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  • expression  (2)
  • Surface physics, nanoscale physics, low-dimensional systems  (1)
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Plant molecular biology 26 (1994), S. 1611-1636 
    ISSN: 1573-5028
    Keywords: guanine nucleotide-binding proteins ; heterotrimeric G proteins ; small G proteins ; blochemical detection ; cDNAs ; expression ; yeast complementation ; transgenic plants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Regulatory guanine nucleotide-binding proteins (G proteins) have been studied extensively in animal and microbial organisms, and they are divided into the heterotrimeric and the small (monomeric) classes. Heterotrimeric G proteins are known to mediate signal responses in a variety of pathways in animals and simple eukaryotes, whiole small G proteins perform diverse functions including signal transduction, secretion, and regulation of cytoskeleton. In recent years, biochemical analyses have produced a large amount of information on the presence and possible functions of G proteins in plants. Further, molecular cloning has clearly demonstrated that plants have both heterotrimeric and small G proteins. Although the functions of the plant heterotrimeric G proteins are yet to be determined, expression analysis of an Arabidopsis Gα protein suggests that it may be involved in the regulation of cell division and differentiation. In contrast to the very few genes cloned thus far that encode heterotrimeric G proteins in plants, a large number of small G proteins have been identified by molecular cloning from various plants. In addition, several plant small G proteins have been shown to be functional homologues of their counterparts in animals and yeasts. Future studies using a number of approaches are likely to yield insights into the role plant G proteins play.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-5028
    Keywords: Arabidopsis ; expression ; glutamine-rich region ; MADS-box gene ; DNA binding ; consensus sequence ; CArG box
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The Arabidopsis AGL3 gene was previously identified on the basis of sequence similarity to the floral homeotic gene AGAMOUS (AG), which encodes a protein with a conserved MADS domain that is also found in human and yeast transcription factors (SRF and MCM1, respectively). Analysis of newly isolated full-length cDNA clones as well as genomic clones indicates that AGL3 is indeed a MADS-box gene with a general intron-exon structure similar to other plant MADS-box genes. However, unlike the others, which are expressed specifically in flowers, AGL3 is expressed in all above-ground vegetative organs, as well as in flowers, but not in roots. Furthermore, since AGL3 is MADS-domain protein, it is likely that it is also a DNA-binding protein regulating transcription. To characterize AGL3 as a DNA-binding protein in vitro, we expressed the AGL3 protein in Escherichia coli, and characterized its DNA-binding properties. We show that AGL3 binds to sequences which resemble the target sequences of SRF and MCM1, and have determined the consensus sequence to which AGL3 binds using random oligonucleotides. These results suggest that AGL3 is a widely distributed DNA-binding protein, which may be involved the transcriptional regulation of genes in many cells.
    Type of Medium: Electronic Resource
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  • 3
    Publication Date: 2017-05-10
    Description: Author(s): Jia-Bin Qiao, Yue Gong, Wei-Jie Zuo, Yi-Cong Wei, Dong-Lin Ma, Hong Yang, Ning Yang, Kai-Yao Qiao, Jin-An Shi, Lin Gu, and Lin He Assembling different two-dimensional (2D) crystals, covering a very broad range of properties, into van der Waals (vdW) heterostructures enables unprecedented possibilities for combining the best of different ingredients in one objective material. So far, metallic, semiconducting, and insulating 2D … [Phys. Rev. B 95, 201403(R)] Published Mon May 08, 2017
    Keywords: Surface physics, nanoscale physics, low-dimensional systems
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
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