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Biophys. J. BioFAST: First Published July 22, 2005. doi:10.1529/biophysj.105.063511
© 2005 by the Biophysical Society.

A more recent version of this article appeared on October 1, 2005.
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Victor M. Bolanos-Garcia
Sylvie Beaufils
Anne Renault
Gunter Grossman
Suzanne Brewerton
Miyoung Lee
Ashok Venkitaraman
Tom L. Blundell
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PROTEINS

The conserved N-terminal region of the mitotic checkpoint protein BUBR1: a putative TPR motif of high surface activity

Victor M. Bolanos-Garcia 1*, Sylvie Beaufils 2, Anne Renault 2, Gunter Grossman 3, Suzanne Brewerton 4, Miyoung Lee 5, Ashok Venkitaraman 5 and Tom L. Blundell 6

1 University of Cambridge
2 Universite de Rennes
3 Synchrotron Radiation Department, CCLRC Daresbury Laboratory, Warrington, UK
4 Astex Technology
5 The Hutchison/MRC Research Centre. Cambridge, UK
6 Department of Biochemistry, University of Cambridge

* To whom correspondence should be addressed. E-mail: victor{at}cryst.bioc.cam.ac.uk.

Submitted on March 25, 2005
Revised on May 17, 2005
Accepted on 22 June 2005


  Abstract
BUBR1, a key component of the mitotic spindle checkpoint, is a multidomain protein kinase that is activated in response to kinetochore tension. Although BUB1 and BUBR1 play an important role in cell division, very little is known about their structural characteristics. We show that the conserved N-terminal region of BUBR1, comprising residues 1-204, is a globular domain of high a-helical content (» 60%), stable in the pH range 4-9 and probably organised as a tetratricopeptide motif repeat (TPR), most closely resembling residues 16-181 of protein phosphatase 5. Because the latter presents a continuous amphipathic groove and is regulated by binding certain fatty acids, we compared the properties of BUBR1(1-204) and TPR-PP5(16-181) at air/water interfaces and found that both proteins exhibited a similar surface-activity and formed stable, rigid monolayers. The deletion of a region that probably comprises several a-helices of BUBR1 indicates that long-range interactions are essential for the stability of the N-terminal domain. The presence of the putative TPR motif strongly suggests that the N-terminal domain of BUBR1 is involved in direct protein-protein interactions and/or protein-lipid interactions.

Key Words: BUB protein family, mitotic control, mitotic spindle checkpoint, protein monolayers, putative TPR motif, surface rheology




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Copyright © 2005 by the Biophysical Society.