Structural studies on the LINC complex and Fic-1
Name
910562619-MIT.pdf
Description
Full printable version
Size
7.27 MB
Format
Adobe PDF
Checksum (MD5)
59cd6a11f04d8803bf6bf1c9f8470489
Author(s)
Guo, Xuanzong
Advisor(s)
Thomas U. Schwartz.
Date Issued
2015
Publisher
Massachusetts Institute of Technology
Abstract
LINC complexes span the nuclear envelope and connect the nucleoskeleton to the cytoskeleton. In 2012, our lab solved the first LINC complex structure, that of SUN domain of human SUN2 bound with KASH1 or KASH2 peptides. In this project testes-specific human SUN proteins (SUN3, SPAG4, and SUNS) were compared to ubiquitously-expressed SUN2. Secondly, fission and budding yeast LINC complexes differ from human ones and were analyzed as well. I was able to confirm SUN-KASH interaction in human and yeast. For structural analysis I explored various expression strategies. Fic-1 is a C. elegans Fic-domain protein with diverse cellular functions. As a subfamily III Fic enzyme, Fic-1 may reveal valuable insights into Fic enzyme mechanisms from its structure. After trying different knowledge-informed constructs and crystal optimization, small Fic-1 crystals were obtained, which diffracted X-rays to ~ 7 [angstroms]. With modest additional effort diffraction-quality crystals should be achievable.
Description
Thesis: S.M., Massachusetts Institute of Technology, Department of Biology, 2015.
Cataloged from PDF version of thesis.
Includes bibliographical references (pages 37-38).
Subjects
Biology.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Terms of Use
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