A new Mad2-interacting domain of Cdc20 is critical for the function of Mad2–Cdc20 complex in the spindle assembly checkpoint

Mondal, Gourish and Baral, Rathindra N and Roychoudhury, Susanta (2006) A new Mad2-interacting domain of Cdc20 is critical for the function of Mad2–Cdc20 complex in the spindle assembly checkpoint. Biochem. Journal, 396. pp. 243-253.

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    Abstract

    Interaction between Mad2 and Cdc20 (cell division cycle 20) is a key event during spindle assembly checkpoint activation. In the past, an N-terminal peptide containing amino acid residues 111–150 of Cdc20 was shown to bind Mad2 much better than the full-length Cdc20 protein. Using co-localization, co-immunoprecipitation and peptide inhibition analysis with different deletion mutants of Cdc20, we identified another Mad2-binding domain on Cdc20 from amino acids 342–355 within the WD repeat region. An intervening region between these two domains interferes with its Mad2 binding when present individually with any of these two Mad2-binding sites. We suggest that these three domains together determine the overall strength of Mad2 binding with Cdc20. Functional analysis suggests that an optimum Mad2 binding efficiency of Cdc20 is required during checkpoint arrest and release. Further, we have identified a unique polyhistidine motif with metal binding property adjacent to this second binding domain that may be important for maintaining the overall conformation of Cdc20 for its binding to Mad2. Key words: cell division cycle 20 (Cdc20) domain, Mad2–Cdc20 interaction, nocodazole, polyhistidine motif, spindle assembly checkpoint, WD repeat.

    Item Type: Article
    URI: http://www.eprints.iicb.res.in/id/eprint/418
    Subjects: Molecular & Human Genetics
    Divisions: Indian Institute of Chemical Biology
    Depositing User: Mr Shyamal Nath
    Date Deposited: 01 Nov 2011 17:37
    Last Modified: 03 Feb 2012 12:30
    Official URL: htpp://dx.doi.org/10.1042/BJ20051914
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