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High-throughput identification of nuclear envelope protein interactions in Schizosaccharomyces pombe using an arrayed membrane yeast-two hybrid library

View ORCID ProfileJoseph M. Varberg, Jennifer M. Gardner, Scott McCroskey, Snehabala Saravanan, William D. Bradford, View ORCID ProfileSue L. Jaspersen
doi: https://doi.org/10.1101/2020.07.29.227819
Joseph M. Varberg
1Stowers Institute for Medical Research, Kansas City, MO, United States
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Jennifer M. Gardner
1Stowers Institute for Medical Research, Kansas City, MO, United States
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Scott McCroskey
1Stowers Institute for Medical Research, Kansas City, MO, United States
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Snehabala Saravanan
1Stowers Institute for Medical Research, Kansas City, MO, United States
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William D. Bradford
1Stowers Institute for Medical Research, Kansas City, MO, United States
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Sue L. Jaspersen
1Stowers Institute for Medical Research, Kansas City, MO, United States
2Department of Molecular and Integrative Physiology, University of Kansas Medical Center, Kansas City, KS, United States
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  • ORCID record for Sue L. Jaspersen
  • For correspondence: slj@stowers.org
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Abstract

The nuclear envelope (NE) contains a specialized set of integral membrane proteins that maintain nuclear shape and integrity and influence chromatin organization and gene expression. Advances in proteomics techniques and studies in model organisms have identified hundreds of proteins that localize to the NE. However, the function of many of these proteins at the NE remains unclear, in part due to a lack of understanding of the interactions that these proteins participate in at the NE membrane. To assist in the characterization of NE transmembrane protein interactions we developed an arrayed library of integral and peripheral membrane proteins in the fission yeast Schizosaccharomyces pombe for high-throughput screening using the split-ubiquitin based membrane yeast two hybrid sys-tem. We used this approach to characterize protein interactions for three conserved proteins that localize to the inner nu-clear membrane: Cut11/Ndc1, Lem2, and Ima1/Samp1/NET5. Additionally, we determined how the interaction network for Cut11 is altered in canonical temperature-sensitive cut11 mutants. This library and screening approach is readily applicable to characterizing the interactomes of integral membrane proteins localizing to various subcellular compartments.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license.
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Posted July 30, 2020.
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High-throughput identification of nuclear envelope protein interactions in Schizosaccharomyces pombe using an arrayed membrane yeast-two hybrid library
Joseph M. Varberg, Jennifer M. Gardner, Scott McCroskey, Snehabala Saravanan, William D. Bradford, Sue L. Jaspersen
bioRxiv 2020.07.29.227819; doi: https://doi.org/10.1101/2020.07.29.227819
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High-throughput identification of nuclear envelope protein interactions in Schizosaccharomyces pombe using an arrayed membrane yeast-two hybrid library
Joseph M. Varberg, Jennifer M. Gardner, Scott McCroskey, Snehabala Saravanan, William D. Bradford, Sue L. Jaspersen
bioRxiv 2020.07.29.227819; doi: https://doi.org/10.1101/2020.07.29.227819

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