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Full-Text Articles in Life Sciences
Biochemical And Structural Analysis Of The Nucleoporin Nup214 And Its Involvement In Mrna Export, Johanna Napetschnig
Biochemical And Structural Analysis Of The Nucleoporin Nup214 And Its Involvement In Mrna Export, Johanna Napetschnig
Student Theses and Dissertations
In order to gain a deeper understanding of the role of nups in leukemogenesis, and to make sense of the architecture and regulation of the mRNA export machinery at the NPC, I set out to biochemically and structurally characterize Nup214. In this thesis, I present the crystal structure of the human Nup214 N-terminal domain at 1.65 Ã… resolution. The structure reveals a sevenbladed !-propeller fold followed by a 30-residue C-terminal extended peptide segment (CTE). The CTE folds back onto the !-propeller and binds to its bottom face. Conserved surface patches on the Nup214 NTD reveal putative proteininteraction sites, one of …
Biophysical Characterization Of Structure And Dynamics Of Nuclear Pore Complex Components, Martin Kampmann
Biophysical Characterization Of Structure And Dynamics Of Nuclear Pore Complex Components, Martin Kampmann
Student Theses and Dissertations
The Nuclear Pore Complex (NPC) mediates nucleo-cytoplasmic transport in all eukaryotes and is among the largest cellular assemblies of proteins, called nucleoporins (nups). The details of NPC architecture, dynamics, and mechanism are still unknown. NPCs can be dissected biochemically into distinct subcomplexes. One of the best-characterized subcomplexes, the Nup84 complex, consists of seven nups and was proposed to form a membrane-coating module of the NPC. I optimized the isolation of the heptameric complex from budding yeast and analyzed its structure by negative-stain electron microscopy (EM). My data confirm the previously reported flexible Y-shape. I solved the three-dimensional structures of two …
Architecture Of A Coat For The Nuclear Pore Membrane, Kuo-Chiang Hsia
Architecture Of A Coat For The Nuclear Pore Membrane, Kuo-Chiang Hsia
Student Theses and Dissertations
Nuclear pore complexes (NPCs) reside in the nuclear membrane and mediate macromolecules exchange between the nucleus and cytoplasm. Although the protein components of NPCs, termed collectively nucleoporin, have been identified, how nucleoporins arrange in NPC, however, is still an enigma. NPC is a highly symmetric protein complex, which contains an eight-fold rotational symmetry across the center of the pore and a two-fold symmetry in the plane of the nuclear envelope. In addition, according to electron microscopic reconstruction model, NPC can also be considered schematically as a series of concentric cylinders. A peripheral cylinder coating the nuclear pore membrane contains a …
Proteomic, Bioinformatic And Functional Characterization Of The Nuclear Pore Complex Of The African Trypanosome, Jeffrey Allen Degrasse
Proteomic, Bioinformatic And Functional Characterization Of The Nuclear Pore Complex Of The African Trypanosome, Jeffrey Allen Degrasse
Student Theses and Dissertations
The eukaryotic genome, and its associated proteins, is intricately packaged and sequestered within the boundary of a double membrane, known as the nuclear envelope (NE). Transport across the NE is mediated by large protein assemblages known as nuclear pore complexes (NPCs). Yeast and vertebrate NPCs are comprised of about 30 proteins, termed nucleoporins (Nups), which are present in multiple copies. The origins and evolution of the nucleus and NPC are not yet clear, although it seems likely that the nucleus arose only once in eukaryotic evolution. To further our understanding of the evolution of the NPC, we characterized the NPC …
Myosin-Like Proteins In S. Cerevisiae: Multifunctional, Structural Components Of The Nuclear Envelope, Mario Niepel
Myosin-Like Proteins In S. Cerevisiae: Multifunctional, Structural Components Of The Nuclear Envelope, Mario Niepel
Student Theses and Dissertations
The nuclear envelope (NE) separates the genetic material from the rest of the cell, delimits and defines the nucleus, organizes the intranuclear architecture and serves as a regulator for multiple nuclear processes. In all eukaryotes, filamentous coiled-coil proteins are associated with the intranuclear surface of the NE and are integral to proper nuclear function. One such protein, called Tpr in vertebrates, attaches to the NPC and appears to form the nuclear basket structure, is conserved throughout all eukaryotes. The two yeast homologs of Tpr are termed Mlp1p and Mlp2p. The Mlp proteins also attach to the nuclear face of the …