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Conservation of separase N-terminal domain

Michael Melesse, Joshua N. Bembenek, Igor B. Zhulin
doi: https://doi.org/10.1101/236216
Michael Melesse
1Department of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, TN
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Joshua N. Bembenek
1Department of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, TN
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Igor B. Zhulin
2Department of Microbiology, University of Tennessee, Knoxville, Tennessee, USA
3Computational Sciences and Engineering Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee, USA
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Abstract

We report a reanalysis of the sequence conservation of the cell cycle regulatory protease, separase. The sequence and structural conservation of the protease domain has long been recognized. Here we reexamine the protein sequence conservation at the N-terminus using PSI-BLAST analysis and report our discovery of a cysteine rich motif (CxCXXC) conserved in nematodes and vertebrates. This motif is found in a solvent exposed linker region connecting two TPR-like helical motifs. Mutation of this motif in Caenorhabditis elegans separase leads to a temperature sensitive hypomorphic protein, and several N-terminal residues identified as intragenic suppressors are not conserved. Conservation of this motif in multiple organisms raises the possibility that the motif plays similar roles across species.

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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-NC-ND 4.0 International license.
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Posted December 19, 2017.
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Conservation of separase N-terminal domain
Michael Melesse, Joshua N. Bembenek, Igor B. Zhulin
bioRxiv 236216; doi: https://doi.org/10.1101/236216
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Conservation of separase N-terminal domain
Michael Melesse, Joshua N. Bembenek, Igor B. Zhulin
bioRxiv 236216; doi: https://doi.org/10.1101/236216

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