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MBC in Press, published online ahead of print November 5, 2008
Mol. Biol. Cell 10.1091/mbc.E08-07-0754

A more recent version of this article appeared on January 1, 2009
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Submitted on July 23, 2008
Revised on September 22, 2008
Accepted on October 29, 2008

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

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, while 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.

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






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