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  • 1
    Online Resource
    Online Resource
    Oxford University Press (OUP) ; 2001
    In:  Plant Physiology Vol. 126, No. 3 ( 2001-07-01), p. 1250-1258
    In: Plant Physiology, Oxford University Press (OUP), Vol. 126, No. 3 ( 2001-07-01), p. 1250-1258
    Abstract: The SPINDLY (SPY) protein of Arabidopsis is a negative regulator of gibberellin (GA) response. The SPY protein has 10 copies of the tetratricopeptide repeat (TPR) at the N terminus. TPR motifs function as protein-protein interaction domains. Several spyalleles are affected only in the TPR region suggesting that protein-protein interactions mediated by this domain are important for proper GA signaling. We have used a reverse genetics approach to further investigate the role of the TPR domain. The TPR domain of SPY was overexpressed in wild-type, gai, andspy plants. Expression of the TPR domain alone is not sufficient to rescue spy mutants. Expression of the TPR domain in a wild-type background produces phenotypes similar to those caused by loss-of-function spy mutants including resistance to GA biosynthesis inhibitors, short hypocotyl length, and early flowering. The dwarfing of the floral shoot internodes caused by the gai mutation was suppressed by expression of the TRP domain. Expression of the TPR domain had no effect on the abundance of endogenous SPY mRNA. The TPR domain was found to interact with SPY both in vitro and in yeast two-hybrid assays. These data indicate that the TPR domain of SPY can participate in protein-protein interactions and that these interactions are important for the proper functioning of SPY.
    Type of Medium: Online Resource
    ISSN: 1532-2548 , 0032-0889
    RVK:
    Language: English
    Publisher: Oxford University Press (OUP)
    Publication Date: 2001
    detail.hit.zdb_id: 2004346-6
    detail.hit.zdb_id: 208914-2
    SSG: 12
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  • 2
    In: Plant Physiology, Oxford University Press (OUP), Vol. 143, No. 1 ( 2007-01), p. 517-529
    Type of Medium: Online Resource
    ISSN: 0032-0889 , 1532-2548
    RVK:
    Language: English
    Publisher: Oxford University Press (OUP)
    Publication Date: 2007
    detail.hit.zdb_id: 2004346-6
    detail.hit.zdb_id: 208914-2
    SSG: 12
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  • 3
    Online Resource
    Online Resource
    Oxford University Press (OUP) ; 2010
    In:  The Plant Cell Vol. 22, No. 2 ( 2010-03-25), p. 392-402
    In: The Plant Cell, Oxford University Press (OUP), Vol. 22, No. 2 ( 2010-03-25), p. 392-402
    Abstract: Phototropins (phot) sense blue light through the two N-terminal chromophore binding LOV domains and activate the C-terminal kinase domain. The resulting phototropin autophosphorylation is essential for biological activity. We identified the A1 subunit of Ser/Thr protein phosphatase 2A (PP2A) as interacting with full-length phot2 in yeast and also interacting with phot2 in an in vitro protein binding assay. Phenotypic characterizations of a phot1-5 rcn1-1 (for root curling in n-naphthylphthalamic acid1) double mutant, in which phot2 is the only functional phototropin and PP2A activity is reduced, showed enhanced phototropic sensitivity and enhanced blue light–induced stomatal opening, suggesting that PP2A activity is involved in regulating phot2 function. When treated with cantharidin, a chemical inhibitor of PP2A, the phot1-5 mutant exhibited enhanced phot2-mediated phototropic responses like those of the phot1-5 rcn1-1 double mutant. Immunoblot analysis to examine phot2 endogenous phosphorylation levels and in vitro phosphorylation assays of phot2 extracted from plants during dark recovery from blue light exposure confirmed that phot2 is more slowly dephosphorylated in the reduced PP2A activity background than in the wild-type PP2A background, suggesting that phosphorylated phot2 is a substrate of PP2A activity. While reduced PP2A activity enhanced the activity of phot2, it did not enhance either phot1 dephosphorylation or the activity of phot1 in mediating phototropism or stomatal opening.
    Type of Medium: Online Resource
    ISSN: 1532-298X , 1040-4651
    Language: English
    Publisher: Oxford University Press (OUP)
    Publication Date: 2010
    detail.hit.zdb_id: 623171-8
    detail.hit.zdb_id: 2004373-9
    SSG: 12
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  • 4
    In: The Plant Cell, Oxford University Press (OUP), Vol. 24, No. 1 ( 2012-02-28), p. 96-108
    Abstract: O-linked N-acetylglucosamine (O-GlcNAc) modifications regulate the posttranslational fate of target proteins. The Arabidopsis thaliana O-GlcNAc transferase (OGT) SPINDLY (SPY) suppresses gibberellin signaling and promotes cytokinin (CK) responses by unknown mechanisms. Here, we present evidence that two closely related class I TCP transcription factors, TCP14 and TCP15, act with SPY to promote CK responses. TCP14 and TCP15 interacted with SPY in yeast two-hybrid and in vitro pull-down assays and were O-GlcNAc modified in Escherichia coli by the Arabidopsis OGT, SECRET AGENT. Overexpression of TCP14 severely affected plant development in a SPY-dependent manner and stimulated typical CK morphological responses, as well as the expression of the CK-regulated gene RESPONSE REGULATOR5. TCP14 also promoted the transcriptional activity of the CK-induced mitotic factor CYCLIN B1;2. Whereas TCP14-overexpressing plants were hypersensitive to CK, spy and tcp14 tcp15 double mutant leaves and flowers were hyposensitive to the hormone. Reducing CK levels by overexpressing CK OXIDASE/DEHYDROGENASE3 suppressed the TCP14 overexpression phenotypes, and this suppression was reversed when the plants were treated with exogenous CK. Taken together, we suggest that responses of leaves and flowers to CK are mediated by SPY-dependent TCP14 and TCP15 activities.
    Type of Medium: Online Resource
    ISSN: 1532-298X , 1040-4651
    Language: English
    Publisher: Oxford University Press (OUP)
    Publication Date: 2012
    detail.hit.zdb_id: 623171-8
    detail.hit.zdb_id: 2004373-9
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  • 5
    In: International Journal of Molecular Sciences, MDPI AG, Vol. 24, No. 18 ( 2023-09-06), p. 13720-
    Abstract: Rhizobacteria from various ecological niches display variations in physiological characteristics. This study investigates the transcriptome profiling of two Bacillus subtilis strains, BsCP1 and BsPG1, each isolated from distinct environments. Gene expression linked to the synthesis of seven types of antibiotic compounds was detected in both BsCP1 and BsPG1 cultures. Among these, the genes associated with plipastatin synthesis were predominantly expressed in both bacterial strains. However, genes responsible for the synthesis of polyketide, subtilosin, and surfactin showed distinct transcriptional patterns. Additionally, genes involved in producing exopolysaccharides (EPS) showed higher expression levels in BsPG1 than in BsCP1. Consistently with this, a greater quantity of EPS was found in the BsPG1 culture compared to BsCP1. Both bacterial strains exhibited similar effects on Arabidopsis seedlings, promoting root branching and increasing seedling fresh weight. However, BsPG1 was a more potent enhancer of drought, heat, and copper stress tolerance than BsCP1. Treatment with BsPG1 had a greater impact on improving survival rates, increasing starch accumulation, and stabilizing chlorophyll content during the post-stress stage. qPCR analysis was used to measure transcriptional changes in Arabidopsis seedlings in response to BsCP1 and BsPG1 treatment. The results show that both bacterial strains had a similar impact on the expression of genes involved in the salicylic acid (SA) and jasmonic acid (JA) signaling pathways. Likewise, genes associated with stress response, root development, and disease resistance showed comparable responses to both bacterial strains. However, treatment with BsCP1 and BsPG1 induced distinct activation of genes associated with the ABA signaling pathway. The results of this study demonstrate that bacterial strains from different ecological environments have varying abilities to produce beneficial metabolites for plant growth. Apart from the SA and JA signaling pathways, ABA signaling triggered by PGPR bacterial strains could play a crucial role in building an effective resistance to various abiotic stresses in the plants they colonize.
    Type of Medium: Online Resource
    ISSN: 1422-0067
    Language: English
    Publisher: MDPI AG
    Publication Date: 2023
    detail.hit.zdb_id: 2019364-6
    SSG: 12
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  • 6
    In: Chronobiology International, Informa UK Limited, Vol. 19, No. 6 ( 2002-01), p. 1005-1022
    Type of Medium: Online Resource
    ISSN: 0742-0528 , 1525-6073
    Language: English
    Publisher: Informa UK Limited
    Publication Date: 2002
    detail.hit.zdb_id: 2026725-3
    SSG: 12
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  • 7
    Online Resource
    Online Resource
    Oxford University Press (OUP) ; 2007
    In:  Plant Physiology Vol. 143, No. 2 ( 2007-02-06), p. 987-1000
    In: Plant Physiology, Oxford University Press (OUP), Vol. 143, No. 2 ( 2007-02-06), p. 987-1000
    Abstract: The Arabidopsis (Arabidopsis thaliana) SPINDLY (SPY) protein negatively regulates the gibberellin (GA) signaling pathway. SPY is an O-linked N-acetylglucosamine (GlcNAc) transferase (OGT) with a protein-protein interaction domain consisting of 10 tetratricopeptide repeats (TPR). OGTs add a GlcNAc monosaccharide to serine/threonine residues of nuclear and cytosolic proteins. Determination of the molecular defects in 14 new spy alleles reveals that these mutations cluster in three TPRs and the C-terminal catalytic region. Phenotypic characterization of 12 spy alleles indicates that TPRs 6, 8, and 9 and the catalytic domain are crucial for GA-regulated stem elongation, floral induction, and fertility. TPRs 8 and 9 and the catalytic region are also important for modulating trichome morphology and inflorescence phyllotaxy. Consistent with a role for SPY in embryo development, several alleles affect seedling cotyledon number. These results suggest that three of the TPRs and the OGT activity in SPY are required for its function in GA signal transduction. We also examined the effect of spy mutations on another negative regulator of GA signaling, REPRESSOR OF ga1-3 (RGA). The DELLA motif in RGA is essential for GA-induced proteolysis of RGA, and deletion of this motif (as in rga-Δ17) causes a GA-insensitive dwarf phenotype. Here, we demonstrate that spy partially suppresses the rga-Δ17 phenotype but does not reduce rga-Δ17 or RGA protein levels or alter RGA nuclear localization. We propose that SPY may function as a negative regulator of GA response by increasing the activity of RGA, and presumably other DELLA proteins, by GlcNAc modification.
    Type of Medium: Online Resource
    ISSN: 1532-2548
    Language: English
    Publisher: Oxford University Press (OUP)
    Publication Date: 2007
    detail.hit.zdb_id: 2004346-6
    detail.hit.zdb_id: 208914-2
    SSG: 12
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  • 8
    Online Resource
    Online Resource
    Informa UK Limited ; 2010
    In:  Plant Signaling & Behavior Vol. 5, No. 2 ( 2010-02), p. 184-186
    In: Plant Signaling & Behavior, Informa UK Limited, Vol. 5, No. 2 ( 2010-02), p. 184-186
    Type of Medium: Online Resource
    ISSN: 1559-2324
    Language: English
    Publisher: Informa UK Limited
    Publication Date: 2010
    detail.hit.zdb_id: 2252855-6
    SSG: 12
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  • 9
    In: Molecular Plant, Elsevier BV, Vol. 7, No. 9 ( 2014-09), p. 1441-1454
    Type of Medium: Online Resource
    ISSN: 1674-2052
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2014
    detail.hit.zdb_id: 2393618-6
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  • 10
    In: Journal of Integrative Plant Biology, Wiley, Vol. 49, No. 1 ( 2007-01), p. 4-10
    Abstract: The phototropins phot1 and phot2 are plant blue‐light receptors that mediate phototropism, chloroplast movements, stomatal opening, leaf expansion, the rapid inhibition of hypocotyl growth in etiolated seedlings, and possibly solar tracking by leaves in those species in which it occurs. The phototropins are plasma membrane‐associated hydrophilic proteins with two chromophore domains (designated LOV1 and LOV2 for their resemblance to domains in other signaling proteins that detect light, oxygen, or voltage) in their N‐terminal half and a classic serine/threonine kinase domain in their C‐terminal half. Both chromophore domains bind flavin mononucleotide (FMN) and both undergo light‐activated formation of a covalent bond between a nearby cysteine and the C(4a) carbon of the FMN to form the signaling state. LOV2‐cysteinyl adduct formation leads to the release downstream of a tightly bound amphipathic α‐helix, a step required for activation of the kinase function. This cysteinyl adduct then slowly decays over a matter of seconds or minutes to return the photoreceptor chromophore modules to their ground state. Functional LOV2 is required for light‐activated phosphorylation and for various blue‐light responses mediated by the phototropins. The function of LOV1 is still unknown, although it may serve to modulate the signal generated by LOV2. The LOV domain is an ancient chromophore module found in a wide range of otherwise unrelated proteins in fungi and prokaryotes, the latter including cyanobacteria, eubacteria, and archaea. Further general reviews on the phototropins are those by Celaya and Liscum (2005) and Christie and Briggs (2005).
    Type of Medium: Online Resource
    ISSN: 1672-9072 , 1744-7909
    URL: Issue
    Language: English
    Publisher: Wiley
    Publication Date: 2007
    detail.hit.zdb_id: 2130095-1
    SSG: 12
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