLY1 overexpression, results in decreased apical dominance and a prone growth habit suggesting that SNE may play a unique role in development.2,4 Our model is that in addition to regulating DELLA proteins RGA and GAI, SNE may also regulate a yet unidentified target involved in apical dominance (Fig. 2). Future research will need to elucidate the role of SNE in Arabidopsis growth and development.Open in a separate windowFigure 2Model for SNE function in Arabidopsis. Both SLY1 and SNE act as positive regulators of GA responses via DELLA protein destruction. SNE may negatively regulate an unknown protein that maintains apical dominance. 相似文献
17.
Peng Xu Huiru Chen Ting Li Feng Xu Zhilei Mao Xiaoli Cao Langxi Miao Shasha Du Jie Hua Jiachen Zhao Tongtong Guo Shuang Kou Wenxiu Wang Hong-Quan Yang 《The Plant cell》2021,33(7):2375
Cryptochromes are blue light photoreceptors that mediate various light responses in plants and mammals. In Arabidopsis (Arabidopsis thaliana), cryptochrome 1 (CRY1) mediates blue light-induced photomorphogenesis, which is characterized by reduced hypocotyl elongation and enhanced anthocyanin production, whereas gibberellin (GA) signaling mediated by the GA receptor GA-INSENSITIVE DWARF1 (GID1) and DELLA proteins promotes hypocotyl elongation and inhibits anthocyanin accumulation. Whether CRY1 control of photomorphogenesis involves regulation of GA signaling is largely unknown. Here, we show that CRY1 signaling involves the inhibition of GA signaling through repression of GA-induced degradation of DELLA proteins. CRY1 physically interacts with DELLA proteins in a blue light-dependent manner, leading to their dissociation from SLEEPY1 (SLY1) and the inhibition of their ubiquitination. Moreover, CRY1 interacts directly with GID1 in a blue light-dependent but GA-independent manner, leading to the inhibition of the interaction between GID1 with DELLA proteins. These findings suggest that CRY1 controls photomorphogenesis through inhibition of GA-induced degradation of DELLA proteins and GA signaling, which is mediated by CRY1 inhibition of the interactions of DELLA proteins with GID1 and SCFSLY1, respectively.Blue light-dependent interactions of CRY1 with GID1 and DELLA proteins inhibit gibberellin (GA)-induced degradation of DELLA proteins to regulate GA signaling and photomorphogenesis. 相似文献
18.
The suppressive function of the rice DELLA protein SLR1 is dependent on its transcriptional activation activity 总被引:1,自引:0,他引:1
Hirano K Kouketu E Katoh H Aya K Ueguchi-Tanaka M Matsuoka M 《The Plant journal : for cell and molecular biology》2012,71(3):443-453
When the gibberellin (GA) receptor GIBBERELLIN INSENSITIVE DWARF 1 (GID1) binds to GA, GID1 interacts with DELLA proteins, repressors of GA signaling. This interaction inhibits the suppressive function of DELLA protein and thereby activates the GA response. However, how DELLA proteins exert their suppressive function and how GID1s inhibit suppressive function of DELLA proteins is unclear. By yeast one-hybrid experiments and transient expression of the N-terminal region of rice DELLA protein (SLR1) in rice callus, we established that the N-terminal DELLA/TVHYNP motif of SLR1 possesses transactivation activity. When SLR1 proteins with various deletions were over-expressed in rice, the severity of dwarfism correlated with the transactivation activity observed in yeast, indicating that SLR1 suppresses plant growth through transactivation activity. This activity was suppressed by the GA-dependent GID1-SLR1 interaction, which may explain why GA responses are induced in the presence of GA. The C-terminal GRAS domain of SLR1 also exhibits a suppressive function on plant growth, possibly by directly or indirectly interacting with the promoter region of target genes. Our results indicate that the N-terminal region of SLR1 has two roles in GA signaling: interaction with GID1 and transactivation activity. 相似文献
19.
Nitric oxide regulates DELLA content and PIF expression to promote photomorphogenesis in Arabidopsis
The transition from etiolated to green seedlings involves a shift from hypocotyl growth-promoting conditions to growth restraint. These changes occur through a complex light-driven process involving multiple and tightly coordinated hormonal signaling pathways. Nitric oxide (NO) has been lately characterized as a regulator of plant development interacting with hormone signaling. Here, we show that Arabidopsis (Arabidopsis thaliana) NO-deficient mutant hypocotyls are longer than those from wild-type seedlings under red light but not under blue or far-red light. Accordingly, exogenous treatment with the NO donor sodium nitroprusside and mutant plants with increased endogenous NO levels resulted in reduced hypocotyl length. In addition to increased hypocotyl elongation, NO deficiency led to increased anthocyanin levels and reduced PHYB content under red light, all processes governed by phytochrome-interacting factors (PIFs). NO-deficient plants accordingly showed an enhanced expression of PIF3, PIF1, and PIF4. Moreover, exogenous NO increased the levels of the gibberellin (GA)-regulated DELLA proteins and shortened hypocotyls, likely through the negative regulation of the GA Insensitive Dwarf1 (GID1)-Sleepy1 (SLY1) module. Consequently, NO-deficient seedlings displayed up-regulation of SLY1, defective DELLA accumulation, and altered GA sensitivity, thus resulting in defective deetiolation under red light. Accumulation of NO in wild-type seedlings undergoing red light-triggered deetiolation and elevated levels of NO in the GA-deficient ga1-3 mutant in darkness suggest a mutual NO-GA antagonism in controlling photomorphogenesis. PHYB-dependent NO production promotes photomorphogenesis by a GID1-GA-SLY1-mediated mechanism based on the coordinated repression of growth-promoting PIF genes and the increase in the content of DELLA proteins. 相似文献
20.
Sho Miyazaki Kenji Tomita Hisakazu Yamane Masatomo Kobayashi Tadao Asami Masatoshi Nakajima 《Bioorganic & medicinal chemistry letters》2018,28(14):2465-2470
Helminthosporol, a natural growth regulator isolated from a fungus, stimulates hypocotyl growth and seed germination, similar to gibberellin (GA). We recently reported that helminthosporic acid (H-acid), a synthetic analog of helminthosporol, acts as an agonist of GA receptor. In this study, we showed that a H-acid analog, in which the hydroxymethyl group at the C-8 position of H-acid was converted to a keto group, acts as a selective GA receptor agonist. 1) This analog shows higher hypocotyl elongation activity in Arabidopsis than H-acid does, and induces the degradation of DELLA protein and 2) leads to the formation of the GID1-DELLA complex and 3) regulates the expression of GA-related genes. In addition, 4) its hypocotyl elongation activity was not observed in a atgid1a single mutant, and 5) this analog could promote only the interaction between specific GA receptors and DELLA proteins in vitro. Taken together, our results strongly suggest that the selectivity of the reported H-acid analog depends on the specificity of its GA receptor binding activity. 相似文献