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  • 1
    Language: English
    In: Nature (London), 2010, Vol.464 (7290), p.913-916
    Description: Acquisition of cell identity in plants relies strongly on positional information1, hence cell–cell communication and inductive signalling are instrumental for developmental patterning. During Arabidopsis embryogenesis, an extra-embryonic cell is specified to become the founder cell of the primary root meristem, hypophysis, in response to signals from adjacent embryonic cells2. The auxin-dependent transcription factor MONOPTEROS (MP) drives hypophysis specification by promoting transport of the hormone auxin from the embryo to the hypophysis precursor. However, auxin accumulation is not sufficient for hypophysis specification, indicating that additional MP-dependent signals are required3. Here we describe the microarray-based isolation of MP target genes that mediate signalling from embryo to hypophysis. Of three direct transcriptional target genes, TARGET OF MP 5 (TMO5) and TMO7 encode basic helix–loop–helix (bHLH) transcription factors that are expressed in the hypophysis-adjacent embryo cells, and are required and partially sufficient for MP-dependent root initiation. Importantly, the small TMO7 transcription factor moves from its site of synthesis in the embryo to the hypophysis precursor, thus representing a novel MP-dependent intercellular signal in embryonic root specification
    Subject(s): mutation ; embryogenesis ; receptor ; arabidopsis-thaliana ; auxin-response factors ; gene-expression ; loop-helix proteins ; family ; activation ; encodes ; Fundamental and applied biological sciences. Psychology ; Vegetative apparatus, growth and morphogenesis. Senescence ; Biological and medical sciences ; Plant physiology and development ; Meristem - cytology ; Plant Roots - metabolism ; Indoleacetic Acids - metabolism ; Oligonucleotide Array Sequence Analysis ; Signal Transduction ; Arabidopsis - cytology ; Embryonic Development - genetics ; Arabidopsis - embryology ; Plant Roots - cytology ; Arabidopsis - metabolism ; Arabidopsis Proteins - metabolism ; DNA-Binding Proteins - metabolism ; Transcription Factors - metabolism ; Basic Helix-Loop-Helix Transcription Factors - metabolism ; Genes, Plant - genetics ; Plant Roots - embryology ; Meristem - embryology ; Gene Expression Regulation, Plant ; Meristem - metabolism ; Physiological aspects ; Embryonic development ; Transcription factors ; Genetic aspects ; Research ; Arabidopsis ; Index Medicus
    ISSN: 0028-0836
    E-ISSN: 1476-4687
    Source: Academic Search Ultimate
    Source: Alma/SFX Local Collection
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 2
    Language: English
    In: The EMBO journal, 2005-05-18, Vol.24 (10), p.1874-1885
    Description: The plant hormone auxin elicits many specific context‐dependent developmental responses. Auxin promotes degradation of Aux/IAA proteins that prevent transcription factors of the auxin response factor (ARF) family from regulating auxin‐responsive target genes. Aux/IAAs and ARFs are represented by large gene families in Arabidopsis. Here we show that stabilization of BDL/IAA12 or its sister protein IAA13 prevents MP/ARF5‐dependent embryonic root formation whereas stabilized SHY2/IAA3 interferes with seedling growth. Although both bdl and shy2‐2 proteins inhibited MP/ARF5‐dependent reporter gene activation, shy2‐2 was much less efficient than bdl to interfere with embryonic root initiation when expressed from the BDL promoter. Similarly, MP was much more efficient than ARF16 in this process. When expressed from the SHY2 promoter, both shy2‐2 and bdl inhibited cell elongation and auxin‐induced gene expression in the seedling hypocotyl. By contrast, gravitropism and auxin‐induced gene expression in the root, which were promoted by functionally redundant NPH4/ARF7 and ARF19 proteins, were inhibited by shy2‐2, but not by bdl protein. Our results suggest that auxin signals are converted into specific responses by matching pairs of coexpressed ARF and Aux/IAA proteins.
    Subject(s): embryo ; Aux/IAA protein ; ARF transcription factor ; Arabidopsis ; root gravitropism ; Arabidopsis Proteins - metabolism ; Transcription Factors - metabolism ; Promoter Regions, Genetic ; Indoleacetic Acids - metabolism ; Arabidopsis - embryology ; Nuclear Proteins - metabolism ; Hypocotyl - metabolism ; Arabidopsis - metabolism ; Index Medicus ; IAA protein ; Aux
    ISSN: 0261-4189
    E-ISSN: 1460-2075
    Source: HighWire Press (Free Journals)
    Source: PubMed Central
    Source: Alma/SFX Local Collection
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 3
    Language: English
    In: eLife, 2014-04-08, Vol.3, p.e02131-e02131
    Description: Membrane trafficking is essential to fundamental processes in eukaryotic life, including cell growth and division. In plant cytokinesis, post-Golgi trafficking mediates a massive flow of vesicles that form the partitioning membrane but its regulation remains poorly understood. Here, we identify functionally redundant Arabidopsis ARF guanine-nucleotide exchange factors (ARF-GEFs) BIG1-BIG4 as regulators of post-Golgi trafficking, mediating late secretion from the trans-Golgi network but not recycling of endocytosed proteins to the plasma membrane, although the TGN also functions as an early endosome in plants. In contrast, BIG1-4 are absolutely required for trafficking of both endocytosed and newly synthesized proteins to the cell-division plane during cytokinesis, counteracting recycling to the plasma membrane. This change from recycling to secretory trafficking pathway mediated by ARF-GEFs confers specificity of cargo delivery to the division plane and might thus ensure that the partitioning membrane is completed on time in the absence of a cytokinesis-interphase checkpoint. DOI: http://dx.doi.org/10.7554/eLife.02131.001.
    Subject(s): Arabidopsis Proteins - metabolism ; Endocytosis ; Cell Division ; Golgi Apparatus - metabolism ; Arabidopsis Proteins - secretion ; Arabidopsis - metabolism ; Protein Transport ; Seeds ; Cytokinesis ; Guanine ; Golgi apparatus ; Proteins ; Microscopy ; Phylogenetics ; Membrane trafficking ; Physiology ; Software ; Flowers & plants ; Recycling ; Molecular biology ; Guanine nucleotide exchange factor ; Localization ; Index Medicus ; Plant Biology ; ARF-GEF ; secretion ; Arabidopsis ; cell division ; post-Golgi trafficking ; recycling ; gegulation of vesicle traffic ; Cell Biology
    ISSN: 2050-084X
    E-ISSN: 2050-084X
    Source: PubMed Central
    Source: Directory of Open Access Journals
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 4
    Language: English
    In: Journal of experimental botany, 2013-01-01, Vol.64 (10), p.3009-3019
    Description: In Arabidopsis thaliana, the phytohormone auxin is an important patterning agent during embryogenesis and post-embryonic development, exerting effects through transcriptional regulation. The main determinants of the transcriptional auxin response machinery are AUXIN RESPONSE FACTOR (ARF) transcription factors and AUXIN/INDOLE-3-ACETIC ACID (AUX/IAA) inhibitors. Although members of these two protein families are major developmental regulators, the transcriptional regulation of the genes encoding them has not been well explored. For example, apart from auxin-linked regulatory inputs, factors regulating the expression of the AUX/IAA BODENLOS (BDL)/IAA12 are not known. Here, it was shown that the HOMEODOMAIN-LEUCINE ZIPPER (HD-ZIP) transcription factor HOMEOBOX PROTEIN 5 (HB5) negatively regulates BDL expression, which may contribute to the spatial control of BDL expression. As such, HB5 and probably other class I HD-ZIP proteins, appear to modulate BDL-dependent auxin response.
    Subject(s): Embryogenesis ; Transcription factors ; Cotyledons ; Genes ; Auxins ; Plants ; Molecular biology ; Embryos ; RESEARCH PAPER ; Seedlings ; Plant cells ; plant development ; regulated gene-expression ; shade avoidance ; class-i ; homeodomain ; protein ; of-function mutation ; auxin response ; homeobox gene ; root initiation ; Fundamental and applied biological sciences. Psychology ; Biological and medical sciences ; Plant physiology and development ; Arabidopsis Proteins - genetics ; Arabidopsis - chemistry ; Transcription Factors - chemistry ; Indoleacetic Acids - metabolism ; Down-Regulation ; Homeodomain Proteins - metabolism ; Leucine Zippers ; Repressor Proteins - genetics ; Transcription Factors - genetics ; Homeodomain Proteins - chemistry ; Homeodomain Proteins - genetics ; Arabidopsis - metabolism ; Arabidopsis - genetics ; Arabidopsis Proteins - metabolism ; Transcription Factors - metabolism ; Arabidopsis Proteins - chemistry ; Gene Expression Regulation, Plant ; Plant Growth Regulators - metabolism ; Repressor Proteins - metabolism ; Index Medicus ; HOMEOBOX PROTEIN 5 (HB5) ; auxin ; Arabidopsis ; BODENLOS (BDL) ; transcriptional regulation ; embryo ; Research Paper
    ISSN: 0022-0957
    E-ISSN: 1460-2431
    Source: Alma/SFX Local Collection
    Source: Oxford Journals 2016 Current and Archive A-Z Collection
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 5
    Language: English
    In: The Plant cell, 2000-03-01, Vol.12 (3), p.343-356
    Description: The Arabidopsis GNOM protein, a guanine nucleotide exchange factor (GEF) that acts on ADP ribosylation factor (ARF)-type G proteins, is required for coordination of cell polarity along the apical-basal embryo axis. Interallelic complementation of gnom mutants suggested that dimerization is involved in GNOM function. Here, direct interaction between GNOM molecules is demonstrated in vitro and by using a yeast two-hybrid system. Interaction was confined to an N-terminal domain conserved within a subgroup of large ARF GEFs. The same domain mediated in vitro binding to cyclophilin 5 (Cyp5), which was identified as a GNOM interactor in two-hybrid screening. Cyp5 displayed peptidylprolyl cis/trans-isomerase and protein refolding activities that were sensitive to cyclosporin A. Cyp5 protein accumulated in several plant organs and, like GNOM, was partitioned between cytosolic and membrane fractions. Cyp5 protein was also expressed in the developing embryo. Our results suggest that Cyp5 may regulate the ARF GEF function of the GNOM protein during embryogenesis.
    Subject(s): Proteins ; Yeasts ; Antiserum ; Complementary DNA ; Cyclosporins ; Protein refolding ; Amino acids ; Embryos ; Dimerization ; Plant cells ; Cyclosporine - pharmacology ; Molecular Sequence Data ; Arabidopsis - embryology ; Recombinant Fusion Proteins - metabolism ; Seeds - growth & development ; Guanine Nucleotide Exchange Factors - metabolism ; Plant Proteins - chemistry ; Conserved Sequence ; Peptidylprolyl Isomerase - metabolism ; Peptidylprolyl Isomerase - isolation & purification ; Plant Proteins - metabolism ; Peptidylprolyl Isomerase - genetics ; ADP-Ribosylation Factors - genetics ; Binding Sites ; Protein Structure, Tertiary ; Amino Acid Sequence ; Guanine Nucleotide Exchange Factors - genetics ; Seeds - metabolism ; Protein Folding ; Arabidopsis - metabolism ; Arabidopsis - genetics ; Sequence Homology, Amino Acid ; Catalysis - drug effects ; Plant Proteins - genetics ; Two-Hybrid System Techniques ; ADP-Ribosylation Factors - chemistry ; Protein Binding ; Recombinant Fusion Proteins - genetics ; Guanine Nucleotide Exchange Factors - chemistry ; Research ; Cyclophilin ; Arabidopsis ; Guanine ; Index Medicus
    ISSN: 1040-4651
    E-ISSN: 1532-298X
    Source: American Society of Plant Biologists
    Source: HighWire Press (Free Journals)
    Source: Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
    Source: PubMed Central
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 6
    Language: English
    In: PLoS genetics, 2018-11, Vol.14 (11), p.e1007795-e1007795
    Description: In eukaryotes, GTP-bound ARF GTPases promote intracellular membrane traffic by mediating the recruitment of coat proteins, which in turn sort cargo proteins into the forming membrane vesicles. Mammals employ several classes of ARF GTPases which are activated by different ARF guanine-nucleotide exchange factors (ARF-GEFs). In contrast, flowering plants only encode evolutionarily conserved ARF1 GTPases (class I) but not the other classes II and III known from mammals, as suggested by phylogenetic analysis of ARF family members across the five major clades of eukaryotes. Instead, flowering plants express plant-specific putative ARF GTPases such as ARFA and ARFB, in addition to evolutionarily conserved ARF-LIKE (ARL) proteins. Here we show that all eight ARF-GEFs of Arabidopsis interact with the same ARF1 GTPase, whereas only a subset of post-Golgi ARF-GEFs also interacts with ARFA, as assayed by immunoprecipitation. Both ARF1 and ARFA were detected at the Golgi stacks and the trans-Golgi network (TGN) by both live-imaging with the confocal microscope and nano-gold labeling followed by EM analysis. ARFB representing another plant-specific putative ARF GTPase was detected at both the plasma membrane and the TGN. The activation-impaired form (T31N) of ARF1, but neither ARFA nor ARFB, interfered with development, although ARFA-T31N interfered, like ARF1-T31N, with the GDP-GTP exchange. Mutant plants lacking both ARFA and ARFB transcripts were viable, suggesting that ARF1 is sufficient for all essential trafficking pathways under laboratory conditions. Detailed imaging of molecular markers revealed that ARF1 mediated all known trafficking pathways whereas ARFA was not essential to any major pathway. In contrast, the hydrolysis-impaired form (Q71L) of both ARF1 and ARFA, but not ARFB, had deleterious effects on development and various trafficking pathways. However, the deleterious effects of ARFA-Q71L were abolished by ARFA-T31N inhibiting cognate ARF-GEFs, both in cis (ARFA-T31N,Q71L) and in trans (ARFA-T31N + ARFA-Q71L), suggesting indirect effects of ARFA-Q71L on ARF1-mediated trafficking. The deleterious effects of ARFA-Q71L were also suppressed by strong over-expression of ARF1, which was consistent with a subset of BIG1-4 ARF-GEFs interacting with both ARF1 and ARFA. Indeed, the SEC7 domain of BIG5 activated both ARF1 and ARFA whereas the SEC7 domain of BIG3 only activated ARF1. Furthermore, ARFA-T31N impaired root growth if ARF1-specific BIG3 was knocked out and only ARF1- and ARFA-activating BIG4 was functional. Activated ARF1 recruits different coat proteins to different endomembrane compartments, depending on its activation by different ARF-GEFs. Unlike ARF GTPases, ARF-GEFs not only localize at distinct compartments but also regulate specific trafficking pathways, suggesting that ARF-GEFs might play specific roles in traffic regulation beyond the activation of ARF1 by GDP-GTP exchange.
    Subject(s): Arabidopsis Proteins - genetics ; Guanine Nucleotide Exchange Factors - genetics ; Signal Transduction ; Arabidopsis - ultrastructure ; Genome, Plant ; Phylogeny ; Guanine Nucleotide Exchange Factors - classification ; Arabidopsis - metabolism ; Protein Transport ; Arabidopsis - genetics ; Arabidopsis Proteins - metabolism ; Up-Regulation - drug effects ; trans-Golgi Network - metabolism ; GTP Phosphohydrolases - metabolism ; GTP Phosphohydrolases - genetics ; Guanine Nucleotide Exchange Factors - metabolism ; Models, Biological ; GTP Phosphohydrolases - classification ; Plants, Genetically Modified ; Arabidopsis Proteins - classification ; Estradiol - pharmacology ; Intracellular Membranes - metabolism ; Arabidopsis thaliana ; Physiological aspects ; Guanosine triphosphatase ; Proteins ; Traffic regulations ; G proteins ; Index Medicus ; Biology and Life Sciences ; Research and Analysis Methods ; Immunoprecipitation ; Peptides ; Cell division ; Membrane vesicles ; Guanosine triphosphatases ; Genomes ; Kinases ; Mammals ; Gene expression ; Guanine ; Golgi apparatus ; Guanosine triphosphate ; Overexpression ; Guanosine diphosphate ; Proteomics ; Flowering ; Membrane trafficking ; Molecular biology ; Guanine nucleotide exchange factor ; Endoplasmic reticulum
    ISSN: 1553-7404
    ISSN: 1553-7390
    E-ISSN: 1553-7404
    Source: Academic Search Ultimate
    Source: PubMed Central
    Source: Directory of Open Access Journals
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 7
    Language: English
    In: Developmental cell, 2006, Vol.10 (2), p.265-270
    Description: The Arabidopsis embryonic root meristem is initiated by the specification of a single cell, the hypophysis. This event critically requires the antagonistic auxin response regulators MONOPTEROS and BODENLOS, but their mechanism of action is unknown. We show that these proteins interact and transiently act in a small subdomain of the proembryo adjacent to the future hypophysis. Here they promote transport of auxin, which then elicits a second response in the hypophysis itself. Our results suggest that hypophysis specification is not the direct result of a primary auxin response but rather depends on cell-to-cell signaling triggered by auxin in adjacent cells.
    Subject(s): DEVBIO ; SIGNALING ; mutation ; expression ; arf ; gene ; protein ; root ; embryo ; transformation ; movement ; monopteros ; Fundamental and applied biological sciences. Psychology ; Biological and medical sciences ; Cell physiology ; Molecular and cellular biology ; Cell differentiation, maturation, development, hematopoiesis ; Meristem - cytology ; Arabidopsis Proteins - genetics ; Plant Roots - metabolism ; Indoleacetic Acids - metabolism ; Signal Transduction ; Genes, Plant ; Arabidopsis - embryology ; Transcription Factors - genetics ; DNA-Binding Proteins - genetics ; Arabidopsis - metabolism ; Arabidopsis - genetics ; Arabidopsis Proteins - metabolism ; DNA-Binding Proteins - metabolism ; Transcription Factors - metabolism ; Biological Transport, Active ; Gene Expression Regulation, Developmental ; Models, Biological ; Plant Roots - embryology ; Meristem - embryology ; Plants, Genetically Modified ; Gene Expression Regulation, Plant ; Meristem - metabolism ; Mutation ; Arabidopsis thaliana ; Proteins ; Embryonic development ; Index Medicus
    ISSN: 1534-5807
    E-ISSN: 1878-1551
    Source: Cell Press Collection [ECCPC]
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 8
    Language: English
    In: Developmental cell, 2012-01-17, Vol.22 (1), p.211-222
    Description: The cell types of the plant root are first specified early during embryogenesis and are maintained throughout plant life. Auxin plays an essential role in embryonic root initiation, in part through the action of the ARF5/MP transcription factor and its auxin-labile inhibitor IAA12/BDL. MP and BDL function in embryonic cells but promote auxin transport to adjacent extraembryonic suspensor cells, including the quiescent center precursor (hypophysis). Here we show that a cell-autonomous auxin response within this cell is required for root meristem initiation. ARF9 and redundant ARFs, and their inhibitor IAA10, act in suspensor cells to mediate hypophysis specification and, surprisingly, also to prevent transformation to embryo identity. ARF misexpression, and analysis of the short suspensor mutant, demonstrates that lineage-specific expression of these ARFs is required for normal embryo development. These results imply the existence of a prepattern for a cell-type-specific auxin response that underlies the auxin-dependent specification of embryonic cell types. ► Interdependent auxin responses mediate embryonic root formation ► Auxin controls extraembryonic identity of suspensor cells ► Lineage-specific ARF transcription factors direct cellular auxin response ► ARF expression is controlled by an early axis regulator
    Subject(s): root-meristem ; transcription factor ; expression map ; proteins ; aux/iaa genes ; seed development ; family ; transformation ; arabidopsis embryo ; monopteros ; Fundamental and applied biological sciences. Psychology ; Biological and medical sciences ; Cell physiology ; Molecular and cellular biology ; Cell differentiation, maturation, development, hematopoiesis ; Arabidopsis - drug effects ; Plant Roots - metabolism ; Seeds - metabolism ; Plants, Genetically Modified - genetics ; Signal Transduction ; Genes, Plant ; Plants, Genetically Modified - drug effects ; Seeds - drug effects ; Arabidopsis - embryology ; Arabidopsis - metabolism ; Plant Roots - drug effects ; Arabidopsis Proteins - metabolism ; Cell Lineage ; In Situ Hybridization ; Plants, Genetically Modified - metabolism ; Seeds - growth & development ; Indoleacetic Acids - pharmacology ; Plant Roots - embryology ; Gene Expression Regulation, Plant ; Fluorescence Resonance Energy Transfer ; ADP-Ribosylation Factor 1 - metabolism ; Plant Growth Regulators - pharmacology ; Embryonic development ; Embryo ; Plant physiology ; Developmental biology ; Analysis ; Index Medicus
    ISSN: 1534-5807
    E-ISSN: 1878-1551
    Source: Cell Press Collection [ECCPC]
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 9
    Language: English
    In: Genes & development, 2002-07-01, Vol.16 (13), p.1610-1615
    Description: Developmental responses to the plant hormone auxin are thought to be mediated by interacting pairs from two protein families: short-lived inhibitory IAA proteins and ARF transcription factors binding to auxin-response elements. monopteros mutants lacking activating ARF5 and the auxin-insensitive mutant bodenlos fail to initiate the root meristem during early embryogenesis. Here we show that the bodenlos phenotype results from an amino-acid exchange in the conserved degradation domain of IAA12. BODENLOS and MONOPTEROS interact in the yeast two-hybrid assay and the two genes are coexpressed in early embryogenesis, suggesting that BODENLOS inhibits MONOPTEROS action in root meristem initiation.
    Subject(s): Arabidopsis - genetics ; Promoter Regions, Genetic ; Phenotype ; Transcription Factors - physiology ; Arabidopsis Proteins ; Seeds - growth & development ; Genes, Plant ; Base Sequence ; Gene Expression Regulation ; Arabidopsis - embryology ; DNA Primers ; DNA-Binding Proteins ; Proteins ; Developmental genetics ; Auxin ; Arabidopsis ; Analysis ; Genetic research ; Physiological aspects ; Genetic aspects ; Research ; Gene expression ; Plant hormones ; Index Medicus ; root meristem initiation ; Research Communication ; BODENLOS ; MONOPTEROS ; auxin response ; embryo patterning
    ISSN: 0890-9369
    E-ISSN: 1549-5477
    Source: HighWire Press (Free Journals)
    Source: Cold Spring Harbor Laboratory Press
    Source: Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
    Source: PubMed Central
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 10
    Language: English
    Description: In Arabidopsis thaliana, the phytohormone auxin is an important patterning agent during embryogenesis and post-embryonic development, exerting effects through transcriptional regulation. The main determinants of the transcriptional auxin response machinery are AUXIN RESPONSE FACTOR (ARF) transcription factors and AUXIN/INDOLE-3-ACETIC ACID (AUX/IAA) inhibitors. Although members of these two protein families are major developmental regulators, the transcriptional regulation of the genes encoding them has not been well explored. For example, apart from auxin-linked regulatory inputs, factors regulating the expression of the AUX/IAA BODENLOS (BDL)/IAA12 are not known. Here, it was shown that the HOMEODOMAIN-LEUCINE ZIPPER (HD-ZIP) transcription factor HOMEOBOX PROTEIN 5 (HB5) negatively regulates BDL expression, which may contribute to the spatial control of BDL expression. As such, HB5 and probably other class I HD-ZIP proteins, appear to modulate BDL-dependent auxin response.
    Subject(s): HOMEODOMAIN ; OF-FUNCTION MUTATION ; PROTEIN ; REGULATED GENE-EXPRESSION ; auxin ; BODENLOS (BDL) ; Arabidopsis ; transcriptional regulation ; embryo ; PLANT DEVELOPMENT ; HOMEOBOX PROTEIN 5 (HB5) ; Biology and Life Sciences ; CLASS-I ; ROOT INITIATION ; SHADE AVOIDANCE ; AUXIN RESPONSE ; HOMEOBOX GENE
    ISSN: 0022-0957
    E-ISSN: 1460-2431
    Source: Ghent University Academic Bibliography
    Source: Alma/SFX Local Collection
    Source: Oxford Journals 2016 Current and Archive A-Z Collection
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