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  • 1
    Electronic Resource
    Electronic Resource
    14-3-3 proteins: regulation of signal-induced events (2004)
    Oxford, UK; Malden , USA : Munksgaard International Publishers
    Physiologia plantarum 120 (2004), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The field of signal transduction has experienced a significant paradigm shift as a result of an increased understanding of the roles of 14-3-3 proteins. There are many cases where signal-induced phosphorylation itself may cause a change in protein function. This simple modification is, in fact, the primary basis of signal transduction events in many systems. There are a large and growing number of cases, however, where simple phosphorylation is not enough to effect a change in protein function. In these cases, the 14-3-3 proteins can be required to complete the change in function. Therefore signal transduction can be either the relatively simple process where phosphorylation alters target activity, or it can be a more complex, multistep process with the 14-3-3 proteins playing the major role of bringing the signal transduction event to completion. This makes 14-3-3-modulated signal transduction a more complicated process with additional avenues for regulation and variety. Adding further complexity to the process is the fact that 14-3-3 proteins are present as multigene families in most organisms (Aitken et al. Trends Biochem Sci 17: 498–501, 1992; Ferl Annu Rev Plant Physiol Plant Molecular Biology 47: 49–73, 1996), with each member of the family being differentially expressed in various tissues and with potentially differential affinity for various target proteins. This review focuses on the 14-3-3 family of Arabidopsis as a model for further developing understanding of the roles of the 14-3-3 proteins as modulators of signal transduction events in plants. The primary approaches to these questions are not unlike the approaches that would be used in the functional dissection of any multigene family, but the interpretation of these data will have wide implications since the 14-3-3 s physically interact with other protein families.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.0031-9317.2004.0239.x
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  • 2
    Electronic Resource
    Electronic Resource
    14-3-3 PROTEINS AND SIGNAL TRANSDUCTION (1996)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Plant Physiology and Plant Molecular Biology 47 (1996), S. 49-73 
    Details
    ISSN: 1040-2519
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Notes: Abstract Perhaps in keeping with their enigmatic name, 14-3-3 proteins offer a seemingly bewildering array of opportunities for interaction with signal transduction pathways. In each organism there are many isoforms that can form both homo- and heterodimers, and many biochemical activities have been attributed to the 14-3-3 group. The potential for diversity-and also confusion-is high. The mammalian literature on 14-3-3 proteins provides an appropriate context to appreciate the potential roles of 14-3-3s in plant signal transduction pathways. In addition, functional and structural themes emerge when 14-3-3s are examined and compiled in ways that draw attention to their participation in protein phosphorylation and protein-protein interactions. These themes allow examination of plant 14-3-3s from two perspectives: the ways in which plant 14-3- 3s contribute to and extend ideas already described in animals, and the ways that plant 14-3-3s present unique contributions to the field. The crystal structure of an animal 14-3- 3 has been solved. When considered with the evolutionary stability of large segments of the 14-3-3 protein, the structure illuminates several aspects of 14-3-3 function. However, diversity in other regions of the 14-3-3s and their presence as multigene families offer many opportunities for cell-specific specialization of individual functions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.arplant.47.1.49
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  • 3
    Electronic Resource
    Electronic Resource
    Evolution of the 14-3-3 Protein Family: Does the Large Number of Isoforms in Multicellular Organisms Reflect Functional Specificity? (2000)
    Springer
    Journal of molecular evolution 51 (2000), S. 446-458 
    Details
    ISSN: 1432-1432
    Keywords: Key words: 14-3-3 — Isoforms — Functional specificity — Affinity — H+ATPase — Phylogeny — Surface plasmon resonance
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. 14-3-3 proteins constitute a family of eukaryotic proteins that are key regulators of a large number of processes ranging from mitosis to apoptosis. 14-3-3s function as dimers and bind to particular motifs in their target proteins. To date, 14-3-3s have been implicated in regulation or stabilization of more than 35 different proteins. This number is probably only a fraction of the number of proteins that 14-3-3s bind to, as reports of new target proteins have become more frequent. An examination of 14-3-3 entries in the public databases reveals 153 isoforms, including alleloforms, reported in 48 different species. The number of isoforms range from 2, in the unicellular organism Saccharomyces cerevisiae, to 12 in the multicellular organism Arabidopsis thaliana. A phylogenetic analysis reveals that there are four major evolutionary lineages: Viridiplantae (plants), Fungi, Alveolata, and Metazoa (animals). A close examination of the aligned amino acid sequences identifies conserved amino acid residues and regions of importance for monomer stabilization, dimer formation, target protein binding, and the nuclear export function. Given the fact that 53% of the protein is conserved, including all amino acid residues in the target binding groove of the 14-3-3 monomer, one might expect little to no isoform specificity for target protein binding. However, using surface plasmon resonance we show that there are large differences in affinity between nine 14-3-3 isoforms of A. thaliana and a target peptide representing a novel binding motif present in the C terminus of the plant plasma membrane H+ATPase. Thus, our data suggest that one reason for the large number of isoforms found in multicellular organisms is isoform-specific functions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002390010107
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  • 4
    Electronic Resource
    Electronic Resource
    Detection of cytosine methylation in the maize alcohol dehydrogenase gene by genomic sequencing (1986)
    [s.l.] : Nature Publishing Group
    Nature 319 (1986), S. 243-246 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Restriction endonucleases whose activity is blocked when their recognition site is methylated have been used to detect modified C-G sites in the genome12'13. However, even with the ability to use additional enzymes such as Pstl and Pvull (r(c)f. 14) for methylation analysis in plants, restriction ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/319243a0
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  • 5
    Electronic Resource
    Electronic Resource
    In vitro translation of maize ADH: Evidence for the anaerobic induction of mRNA (1980)
    Springer
    Biochemical genetics 18 (1980), S. 681-691 
    Details
    ISSN: 1573-4927
    Keywords: maize ; alcohol dehydrogenase ; mRNA ; in vitro translation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Total cellular RNA from anaerobically stressed maize seedling roots was used to stimulate in vitro translation of authentic maize alcohol dehydrogenase (ADH) in a rabbit reticulocyte lysate system. Total products from such reactions were displayed on NEPHGE-SDS two-dimensional gels and the Adhl-specific translation products were identified by using RNA from sib seedlings segregating for Adhl charge and size variants. The application of a rapid RNA isolation procedure allowed the efficient isolation of biologically active RNAs from small amounts of seedling material. Maize ADHs translated in vitro are identical in size to in vivo ADH. Further, no ADH was detected in the products of an in vitro translation reaction stimulated by total RNA from aerobically grown seedlings. This suggests that induction of ADH protein by anaerobic stress is accomplished by production of Adh mRNA rather than activation of sequestered mRNA. The mRNAs for maize ADH1 and ADH2 are among a small class of mRNAs induced during anaerobiosis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00484585
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  • 6
    Electronic Resource
    Electronic Resource
    Site-specific oligodeoxynucleotide binding to maize Adh1 gene promoter represses Adh1-GUS gene expression in vivo (1992)
    Springer
    Plant molecular biology 19 (1992), S. 715-723 
    Details
    ISSN: 1573-5028
    Keywords: DNase I footprinting ; β-glucuronidase (GUS) ; H-DNA ; transformation ; triple helix
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract There is a 36 bp tract of extreme homopurine/homopyrimidine (PuPy) asymmetry in the maize Adh1 gene promoter (from −44 to −79) that is S1-hypersensitive in plasmids under supercoil tension. Oligodeoxynucleotides corresponding to the PuPy tract were designed to examine the secondary structure of the region and address the possible role of the tract in gene regulation. On the basis of oligodeoxynucleotide band-shift and DNase I footprinting analyses, it was concluded that the homopyrimidine oligodeoxynucleotide can form a triple helix with the duplex PuPy tract in vitro. Transient assays in protoplasts, suspension cells, and seedling roots show that the homopyrimidine oligodeoxynucleotide is also capable of repressing Adh1-GUS gene expression during co-transformation, presumably by the formation of a triple helix with the PuPy tract in vivo. The complementary homopurine oligodeoxynucleotide would not form a triple helix in vitro, nor would it repress Adh1-GUS in vivo. We propose that triple helix formation is a potential regulatory phenomenon in vivo, and that an intraregion triple helix could occur within the Adh1 promoter via the formation of H-DNA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00027068
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  • 7
    Electronic Resource
    Electronic Resource
    Chemical detection of Z-DNA within the maize Adh1 promoter (1992)
    Springer
    Plant molecular biology 18 (1992), S. 1181-1184 
    Details
    ISSN: 1573-5028
    Keywords: alcohol dehydrogenase-1 ; maize ; plant ; promoter ; Z-DNA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Z-DNA is a left-handed helix which can form within tracts of alternating purines and pyrimidines. Tracts of potential Z-DNA identified by sequence inspection are often noted within regulatory portions of genes, but evidence that these tracts of sequence actually exist as Z-DNA is very limited, and not available for any plant gene. In this study, the chemical probes osmium tetroxide, diethylpyrocarbonate and hydroxylamine were used to show that a tract of alternating purines and pyrimidines in the Adh1 promoter (from -311 to -325) actually assumes a Z-DNA conformation under superhelical stress in vitro.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00047722
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  • 8
    Electronic Resource
    Electronic Resource
    Osmium tetroxide footprinting of a scaffold attachment region in the maizeAdh1 promoter (1993)
    Springer
    Plant molecular biology 22 (1993), S. 1145-1151 
    Details
    ISSN: 1573-5028
    Keywords: alcohol dehydrogenase ; chromatin ; plant ; nuclear matrix ; SAR
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Osmium tetroxide (OsO4) reacts with the thymine residues of double-stranded DNA, but thymines that are unpaired or under torsional stress are hyperreactive. Although OsO4 hyperreactivity has been primarily utilized to identify Z-DNA structures in supercoiled plasmids, OsO4 will also identify other torsional perturbations of DNA. In this study, OsO4 was used to footprint an AT-rich region (between −780 and −500) of the maizeAdh1 promoter. Hyperreactive sites were identified bothin vitro andin vivo in an area that coincides with AT motifs similar to those found in scaffold attachment regions. Further, the region of OsO4 hyperreactivity lies within a fragment of DNA that is associated with the nuclear scaffold in histone-depleted nuclei.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00028983
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  • 9
    Electronic Resource
    Electronic Resource
    Partial sequencing and mapping of clones from two maize cDNA libraries (1994)
    Springer
    Plant molecular biology 26 (1994), S. 1085-1101 
    Details
    ISSN: 1573-5028
    Keywords: cDNA clones ; EST sequencing ; maize ; RFLP mapping
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract As one component of a maize genome project, we report the analysis of a number of randomly selected cDNAs, by a combination of measuring mRNA expression, ‘single-pass’ sequencing (SPS), and genome mapping. Etiolated seedling (490) and membrane-free polysomal endosperm cDNA clones (576) were evaluated for their transcription levels by hybridizing with a probe prepared from total mRNA and categorized as corresponding to abundantly or rarely expressed mRNAs and as either constitutive or tissue-specific. A total of 313 clones from the two libraries were submitted to ‘single-pass’ sequencing from the presumed 5′ end of the mRNA and the nucleotide sequence compared with the GenBank database. About 61% of the clones showed no significant similarities within GenBank, 14% of the clones exhibited a high degree of similarity, while the remaining 25% exhibited a lesser degree of similarity. The chromosomal location of more than 300 clones was determined by RFLP mapping using standard populations. The results demonstrate that a combination of analyses provides synergistic information in eventually deducing the actual function of these types of clones.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00040691
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  • 10
    Electronic Resource
    Electronic Resource
    In vivo detection of regulatory factor binding sites of Arabidopsis thaliana Adh (1989)
    Springer
    Plant molecular biology 12 (1989), S. 357-366 
    Details
    ISSN: 1573-5028
    Keywords: trans-acting factor ; protein-DNA interactions ; transcriptional control ; anaerobic response
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In vivo footprinting experiments have been used to analyze the binding of trans-acting regulatory factors in the 5′ flanking region upstream of the alcohol dehydrogenase (Adh) gene from Arabidopsis thaliana. Protein-DNA interactions were detected by dimethyl sulfate footprinting and genomic sequencing, using an A. thaliana cell suspension culture that constitutively expressed the Adh gene. Several distinct footprinting domains have been characterized, and the potential effects of the corresponding trans-acting factors have been inferred from a comparison with data from the maize alcohol dehydrogenase-1 (Adh1) gene. One binding site is similar in sequence to one of the anaerobic response elements (ARE) of the maize gene, which has also been shown to bind to a trans-acting factor. Several of the remaining binding sites apparently represent a class of elements sharing the sequence 5′-GTGG-3′ within their footprint. Comparisons with maize Adh1 in vivo protein interactions reveal that the elements of Adh promoter structure are highly conserved, but the relative and absolute positions of the elements are variable.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00017576
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