1. Conservation of the separase regulatory domain
- Author
-
Michael Melesse, Joshua N. Bembenek, and Igor B. Zhulin
- Subjects
0301 basic medicine ,Cysteine motif ,Nematoda ,Sequence analysis ,medicine.medical_treatment ,PSI-BLAST ,Immunology ,Conservation ,General Biochemistry, Genetics and Molecular Biology ,03 medical and health sciences ,0302 clinical medicine ,Functional importance ,medicine ,Animals ,Discovery Notes ,Caenorhabditis elegans ,lcsh:QH301-705.5 ,Separase ,Ecology, Evolution, Behavior and Systematics ,Genetics ,Protease ,biology ,Applied Mathematics ,Temperature ,Cell cycle ,biology.organism_classification ,030104 developmental biology ,lcsh:Biology (General) ,Modeling and Simulation ,Mutation ,Vertebrates ,General Agricultural and Biological Sciences ,Linker ,030217 neurology & neurosurgery ,Cysteine - Abstract
ᅟ We report a protein sequence analysis of the cell cycle regulatory protease, separase. The sequence and structural conservation of the C-terminal protease domain has long been recognized, whereas the N-terminal regulatory domain of separase was reported to lack detectable sequence similarity. Here we reveal significant sequence conservation of the separase regulatory domain and report a discovery of a cysteine motif (CxCxxC) conserved in major lineages of Metazoa including 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. Conservation of this motif in organisms ranging from C. elegans to humans suggests its functional importance. Reviewers This article was reviewed by Lakshminarayan Iyer and Michael Galperin. Electronic supplementary material The online version of this article (10.1186/s13062-018-0210-0) contains supplementary material, which is available to authorized users.
- Published
- 2018