2026-09-19T16:18:55Zhttps://dspace.mit.edu/server/oai/requestoai:dspace.mit.edu:1721.1/973492022-01-13T07:53:55Zcom_1721.1_7582com_1721.1_7581col_1721.1_131023
Thomas U. Schwartz.
Guo, Xuanzong
Massachusetts Institute of Technology. Department of Biology.
Massachusetts Institute of Technology. Department of Biology
2015-06-10T19:12:27Z
2015-06-10T19:12:27Z
2015
2015
http://hdl.handle.net/1721.1/97349
910562619
Thesis: S.M., Massachusetts Institute of Technology, Department of Biology, 2015.
Cataloged from PDF version of thesis.
Includes bibliographical references (pages 37-38).
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.
by Xuanzong Guo.
S.M.
38 pages
eng
Massachusetts Institute of Technology
M.I.T. theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission.
http://dspace.mit.edu/handle/1721.1/7582
Biology.
Structural studies on the LINC complex and Fic-1
Thesis
application/pdf
Publication
unknown
unknown
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<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.</Abstract>
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