Investigation of Nuclear Pore Complex Protein Interactions and the Implications for Nuclear Transport
Isgro, Timothy A.
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Permalink
https://hdl.handle.net/2142/80549
Description
Title
Investigation of Nuclear Pore Complex Protein Interactions and the Implications for Nuclear Transport
Author(s)
Isgro, Timothy A.
Issue Date
2007
Doctoral Committee Chair(s)
Schulten, Klaus
Department of Study
Physics
Discipline
Physics
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Biology, Molecular
Language
eng
Abstract
"The nucleus of the cell is of central importance to an organism, serving to store and organize genetic material, while separating and protecting this very important information from the host of other cellular components. While the nucleus requires this protective isolation, it also needs to communicate with the rest of the cell, exchanging proteins and RNA, for a variety of nuclear and cytoplasmic processes which act in concert. The nuclear pore complex is responsible for controlling the transport of large molecules into and out of the cell nucleus. It is perhaps the largest protein structure in eukaryotic cells, and because of its size, pointed experimental study has been difficult. As a result, the mechanism by which the nuclear pore complex selectively allows ""good"" material across the nuclear envelope, while preventing the transit of ""bad"", remains unknown. Here, the computer has been used to study interactions between the transport receptors that shuttle material across the nuclear pore complex and FG-nucleoporins, proteins which compose the complex itself and are of great importance in allowing protected nuclear transport. Molecular dynamics simulations have been performed on transport complexes formed by the transport receptors importin-beta, NTF2, and Cse1p. The simulations confirm nearly all interactions previously known about from experimental data, while serving, in some cases, to provide greater detail about these interactions. Furthermore, the simulations uncover a host of previously unknown interactions between each transport receptor and FG-nups. When the interactions are compared across all three transport receptors, a novel binding pattern is revealed that indicates how the nuclear pore complex may recognize the difference between the macromolecules destined to cross the nuclear envelope and the host of other proteins for which it must protect against transport."
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