Genome-Wide Analysis of Basic/Helix-Loop-Helix Transcription Factor Family in Rice and Arabidopsis

Li, Xiaoxing; Duan, Xuepeng; Jiang, Haixiong; Sun, Yujin; Tang, Yiming; Zheng, Yawen; Guo, Jingkang; Liang, Wanqi; Chen, Liang; Yin, Jing; Mā, Hong; Wang, Jian; Zhang, Dabing

doi:10.1104/pp.106.080580

Cited by 543 publications

(578 citation statements)

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“…EAT1 shares sequence similarity with AtbHLH089 and AtbHLH091 41 . To gain further insight into the function of EAT1, we performed a yeast two-hybrid analysis to determine whether EAT1 interacts with TDR.…”

Section: Eat1 Acts Downstream From and Interacts With Tdrmentioning

confidence: 99%

EAT1 promotes tapetal cell death by regulating aspartic proteases during male reproductive development in rice

et al. 2013

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Programmed cell death is essential for the development of multicellular organisms, yet pathways of plant programmed cell death and its regulation remain elusive. Here we report that ETERNAL TAPETUM 1, a basic helix-loop-helix transcription factor conserved in land plants, positively regulates programmed cell death in tapetal cells in rice anthers. eat1 exhibits delayed tapetal cell death and aborted pollen formation. ETERNAL TAPETUM 1 directly regulates the expression of OsAP25 and OsAP37, which encode aspartic proteases that induce programmed cell death in both yeast and plants. Expression and genetic analyses revealed that ETERNAL TAPETUM 1 acts downstream of TAPETUM DEGENERATION RETARDATION, another positive regulator of tapetal programmed cell death, and that ETERNAL TAPETUM 1 can also interact with the TAPETUM DEGENERATION RETARDATION protein. This study demonstrates that ETERNAL TAPETUM 1 promotes aspartic proteases triggering plant programmed cell death, and reveals a dynamic regulatory cascade in male reproductive development in rice.

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Section: Eat1 Acts Downstream From and Interacts With Tdrmentioning

confidence: 99%

EAT1 promotes tapetal cell death by regulating aspartic proteases during male reproductive development in rice

et al. 2013

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“…bHLH transcription factors are proteins that bind as dimers to specific DNA targets and have been characterized as important regulators in diverse biological processes (Bailey et al 2003;Li et al 2006b;Toledo-Ortiz et al 2003). The closest homologue of bHLH162 (CS-07) according to the Database of Arabidopsis Transcription Factors (Guo et al 2005) is At1g10585.…”

Section: Cs Transcription Factorsmentioning

confidence: 99%

Disease-Specific Expression of Host Genes During Downy Mildew Infection of Arabidopsis

Huibers¹,

Jong²,

Dekter³

et al. 2009

MPMI

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Here, we report on the identification of Arabidopsis genes that are induced during compatible but not during incompatible interactions with the downy mildew pathogen Hyaloperonospora arabidopsidis. This set of so-called compatible specific (CS) genes contrasts with the large group of defense-associated genes that is differentially expressed during both compatible and incompatible interactions. From the 17 identified CS genes, 6 belong to the ethylene response factor (ERF) family of transcription factor genes, suggesting that these ERF have a role during compatibility. The majority of CS genes are differentially regulated in response to various forms of abiotic stress. In silico analysis of the CS genes revealed an over-representation of dehydration-responsive element/C-repeat binding factor (DREB1A/ CBF3) binding sites and EveningElement motifs in their promoter regions. The CS-ERF are closely related to the CBF transcription factors and could potentially bind the DREB1A/CBF3 promoter elements in the CS genes. Transcript levels of CS genes peak at 2 to 3 days postinoculation, when pathogen growth is highest, and decline at later stages of infection. The induction of several CS genes was found to be isolate specific. This suggests that the identified CS genes could be the direct or indirect targets of downy mildew effector proteins that promote disease susceptibility.

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“…6,13 Second, although dimerization of MYC2 or MYC3 has not been reported yet, it might occur, at least under certain conditions, because, for instance, heterodimerization of the basic-helix-loophelix (bHLH) proteins GLABRA3 and ENHANCER OF GLABRA3, both involved in trichome development and closely related to MYC2, has already been described. 14,15 In addition, in maize (Zea mays) the homologous bHLH factor R is capable of forming homodimers. 16 Third, JAZ-JAZ dimerizations might facilitate the simultaneous binding of multiple JAZ proteins with MYC proteins.…”

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Dissection of the one-MegaDalton JAZ1 protein complex

Geerinck

Pauwels

Jaeger

et al. 2010

Plant Signaling & Behavior

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JA-Ile, the endogenous bioactive JA, is perceived by the F-box protein CORONATINE INSENSITIVE1 (COI1) that functions as the hormone receptor. In the presence of JA-Ile, the E3 ubiquitin ligase complex SCF COI1 recognizes its targets, the JAZ proteins that are subsequently ubiquitinylated and destroyed by the 26S proteasome. [1][2][3][4][5] In an unelicited state, the JAZ proteins bind and inactivate the transcription factor MYC2, thereby repressing the activation of early JA-responsive genes through a mechanism that remained elusive to date.In our study, 6 we used a tandem affinity purification (TAP) technology platform that had been established in Arabidopsis Dissection of the one-MegaDalton JAZ1 protein complex Jan Geerinck, Laurens Pauwels, Geert De Jaeger and Alain Goossens* Department of Plant Systems Biology; VIB and Department of Plant Biotechnology and Genetics; Ghent University; Ghent, Belgium thaliana cell suspension cultures, 7 to retrieve new interactors of JAZ1 and, thereby, unravel the core JA signaling module. JAZ1-TAP cultures were mock treated or elicited with JA for 1 min and subsequently harvested and analyzed. JAZ1 was found to interact with JAZ12 and MYC3, a close relative of MYC2. Also interaction between COI1 and JAZ1 was observed, but only in the presence of JA, in accordance with the proposed models.1-5 We focused on a previously uncharacterized protein, designated NINJA (At4g28910) that was retrieved with JAZ1 independently of the JA elicitation. Studies with green fluorescent protein (GFP)-tagged proteins demonstrated that the stability of NINJA was not affected by JAs, in contrast to the JAZ proteins that were degraded within minutes after JA application.The specificity of NINJA for JAZ proteins was confirmed by yeast-two hybrid (Y2H) analysis and pull-down experiments. Furthermore, these experiments revealed that NINJA interacted with most JAZ proteins as well as with other ZIMdomain proteins that contain the conserved TIF[F/Y]XG (TIFY) motif and belong to the group II TIFY proteins, 8 such as PEAPOD1 (PPD1), PPD2 and TIFY8. In a Y2H analysis with deletion series of JAZ1, a 39-amino-acid fragment with the TIFY motif was found to be necessary and sufficient for the interaction with NINJA. Conversely, a deletion series of NINJA that is characterized by three conserved protein motifs, designated A, B and C, showed that the C-domain was responsible and sufficient for interaction with JAZ proteins.Analogously to the JAZ1-TAP, a TAP analysis with NINJA as bait revealed that NINJA was present in a complex with the

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Genome-Wide Analysis of Basic/Helix-Loop-Helix Transcription Factor Family in Rice and Arabidopsis

Cited by 543 publications

References 82 publications

EAT1 promotes tapetal cell death by regulating aspartic proteases during male reproductive development in rice

EAT1 promotes tapetal cell death by regulating aspartic proteases during male reproductive development in rice

Disease-Specific Expression of Host Genes During Downy Mildew Infection of Arabidopsis

Dissection of the one-MegaDalton JAZ1 protein complex

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