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  • 1
    Electronic Resource
    Electronic Resource
    Homologues of wheat ubiquitin-conjugating enzymes - TaUBC1 and TaUBC4 are encoded by small multigene families in Arabidopsis thaliana (1994)
    Springer
    Plant molecular biology 24 (1994), S. 651-661 
    Details
    ISSN: 1573-5028
    Keywords: protein degradation ; ubiquitin conjugating enzymes ; DNA repair ; N-end recognition ; wheat ; Arabidopsis thaliana
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Covalent attachment of ubiquitin to other cellular proteins has been implicated in a multitude of diverse physiological processes in eukaryotes including selective protein degradation. This attachment is carried out by a multi-enzyme pathway consisting of three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s), and ubiquitin-protein ligases (E3s). E2s accept activated ubiquitin from E1 and conjugate it to target proteins with or without the participation of specific E3s. Previously, we have isolated wheat cDNAs encoding 16 and 23 kDa E2s, TaUBC1 and TaUBC4, respectively. TaUBC1 shows structural homology to the yeast RAD6 E2 that is essential for DNA repair whereas TaUBC4 is related to the yeast ScUBC8 E2, both of which effectively conjugate ubiquitin to histones in vitro but as yet are without a known in vivo function. Here, we report the isolation of genomic and cDNA homologues of these genes from Arabidopsis thaliana. In Arabidopsis, both of these E2s are encoded by three member gene families. Members of the AtUBC1 gene family, comprising AtUBC1, 2 and 3, encode 150–152 amino acid proteins that are 83–99% identical to each other and TaUBC1 and contain four introns that are conserved with respect to position. Members of the AtUBC4 gene family, comprising AtUBC4, 5 and 6, encode 187–191 amino acid proteins that are 73–88% identical to each other and TaUBC4 and contain five introns that are conserved with respect to position. In contrast, AtUBC1-3 gene products are only 31–36% identical to those derived from AtUBC4-6. mRNA for each family was detected in Arabidopsis roots, leaves, stems, and flowers indicating that members of each family are expressed in most if not all tissues.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00023561
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  • 2
    Electronic Resource
    Electronic Resource
    Proteolysis in plants: mechanisms and functions (1996)
    Springer
    Plant molecular biology 32 (1996), S. 275-302 
    Details
    ISSN: 1573-5028
    Keywords: Arabidopsis ; biotechnology ; ClpAP protease ; protein degradation ; 20S and 26S proteasome ; ubiquitin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Proteolysis is essential for many aspects of plant physiology and development. It is responsible for cellular housekeeping and the stress response by removing abnormal/misfolded proteins, for supplying amino acids needed to make new proteins, for assisting in the maturation of zymogens and peptide hormones by limited cleavages, for controlling metabolism, homeosis, and development by reducing the abundance of key enzymes and regulatory proteins, and for the programmed cell death of specific plant organs or cells. It also has potential biotechnological ramification in attempts to improve crop plants by modifying protein levels. Accumulating evidence indicates that protein degradation in plants is a complex process involving a multitude of proteolytic pathways with each cellular compartment likely to have one or more. Many of these have homologous pathways in bacteria and animals. Examples include the chloroplast ClpAP protease, vacuolar cathepsins, the KEX2-like proteases of the secretory system, and the ubiquitin/26S proteasome system in the nucleus and cytoplasm. The ubiquitin-dependent pathway requires that proteins targeted for degradation become conjugated with chains of multiple ubiquitins; these chains then serve as recognition signals for selective degradation by the 26S proteasome, a 1.5 MDa multisubunit protease complex. The ubiquitin pathway is particularly important for developmental regulation by selectively removing various cell-cycle effectors, transcription factors, and cell receptors such as phytochrome A. From insights into this and other proteolytic pathways, the use of phosphorylation/dephosphorylation and/or the addition of amino acid tags to selectively mark proteins for degradation have become recurring themes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00039386
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  • 3
    Electronic Resource
    Electronic Resource
    Polypeptide tags, ubiquitous modifiers for plant protein regulation (1999)
    Springer
    Plant molecular biology 41 (1999), S. 435-442 
    Details
    ISSN: 1573-5028
    Keywords: APG12 ; protein degradation ; protein modification ; RUB ; SUMO ; ubiquitin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Evidence has emerged over the past few years that plants, like animals and fungi, employ a variety of polypeptides as tags to reversibly or irreversibly affect the function, structure, location, and/or turnover of numerous intracellular proteins. In plants, known polypeptide tags include ubiquitin, SUMO, RUB, and APG12, with the possibility of others. These modifiers are typically added post-translationally using individual sets of conjugase pathways that attach the polypeptides via an isopeptide bond to ε-lysyl amino group(s) in the targets. Often the tags can be removed subsequently by unique proteases that specifically cleave only the isopeptide bond. Examples also exist where the tag is added during translation upon fusion of the coding sequence of the tag with that of the target. Based on the number and diversity of targets, ubiquitin is the most influential modifier which mainly serves as a reusable signal for selective protein degradation by the 26S proteasome. In contrast, SUMO, RUB and APG12 become attached to a more limited number of targets and appear to have specialized functions, including roles in nuclear pore assembly/function, cell-cycle regulation, and lysosomal/vacuole trafficking, respectively. Based on their widespread occurrence in plants and their pervasive role in various biological processes, polypeptide tags likely play a prominent role in plant cell regulation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006323317890
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