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  • 1
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 110 (2000), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Many DNA transactions such as transcription and recombination are regulated by the formation of specific higher-order nucleoprotein structures. Multiple protein/DNA and protein/protein interactions act synergistically to provide the precision required for the regulation of these processes. The assembly of the nucleoprotein complexes often requires that the DNA is specifically folded by DNA-bending proteins. In plants, various chromatin-associated high mobility group (HMG) proteins of the HMG1 and HMGI/Y families have been identified which have the potential to act as architectural factors that modulate DNA structure. In addition, by protein/protein-contacts these proteins assist the binding of regulatory factors to their cognate DNA sites. Therefore, the HMG1 and HMGI/Y proteins might be involved as architectural factors in the regulation of various biological processes.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-2048
    Keywords: External spacer region ; DNA curvature ; Protein/DNA interactions ; High-mobility-group protein ; Zea (DNA)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The 3-kb external spacer from a maize (Zea mays L. cv. A619) nuclear rRNA gene unit which contains nine highly homologous 200-bp repeat elements was found to include a region with DNA-curvature properties. The centre of curvature was localized within repeats 5 and 6 using a circular permutation assay. A 60-bp-long subfragment of this region was found to interact with nuclear proteins, including high-mobility-group (HMG) proteins, and with the maize HMGa protein synthesized in Escherichia coli from a recombinant plasmid. The potential influence of the binding of the HMG proteins on the conformation of this subfragment was studied with a permutation assay based on a bending vector.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Planta 185 (1991), S. 350-355 
    ISSN: 1432-2048
    Keywords: Chromosomal proteins ; DNA binding proteins ; Protein (chromosoma) ; Zea (chromosomal proteins)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Chromosomal nonhistone high-mobility-group (HMG) proteins were purified from nuclei of maize (Zea mays L. cv. A619) endosperm and leaf tissue. Tissuespecific differences were observed in their polypeptide patterns, in in-vitro phosphorylation experiments with a casein-kinase type II, and by Western blot analysis with antisera against different HMG proteins. Gelfiltration chromatography demonstrated that maize HMG proteins occur as monomers. By measuring the capacity of the HMG proteins to bind to the 5′ flanking region of a zein gene, the sensitivity of the proteins to different temperatures, salt concentrations and pH values was determined.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Plant molecular biology 41 (1999), S. 351-361 
    ISSN: 1573-5028
    Keywords: chromatin ; gene expression ; high-mobility-group protein HMG1 ; HMGe ; protein stability ; Zea mays
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The nuclear HMG1 proteins of higher plants are small non-histone proteins that have DNA-bending activity and are considered architectural factors in chromatin. The occurrence of the chromosomal HMG1 proteins, HMGa, HMGc1/2 and HMGd, in various maize tissues was analyzed, and in the course of these studies a novel HMG1 protein, now termed HMGe, was identified. Purification and characterization of HMGe (Mr 13 655) and cloning of the corresponding cDNA revealed that it displays only moderate similarity to other members of the plant HMG1 protein family. The five maize HMG1 proteins could be detected in kernels, leaves, roots and suspension culture cells, indicating that these proteins can be expressed simultaneously and occur relatively ubiquitously. However, the various HMG1 proteins are present in significantly different quantities with HMGa and HMGc1/2 being the most abundant HMG1 proteins in all tissues tested. Furthermore, the relative amounts of the various HMG1 proteins differ among the tissues examined. The HMG1 proteins were found to be relatively stable proteins in vivo, with HMGc1/2, HMGd and HMGe having a half-life of ca. 50 h in cultured cells, while the half-life of the HMGa protein is ca. 65 h. Collectively, these findings are compatible with the concept that the different plant HMG1 proteins might act as general architectural proteins in concert with site-specific factors in the assembly of certain nucleoprotein structures involved in various biological processes.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1573-5028
    Keywords: chromatin ; high-mobility-group (HMG) proteins ; Vicia faba ; Zea mays
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Chromosomal high-mobility-group (HMG) proteins occur ubiquitously in eukaryotes and their common structural and biochemical features indicate a critical role. In this context, we compared structural and functional aspects of HMG proteins from the monocotyledonous plant maize and the dicotyledonous plant Vicia faba. Besides biochemical similarities and immunological differences found between these proteins, the isolation and characterization of a cDNA encoding the V. faba homologue of the maize HMGa protein revealed great similarities between these two proteins, including the HMG-box DNA-binding motif and an acidic domain. Therefore, like the maize HMGa protein, the V. faba HMG protein belongs to the vertebrate HMG1 family, which consists of HMG proteins and transcription factors of various eukaryotes.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Plant molecular biology 25 (1994), S. 565-568 
    ISSN: 1573-5028
    Keywords: chromatin ; high-mobility-group (HMG) proteins ; protein stability ; Zea mays
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Chromosomal non-histone high-mobility-group (HMG) proteins represent essential components of eukaryotic chromatin and have also been isolated from a variety of plants. In maize, studies on structure and function of the two larger of the four major HMG proteins have recently been performed and are now extended by analysis of theirin vivo stability using pulse-chase experiments in a cell suspension culture. The half-life of the analyzed HMGa and HMGb proteins was found to be 65 h or more than 78 h, respectively.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 221 (1990), S. 164-170 
    ISSN: 1617-4623
    Keywords: Zea mays ; Zein ; P2 promoter ; Transcription factors ; HMG protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A 216 by promoter fragment of the 19 kDa protein zein gene pMS1, containing the CCAAT and TATA boxes, was analysed by a variety of techniques for in vitro interactions with nuclear proteins from endosperm tissue. HMG proteins were found to form stable complexes with these A/T-rich promoter sequences and several specific DNA-binding proteins appear to be involved in the formation of DNA-protein complexes with this fragment. A 29 bp region spanning the two CCAAT boxes was protected from DNase I digestion in footprinting experiments.
    Type of Medium: Electronic Resource
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