This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The nucleus is delimited by the double-membraned nuclear envelope (NE), which provides structure to the nucleus, forms a barrier separating the nucleoplasm from the surrounding cytoplasm, and serves as an anchor for many essential nuclear processes. The sole mediators of exchange across the NE are termed nuclear pore complexes (NPCs), which span pores in the NE to connect the nuclear and cytoplasmic compartments. Proteins attached to the nuclear end of the NPC and the nucleoplasmic face of the NE could potentially function in any of the structural, trafficking and anchoring roles of the NE. The only protein with such a position and common among eukaryotes is Tpr, whose Saccharomyces (yeast) homologues are termed Mlp1p and Mlp2p. Studies have suggested pivotal roles for the Tpr family in the control of nucleocytoplasmic trafficking, in chromatin silencing, and in spindle morphogenesis, but almost nothing is known about the actual functions of these proteins.
Specific Aim of Collaboration with NCMI: (i) to image the entire intact purified yeast nucleus at an unprecedentedly high resolution, to gain a better structural understanding of the NPC, the nuclear envelope, and the organization of the nuclear periphery (including particularly the role of the Mlps and NPCs in this organization), and (ii) to determine the structure of the Mlp proteins and the higher order complexes they form.
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| Baranovskiy, Andrey G; Zhang, Yinbo; Suwa, Yoshiaki et al. (2015) Crystal structure of the human primase. J Biol Chem 290:5635-46 |
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