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  • 1
    Electronic Resource
    Electronic Resource
    Peanut growth as affected by liming, Ca-Mn interactions, and Cu plus Zn applications to oxidic samoan soils (1994)
    Springer
    Plant and soil 164 (1994), S. 203-211 
    Details
    ISSN: 1573-5036
    Keywords: Ca deficiency ; critical Ca level ; crop response ; liming ; Mn toxicity nutrient interaction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Effects of coralline lime, in combination with 3 kg Cu ha−1 plus 3 kg Zn ha−1, on yield and nutrient uptake by peanut (Arachis hypogea) were studied at three locations in Western Samoa. Coarse (0–10 mm) coralline lime material containing 31.1% Ca and 1.7% Mg was used as lime at 0, 555, 2222 and 5000 kg ha−1. In the Togitogiga soil, which had the lowest level of exchangeable Ca, peanut yield increased by 6 fold after liming with 555 kg ha−1, relative to the unamended control. This yield increase was associated with reduced Mn toxicity as well as reduced Ca deficiency. The alleviation of Mn toxicity was not likely due to decreased Mn solubility because the lime application (555 kg ha−1) increased soil pH by 〈0.1 unit. Rather it was the increased Ca availability which reduced the Mn toxicity through a Ca/Mn antagonism. The critical range of exchangeable Ca for peanut growth was found to be about 1.5–1.6 cmol 1/2Ca2+ kg−1. A Ca/Mn-ratio 〉80 was required for a desirable Ca/Mn balance in peanut tissue. On the other two locations (with exchangeable Ca levels of 1.5–1.6 cmol 1/2Ca2+ kg−1), liming increased peanut yields by 15–20%. Additions of Cu plus Zn also increased the yields, although the increases were small (7%) and not significant at the 95% probability level.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00010072
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  • 2
    Electronic Resource
    Electronic Resource
    Effects of coralline lime on nutrient uptake and yield of field-grown sweet corn and peanuts in Oxidic soils of Western Samoa (1993)
    Springer
    Nutrient cycling in agroecosystems 36 (1993), S. 211-219 
    Details
    ISSN: 1573-0867
    Keywords: banding ; broadcasting ; Ca deficiency ; crop response ; liming ; Mn toxicity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Effects of coralline lime on yield and nutrient uptake by sweet corn (Zea mays saccharata Sturt.) and peanut (Arachis hypogea) were studied at three locations in Western Samoa. Coarse (0-10 mm) coralline material containing 31.1% Ca and 1.67% Mg was used as lime. There were two modes of application: band and broadcast, and three rates: 6, 12 and 18 ton ha−1. In the highest rainfall location, marketable yields were increased by 250% for peanut and 160% for sweet corn by liming at 6 ton ha−1, relative to the unamended control. Peanut yield increases were associated with reduced Mn toxicity and/or with Ca and Mg deficiency. Sweet corn was less susceptible to Mn toxicity, but more responsive to exchangeable Ca. The critical level of exchangeable Ca was found to be about 2.0 cmol(+)kg−1. Applying lime to a band of 0.25-m wide did not reduce yield relative to broadcast. Soil cultivation caused the lime to spread over a wider band, diluting the applied calcium with a larger soil volume, suggesting that less than 6 ton ha−1 broadcast coarse coralline lime could still be adequate for most Samoan soils.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00748699
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  • 3
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    DNA repair. Proteomics reveals dynamic assembly of repair complexes during bypass of DNA cross-links (2015)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2015-05-02
    Description: DNA interstrand cross-links (ICLs) block replication fork progression by inhibiting DNA strand separation. Repair of ICLs requires sequential incisions, translesion DNA synthesis, and homologous recombination, but the full set of factors involved in these transactions remains unknown. We devised a technique called chromatin mass spectrometry (CHROMASS) to study protein recruitment dynamics during perturbed DNA replication in Xenopus egg extracts. Using CHROMASS, we systematically monitored protein assembly and disassembly on ICL-containing chromatin. Among numerous prospective DNA repair factors, we identified SLF1 and SLF2, which form a complex with RAD18 and together define a pathway that suppresses genome instability by recruiting the SMC5/6 cohesion complex to DNA lesions. Our study provides a global analysis of an entire DNA repair pathway and reveals the mechanism of SMC5/6 relocalization to damaged DNA in vertebrate cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Raschle, Markus -- Smeenk, Godelieve -- Hansen, Rebecca K -- Temu, Tikira -- Oka, Yasuyoshi -- Hein, Marco Y -- Nagaraj, Nagarjuna -- Long, David T -- Walter, Johannes C -- Hofmann, Kay -- Storchova, Zuzana -- Cox, Jurgen -- Bekker-Jensen, Simon -- Mailand, Niels -- Mann, Matthias -- HL098316/HL/NHLBI NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2015 May 1;348(6234):1253671. doi: 10.1126/science.1253671. Epub 2015 Apr 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany. ; Ubiquitin Signaling Group, Department of Disease Biology, Novo Nordisk Foundation Center for Protein Research, University of Copenhagen, DK-2200 Copenhagen, Denmark. ; Howard Hughes Medical Institute and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA. ; Institute of Genetics, University of Cologne, 50674 Cologne, Germany. ; Maintenance of Genome Stability Group, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany. ; Ubiquitin Signaling Group, Department of Disease Biology, Novo Nordisk Foundation Center for Protein Research, University of Copenhagen, DK-2200 Copenhagen, Denmark. simon.bekker-jensen@cpr.ku.dk niels.mailand@cpr.ku.dk mmann@biochem.mpg.de. ; Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany. Novo Nordisk Foundation Center for Protein Research, Proteomics Program, University of Copenhagen, DK-2200 Copenhagen, Denmark. simon.bekker-jensen@cpr.ku.dk niels.mailand@cpr.ku.dk mmann@biochem.mpg.de.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25931565" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromatin/chemistry/metabolism ; *DNA Damage ; *DNA Repair ; DNA Repair Enzymes/*metabolism ; *DNA Replication ; DNA-Binding Proteins/metabolism ; Mass Spectrometry/methods ; Proteomics/methods ; RNA-Binding Proteins/metabolism ; Xenopus
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Histone H1 couples initiation and amplification of ubiquitin signalling after DNA damage (2015)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2015-10-28
    Description: DNA double-strand breaks (DSBs) are highly cytotoxic DNA lesions that trigger non-proteolytic ubiquitylation of adjacent chromatin areas to generate binding sites for DNA repair factors. This depends on the sequential actions of the E3 ubiquitin ligases RNF8 and RNF168 (refs 1-6), and UBC13 (also known as UBE2N), an E2 ubiquitin-conjugating enzyme that specifically generates K63-linked ubiquitin chains. Whereas RNF168 is known to catalyse ubiquitylation of H2A-type histones, leading to the recruitment of repair factors such as 53BP1 (refs 8-10), the critical substrates of RNF8 and K63-linked ubiquitylation remain elusive. Here we elucidate how RNF8 and UBC13 promote recruitment of RNF168 and downstream factors to DSB sites in human cells. We establish that UBC13-dependent K63-linked ubiquitylation at DSB sites is predominantly mediated by RNF8 but not RNF168, and that H1-type linker histones, but not core histones, represent major chromatin-associated targets of this modification. The RNF168 module (UDM1) recognizing RNF8-generated ubiquitylations is a high-affinity reader of K63-ubiquitylated H1, mechanistically explaining the essential roles of RNF8 and UBC13 in recruiting RNF168 to DSBs. Consistently, reduced expression or chromatin association of linker histones impair accumulation of K63-linked ubiquitin conjugates and repair factors at DSB-flanking chromatin. These results identify histone H1 as a key target of RNF8-UBC13 in DSB signalling and expand the concept of the histone code by showing that posttranslational modifications of linker histones can serve as important marks for recognition by factors involved in genome stability maintenance, and possibly beyond.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thorslund, Tina -- Ripplinger, Anita -- Hoffmann, Saskia -- Wild, Thomas -- Uckelmann, Michael -- Villumsen, Bine -- Narita, Takeo -- Sixma, Titia K -- Choudhary, Chunaram -- Bekker-Jensen, Simon -- Mailand, Niels -- England -- Nature. 2015 Nov 19;527(7578):389-93. doi: 10.1038/nature15401. Epub 2015 Oct 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ubiquitin Signaling Group, Protein Signaling Program, The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, DK-2200 Copenhagen, Denmark. ; Proteomics Program, The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, DK-2200 Copenhagen, Denmark. ; Division of Biochemistry, Cancer Genomics Center, Netherlands Cancer Institute, 1066 CX Amsterdam, the Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26503038" target="_blank"〉PubMed〈/a〉
    Keywords: Chromatin/metabolism ; DNA Breaks, Double-Stranded ; *DNA Damage ; DNA Repair ; DNA-Binding Proteins/metabolism ; Histones/chemistry/*metabolism ; Humans ; Lysine/metabolism ; Protein Structure, Tertiary ; *Signal Transduction ; Ubiquitin/*metabolism ; Ubiquitin-Conjugating Enzymes/metabolism ; Ubiquitin-Protein Ligases/chemistry/metabolism ; Ubiquitination
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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