Abstract
After the degradation of its inhibitor securin, separase initiates chromosome segregation during the metaphase-to-anaphase transition by cleaving cohesin. Here we present a density map at a resolution of 25 A of negatively stained separase-securin complex. Based on labeling data and sequence analysis, we propose a model for the structure of separase, consisting of 26 ARM repeats, an unstructured region of 280 residues and two caspase-like domains, with securin binding to the ARM repeats.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Cell Cycle Proteins / chemistry*
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Cell Cycle Proteins / metabolism*
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Cell Cycle Proteins / ultrastructure
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Endopeptidases / chemistry*
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Endopeptidases / metabolism*
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Endopeptidases / ultrastructure
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Humans
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Microscopy, Electron
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Models, Molecular
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Neoplasm Proteins / chemistry*
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Neoplasm Proteins / metabolism*
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Neoplasm Proteins / ultrastructure
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Protein Conformation
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Protein Folding
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Securin
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Separase
Substances
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Cell Cycle Proteins
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Neoplasm Proteins
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Securin
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pituitary tumor-transforming protein 1, human
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Endopeptidases
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ESPL1 protein, human
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Separase