1,358,693 research outputs found

    Maria von Trapp Visit to Rock Hill Records - Accession 1615 - M794 (851)

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    This collection consists of materials related to a visit to Rock Hill, SC by Maria (Kutschera) von Trapp (1905-1987) in April 1978. Maria gained fame as the inspiration for the Broadway musical (1959) and movie musical (1965), The Sound of Music which was based on her book The Story of the Trapp Family Singers (1949). Maria was the stepmother and matriarch of the Austrian singing family, the Trapp Family Singers. The group was comprised of Maria and her seven stepchildren through her marriage to Captain Georg von Trapp (1880-1947). They began their career in Europe, but after Germany annexed Austria the family located to the United States and began touring the Us and Canada. In 1976, the United Methodist Women at St. Johns United Methodist Church in Rock Hill, SC initiated a request to Maria von Trapp to see if she would be interested in visiting as a lecturer for a planned Arts festival held at St. Johns. She eventually agreed and arrived on April 11, 1978, had dinner with the Hornsby Family, gave her lecture, and stayed overnight at the Howard Johnson Motel in Rock Hill. She departed on April 12, 1978. This collection consists of correspondence discussing the possible visit, a photocopy of a newspaper article concerning her visit, several receipts of her stay, and a brief biographical write-up of her and her visit.https://digitalcommons.winthrop.edu/manuscriptcollection_findingaids/2748/thumbnail.jp

    Supplementary Data to PhD thesis 'Earth's Weathering Continuum' (Gerrit Trapp-Müller)

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    The chemical weathering of rocks, e.g., during soil formation, leads to a global scale redistribution of the chemical elements. Weathering on land typically releases nutrients otherwise trapped in rocks and transforms atmospheric carbon dioxide (CO2 dissolved in rain) to dissolved bicarbonate (HCO3-) at rates that appear to accelerate in a warming climate. Because CO2 has a warming effect on climate (‘greenhouse’ effect), weathering is thought to exert carbon-cycle feedback that stabilizes life-supporting Earth surface conditions on long, geological timescales. The relevant timescales depend on the material weathered: Limestone (carbonate minerals, mostly (Ca,Mg)CO3) weathers rapidly but its chemical effects are largely reversed by biological calcification (CaCO3 biomineralization) in the ocean after ~ 50,000 – 100,000 years. However, reorganisation of carbonate sources and sinks within the ocean can drive long-term effects. The bicarbonate released during weathering of silicate rocks (various Si-based minerals) is only partly offset by calcification, hence silicate weathering net sequesters atmospheric CO2, and it also adds salts and nutrients to the oceans. However, despite this relevance to seawater chemistry and Earth system regulation, the role of the weathering feedback and its relationship to biology, tectonics and climate remain enigmatic, impeding our understanding of past and future Earth system evolution. Traditionally, the weathering of continental and oceanic crusts is considered in biogeochemical cycles and Earth system models, but many biogeochemical budgets cannot yet consentaneously be balanced. Moreover, variable weathering responses to carbon cycle perturbations have been demonstrated and remain to be consistently explained. In contrast, the weathering of eroded soils and rocks in marine sediments has largely been ignored, although the widespread occurrence and its relevance to Earth system dynamics have been demonstrated quite early (Chapter 1). We now know that marine sediment weathering quantitatively rivals crustal and land weathering, but the magnitude and even direction of the corresponding chemical fluxes (incl. CO2) vary extensively between different settings and even with depth and time at individual locations. In this PhD thesis, I systematically investigate the role of marine sediment weathering, i.e., chemical reactions between rock and soil-derived minerals, biological remains and seawater, in the global cycles of the element and in the regulation of planetary conditions. Because most of the sediment on the ocean margins originates from land and is transported by rivers, I assembled a comprehensible reference database of river sediment composition (GloRiSe, Chapter 2). This allowed mapping how much of which particle type is discharged by which rivers and what governs the relative abundances of different particles. By comparing the database to various maps of the Earth’s surface and applying statistical techniques, a seamless, global map of eroded limestone fragments (‘detrital carbonates’) discharge by rivers to the ocean was derived (Chapter 3). These data point to a quantitative significance of riverine detrital carbonates for the global biogeochemical cycles of carbon, calcium, alkalinity, and strontium. This detrital carbonate flux was not previously considered and narrows gaps that persisted in corresponding biogeochemical cycles for decades. Variation with hydroclimate, land surface properties and tectonically controlled distributions of limestones are the main factors governing the detrital carbonate fluxes. Challenges remain in the assessment of non-riverine sources of detrital carbonate, particularly coastal erosion, and in quantifying the fate of these minerals in the ocean, where they may either dissolve into seawater or act as ‘seeds’ for inorganic carbonate precipitation from seawater. The remainder of the sediment reaching the ocean is largely made of eroded silicate rock fragments and soil materials, including clays, organic matter, and metal (oxy-)hydroxides (rust). Our data support the view that weathering intensities on land are highest in tropical rivers (latitudinal pattern), broadly consistent with the traditional view of the weathering feedback. Moreover, our database revealed a prominent role of bedrock types and that the degree of weathering of river sediments often increases downstream, emphasizing the roles of tectonics, topography, and hydrology in determining material export fluxes. These data demonstrate significant, climate-dependent pre-processing of these materials before they reach the coasts, with implications for their fate in the ocean. Deltas are the main entry point for sediment in the ocean and represent dynamic and efficient chemical reactors. Using a chemical reaction model, we found systematic weathering patterns in such deltaic sediments (Chapter 5). Acidification, CO2 mobilization, and element consumption (K, Mg, Fe, Si) through so-called ‘reverse’ weathering is promoted in seasonally reworked, low-latitude deltaic muds, where iron-rich ‘green clays’ form rapidly from reactions of lateritic soil materials and plankton remains (including SiO2 biominerals). In contrast, element release (Na, Ca, Mg, Fe, Si), carbon storage and/or alkalinization by sediment weathering are most likely where pristine rock fragments and ashes weather in organic-rich and methane-generating sediments. These reactions would be promoted on continental slopes with nearby mountains and volcanoes, and at high latitudes, where physical erosion readily provides relatively pristine and weatherable rock fragments. Notably, silicate weathering in marine sediments is intimately tied to various other biogeochemical processes (relative to organics, phosphates, oxides, sulfides, carbonates), with potentially far-reaching consequences for nutrient and carbon cycling on local to global scales. I conclude that marine sediment weathering is most accurately thought of as a continuum of reaction balances, moderated by sediment sources (chemical reactant mixes) and by the depositional environment (Chapter 4-6). The diverse range of marine sedimentary environments produces various weathering reaction balances and fluxes that need to be considered in concert to derive global chemical fluxes (Chapter 6). Prominent ‘endmembers’ with fundamentally contrasting weathering dynamics and reaction balances and that are quantitatively significant on the global scale are (I) beaches, rocky coasts, and permeable sediment, (II) muddy river deltas, (III) continental slopes (active vs. passive margins), (IV) deep-sea clays, (V) siliceous oozes, (VI) volcanic and hydrothermal environments, and (VII) carbonate oozes. These results demonstrate how Earth’s weathering feedback may be governed by a continuum of downstream connected weathering reactions extending from the highest mountains to the deepest hadal trenches, moderated by transport and local boundary conditions (Chapter 7). Moreover, we find that deltas and beaches are weathering hotspots of the modern ocean. Clearly, the Earth’s weathering continuum is shaped by physical, chemical, and biological processes, by climatic and oceanic forces and those of the Earth’s interior. An integral understanding of these weathering continuum dynamics will progress our understanding of the behaviour of and role of humans in the Earth system, and aid targeted geo-engineering for the benefit of nature and society

    The structure of the TRAPP subunit TPC6 suggests a model for a TRAPP subcomplex

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    The TRAPP (transport protein particle) complexes are tethering complexes that have an important role at the different steps of vesicle transport. Recently, the crystal structures of the TRAPP subunits SEDL and BET3 have been determined, and we present here the 1.7 Å crystal structure of human TPC6, a third TRAPP subunit. The protein adopts an alpha/beta-plait topology and forms a dimer. In spite of low sequence similarity, the structure of TPC6 strikingly resembles that of BET3. The similarity is especially prominent at the dimerization interfaces of the proteins. This suggests heterodimerization of TPC6 and BET3, which is shown by in vitro and in vivo association studies. Together with TPC5, another TRAPP subunit, TPC6 and BET3 are supposed to constitute a family of paralogous proteins with closely similar three-dimensional structures but little sequence similarity among its members

    Strukturelle und funktionelle Untersuchungen am TRAPP-assoziierten Hefeprotein Tca17 und Organisation von humanen TRAPP-Tethering-Komplexen

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    Intracellular transport between membrane-enclosed organelles is very important for the proper functioning of all eukaryotic cells. Small molecule transport across membranes is normally mediated by transmembrane transporters or channels. As for macromolecules like proteins, the translocation through membranes can be achieved by vesicle trafficking. The objective of the first part of my PhD project was to study the structure and organization of the mammalian TRAPP (transport protein particle) complex. TRAPP is a multi-subunit protein complex involved in tethering of vesicles to the Golgi network. In yeast, at least two different types of TRAPP were identified by their different sizes in affinity purification, the small TRAPP I and the larger TRAPP II complex. In mammalian cells only one type of TRAPP was identified so far, with a subunit composition similar to yeast TRAPP II. To continue our group’s work on TRAPP I complex, I studied the less well-understood TRAPP II complex, mainly focussing on the two proteins NIBP and Ehoc-1, human orthologs of yeast Trs120p and Trs130p, respectively. A fragment of Ehoc-1 could be produced as recombinant protein in E. coli, but could not be studied further with X-ray crystallography, because suitable crystals could not be grown. Based on co-immunoprecipitation experiments on NIBP and Ehoc-1 fragments and the yeast TRAPP II model, a preliminary model for the mammalian TRAPP complex could be proposed. In this model, the central TRAPP-I like subcomplex is capped on both ends by NIBP and Ehoc-1 and forms a triangular structure. This structure may be further stabilized by interactions between conserved peptide segments from the Ehoc-1 N-terminus and the NIBP C-terminus. In the second part of this work, a formerly little known yeast TRAPP-associated protein, Tca17, was studied using biochemical and biophysical methods, as well as X-ray crystallography. Though not previously identified as a TRAPP subunit, Tca17 as well as its mammalian ortholog TRAPPC2L was proposed to be a sub- stoichiometric component of TRAPP II and promote the assembly and stability of TRAPP complexes. The crystal structure at 1.8 Å resolution shows that Tca17 adopts the longin fold characteristic for the Bet5 subfamily of small TRAPP subunits. This fold is composed of a central β-sheet formed by five antiparallel β-strands flanked by one α-helix on one side (α1) and two α-helices on the other side (α2, α3). A disulfide–linked dimer-like arrangement was observed in the crystal structure of Tca17. In order to clarify its oligomerization state in solution, several biophysical experiments were performed. It was found that a small fraction (< 5%) of Tca17 dimerizes in non-reducing buffer, whereas it stays predominantly monomeric in reducing buffer, resembling the reducing environment of the cellular cytoplasm, its natural localization in vivo. On the sequence and structure level, Tca17 is most closely related to the TRAPP subunit Trs20p/sedlin. It can bind the TRAPP subunits Bet3p and Trs33p in vitro, and might regulate the function of TRAPP by transiently integrating into TRAPP. It remains unclear how the integration of Tca17 into TRAPP might be controlled and promoted. If Tca17 were integrated into TRAPP in place of sedlin/Trs20p, the membrane association of TRAPP might be expected to be weakened, since Tca17 would introduce a negatively charged patch into the presumed membrane association interface of TRAPP.Der intrazelluläre Transport zwischen membranumschlossenen Organellen ist essentiell für die einwandfreie Funktion aller eukaryontischen Zellen. Der Transport kleiner Moleküle durch Membranen wird üblicher Weise durch transmembrane Transportproteine oder Kanäle vermittelt. Der Transport von Makromolekülen, zum Beispiel Proteinen, zwischen Membranen jedoch, wird durch den Vesikeltransport bewerkstelligt. Die Zielsetzung des ersten Teils meiner Arbeit befasste sich mit der Untersuchung der Struktur und des Aufbaus des TRAPP (transport protein particle)-Komplexes aus Säugetieren. TRAPP ist ein multimerer Anheftungskomplex, welcher die Anheftung von Vesikeln an das Golgi- Netzwerk vermittelt. In Hefe wurden mindestens zwei unterschiedliche Arten des TRAPP-Komplexes aufgrund ihrer Größe durch Affinitätsreinigung identifiziert, der kleinere TRAPP I- und der größere TRAPP II- Komplex. In Säugetierzellen wurde bisher nur eine Art des TRAPP-Komplexes identifiziert, mit einer Organisation der Untereinheiten, welche dem TRAPP II-Komplex der Hefe ähnt. Im Zuge der fortführenden Arbeiten zum TRAPP I-Komplex in unserer Arbeitsgruppe, untersuchte ich den bisher wenig charaketrisierten TRAPP II-Komplex mit Schwerpunkt bei den humanen Proteinen NIBP und Ehoc-1, den orthologen Proteinen zu Trs120p und Trs130p aus Hefe. Ein Fragment des Proteins Ehoc-1 konnte als rekombinantes Protein aus E. coli gewonnen, jedoch nicht weiter für die Röntgenstrukturanalyse verwendet werden, da keine brauchbaren Kristalle erhalten wurden. Analysen von NIBP- und Ehoc-1-Protein-Konstrukten mittels Co- Immunopräzipitation in Verbindung mit einem publizierten Modell von TRAPP II aus Hefe, erlaubten, ein vorläufiges Modell des TRAPP-Komplexes aus Säugerzellen vorzuschlagen. Dieses Modell postuliert, dass der zentrale TRAPP I-ähnliche Subkomplex durch NIBP und Ehoc-1 an seinen beiden Enden bedeckt wird und eine dreischenkelige Struktur bildet. Interaktionen zwischen konservierten Peptidbereichen nahe dem N-Terminus von Ehoc-1 und dem C-Terminus von NIBP könnten diesen Aufbau zudem stabilisieren. Der zweite Teil meiner Arbeit befasste sich mit dem bisher wenig bekannten TRAPP-assoziierten Protein Tca17. Zur Charakterisierung des Proteins wurchen biochemische und biophysikalische Methoden sowie die Röntgenstrukturanalyse herangezogen. Obwohl Tca17 nicht ursprünglich als TRAPP-Untereinheit identifiziert wurde, wurde es zusammen mit dem homologen TRAPPC2L aus Säugern als unterstöchiometrische Komponente des TRAPP II-Komplexes vorgeschlagen, welches den Aufbau und die Stabilität von TRAPP vermittelt. Die Kristallstruktur bei einer Auflösung von 1,8 Å zeigt einen Longin-Faltungstyp des Proteins Tca17, welcher charakteristisch ist für die Bet5-Unterfamilie der kleinen TRAPP- Unterein- heiten. Der Aufbau besteht aus einem fünfstängigen antiparallelen β-Faltblatt, flankiert von einer α-Helix auf einer Seite des Faltblatts (α1) und zwei weiteren α-Helices auf der anderen Seite (α2, α3). Ein durch eine Disulfidbrücke vermittelter dimer-ähnlicher Aufbau konnte für Tca17 im Kristall beobachtet werden. Um den tatsächlichen Oligomeren-Zustand des Proteins in Lösung zu untersuchen, fanden unterschiedliche biophysikalische Methoden Anwendung. Es zeigte sich, dass ein kleiner Anteil des Proteins (< 5%) Tca17 nur in nicht reduzierenden Puffersystemen dimerisiert, wobei es hauptsächlich monomer in reduzierenden Puffern auftritt, welche dem reduzierenden Medium des Zytoplasmas entspricht, der natürlichen Umgebung des Tca17 in vivo. Sowohl strukturell, als auch in seiner Sequenzähnlichkeit ist Tca17 der TRAPP-Untereinheit Trs20p/Sedlin am nächsten verwandt. Es interagiert mit den TRAPP-Untereinheiten Bet3p und Trs33p in vitro, und könnte die Funktion des TRAPP- Komplexes durch transiente Anbindung an den Komplex regulieren. Obwohl die Art der Anbindung von Tca17 und deren Regulierung an TRAPP weiterhin unklar ist, erscheint es möglich dass eine Bindung an TRAPP Auswirkungen auf die Membran-Assoziation hat. So könnte der Ausstauch von Trs20p/Sedlin durch Tca17 negativ geladene Oberflächenregionen in TRAPP einführen, welche die Membran-Assoziation schwächen

    TRAPP Complexes in Secretion and Autophagy

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    TRAPP is a highly conserved modular multi-subunit protein complex. Originally identified as a transport protein particle with a role in endoplasmic reticulum-to-Golgi transport, its multiple subunits and their conservation from yeast to humans were characterized in the late 1990s. TRAPP attracted attention when it was shown to act as a Ypt/Rab GTPase nucleotide exchanger, GEF, in the 2000s. Currently, three TRAPP complexes are known in yeast, I, II, and III, and they regulate two different intracellular trafficking pathways: secretion and autophagy. Core TRAPP contains four small subunits that self assemble to a stable complex, which has a GEF activity on Ypt1. Another small subunit, Trs20/Sedlin, is an adaptor required for the association of core TRAPP with larger subunits to form TRAPP II and TRAPP III. Whereas the molecular structure of the core TRAPP complex is resolved, the architecture of the larger TRAPP complexes, including their existence as dimers and multimers, is less clear. In addition to its Ypt/Rab GEF activity, and thereby an indirect role in vesicle tethering through Ypt/Rabs, a direct role for TRAPP as a vesicle tether has been suggested. This idea is based on TRAPP interactions with vesicle coat components. While much of the basic information about TRAPP complexes comes from yeast, mutations in TRAPP subunits were connected to human disease. In this review we will summarize new information about TRAPP complexes, highlight new insights about their function and discuss current controversies and future perspectives

    Préface de Julien Trapp

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    Préface de Julien Trapp, L’archéologie à Metz. Des antiquaires à l’archéologie préventive (1750-2008)Collection Archéologie & Culture, Presses Universitaires de Rennes, Renne

    Home of J. S. Trapp with Mrs. J. S. Trapp

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    The home J. S. Trapp is a nine-room Cape Cod country home which was remodeled from a 65-year-old farm dwelling. Mrs. J. S. Trapp is shown sitting at her desk in the den entrance just off the long screened porch. She is working on the farm business. Her desk is next to the staircase leading upstairs. Her unique desk is made of tufted designed material. The wall behind her has a floral wall paper and a picture hung on it. Mrs. Trapp is wearing a patterned, long-sleeved dress with a small necklace. She appears to be smiling slightly. Published in the Fort Worth Star-Telegram morning edition, July 6, 1941.https://mavmatrix.uta.edu/specialcollections_startelegram1940s/9092/thumbnail.jp

    Letter from M. E. Trapp to Senator Josh Lee, dated June 7, 1937

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    Letter from M. E. Trapp to Senator Josh Lee, dated June 7, 1937, defending and praising Cyrus Avery's work through the WPA.The Cyrus S. Avery Collection chronicles the life and times of Cyrus Stevens Avery. Known as the 'Father of Route 66', Avery served in government positions and elected offices as well as in highway associations that led him to have an influential impact on the planning and development of the initial American highway system. Through Avery's involvement with the City of Tulsa, Oklahoma and his own agricultural interests, the collection also documents a growing city and its' rural life in the early twentieth century

    Home of J. S. Trapp with Charles E. Trapp

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    Home of J. S. Trapp with his brother Charles E. Trapp standing in one of the living rooms. Charles helps with the farm work. He is is wearing a pair of eyeglasses and looking to his right. Charles is shown leaning against the fireplace. There are small figures on the mantle of the fireplace, including one of a swan, and a mirror that hung above it. Close to the fireplace are chairs and small tables. This home is a nine-room Cape Cod country home which J. S. Trapp remodeled from a 65-year old farm dwelling in his property, situated west of Fort Worth on Highway 80. Published in the Fort Worth Star-Telegram morning edition, July 6, 1941.https://mavmatrix.uta.edu/specialcollections_startelegram1940s/9091/thumbnail.jp
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