De anno Hebraeorum Jubilaeo : commentatio in certamine literario civium Academiae Georgiae Augustae die IV. Junii MDCCCXXXVII : ex decreto Venerabilis Theologorum Ordinis praemio regio ornata

scripsit Georgius Woldius

El café, o la comedia nueva : comedia en 2 actos, en prosa

por Leandro Fernandez de Moratin

Jüdische Merckwürdigkeiten : vorstellende was sich Curieuses und Denckwürdiges in den neuern Zeiten bey einigen Jahrhunderten mit denen in alle IV Teile der Welt, sonderlich durch Teutschland, zerstreuten Juden zugetragen. Sammt einer vollständigen Franckfurter Juden-Chronik, ...

mit historischer Feder in drey Theilen beschrieben von Johann Jacob Schudt

Ms. lat. oct. 156 - In Thomae de Aquino Summam theologiae, P. III.

Vorbesitzer: Bernhard Diell;

Analysis of Agrobacterium tumefaciens VirB6 and VirB9 of the VirB /D4 type IV secretion system

Agrobacterium tumefaciens uses the VirB/D4 type IV secretion system (T4SS) to translocate oncogenic DNA (T-DNA) and protein substrates to plant cells. Independent of VirD4, the eleven VirB proteins are also essential for elaboration of a conjugative pilus termed the T pilus. The focus of this thesis is the characterization and analysis of two VirB proteins, VirB6 and VirB9, with respect to substrate translocation and T pilus biogenesis. Observed stabilizing effects of VirB6 on other VirB subunits and results of protein-protein interaction studies suggest that VirB6 mediates assembly of the secretion machine and T pilus through interactions with VirB7 and VirB9. Topology studies support a model for VirB6 as a polytopic membrane protein with a periplasmic N terminus, a large internal periplasmic loop, five transmembrane segments, and a cytoplasmic C terminus. Topology studies and Transfer DNA immunoprecipitation (TrIP) assays identified several important VirB6 functional domains: (i) the large internal periplasmic loop mediates interaction of VirB6 with the T-DNA, (ii) the membrane spanning region carboxyl-terminal to the large periplasmic loop mediates substrate transfer from VirB6 to VirB8, and (iii) the terminal regions of VirB6 are required for substrate transfer to VirB2 and VirB9. To analyze structure-function relationships of VirB9, the phenotypic consequences of dipeptide insertion mutations were characterized. Substrate discriminating mutations were shown to selectively export the oncogenic T-DNA and VirE2 to plant cells or a mobilizable IncQ plasmid to bacterial cells. Mutations affecting VirB9 interactions with VirB7 and VirB10 were localized to the C- and N- terminal regions respectively. Additionally, “uncoupling” mutations identified in VirB11 and VirB6 that block T pilus assembly, but not substrate transfer to recipient cells, were also identified in VirB9. These results in conjunction with computer analysis establish that VirB9, like VirB6, is also composed of distinct regions or domains that contribute in various ways to secretion channel activity and T pilus assembly. Lastly, in vivo immunofluorescent studies suggest that VirB9 localizes to the outer membrane and may play a role similar to that of secretion/ushers of types II and III secretion systems to facilitate substrate translocation across this final bacterial barrier. ^

IV Congresso Nacional de Estudos Clássicos. XII Reuniâo da SBEC "Antigüidades"

Fil: Errecalde, Alejandro Martín. Universidad Nacional de La Plata. Facultad de Humanidades y Ciencias de la Educación; Argentina.

III Congresso Nacional de Estudos Classicos ; IX Reuniao da Sociedade Brasileira de Estudos Classicos

Fil: Nápoli, Juan Tobías. Universidad Nacional de La Plata. Facultad de Humanidades y Ciencias de la Educación; Argentina.

IV Congresso Nacional de Estudos Clássicos. XII Reuniâo da SBEC "Antigüidades"

Fil: Errecalde, Alejandro Martín. Universidad Nacional de La Plata. Facultad de Humanidades y Ciencias de la Educación; Argentina.

III Congresso Nacional de Estudos Classicos ; IX Reuniao da Sociedade Brasileira de Estudos Classicos

Fil: Nápoli, Juan Tobías. Universidad Nacional de La Plata. Facultad de Humanidades y Ciencias de la Educación; Argentina.