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Originally published as MBC in Press, 10.1091/mbc.E08-07-0754 on November 5, 2008

Vol. 20, Issue 1, 270-281, January 1, 2009

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Drosophila Orc6 Facilitates GTPase Activity and Filament Formation of the Septin Complex

Richard P.H. Huijbregts, Anton Svitin, Monica W. Stinnett, Matthew B. Renfrow, and Igor Chesnokov

Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, School of Medicine, Birmingham, AL 35294

Submitted July 23, 2008; Revised September 22, 2008; Accepted October 29, 2008
Monitoring Editor: Thomas F.J. Martin

The origin recognition complex or ORC is a six-subunit protein important for DNA replication and other cell functions. Orc6, the smallest subunit of ORC, is essential for both replication and cytokinesis in Drosophila, and interacts with the septin protein Pnut, which is part of the Drosophila septin complex. In this study, we describe the analysis of the interaction of Orc6 with Pnut and whole Drosophila septin complex. Septin complex was purified from Drosophila embryos and also reconstituted from recombinant proteins. The interaction of Orc6 with the septin complex is dependent on the coiled-coil domain of Pnut. Furthermore, the binding of Orc6 to Pnut increases the intrinsic GTPase activity of the Drosophila septin complex, whereas in the absence of GTP it enhances septin complex filament formation. These results suggest an active role for Orc6 in septin complex function. Orc6 might be a part of a control mechanism directing the cytokinesis machinery during the final steps of mitosis.

This was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E08-07-0754) on November 5, 2008.

Address correspondence to: Igor Chesnokov (ichesnokov{at}uab.edu).




This article has been cited by other articles:


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 Proc. Natl. Acad. Sci. USAHome page
M. Balasov, R. P. H. Huijbregts, and I. Chesnokov
Functional analysis of an Orc6 mutant in Drosophila
PNAS, June 30, 2009; 106(26): 10672 - 10677.
[Abstract] [Full Text] [PDF]


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