Format

Send to

Choose Destination
J Cell Biol. 1996 May;133(3):605-16.

A purified Drosophila septin complex forms filaments and exhibits GTPase activity.

Author information

1
Department of Biochemistry and Biophysics, University of California at San Francisco 94143-0448, USA. cfield@socrates.ucsf.edu

Abstract

Septin proteins are necessary for cytokinesis in budding yeast and Drosophila and are thought to be the subunits of the yeast neck filaments. To test whether septins actually form filaments, an immunoaffinity approach was used to isolate a septin complex from Drosophila embryos. The purified complex is comprised of the three previously identified septin polypeptides Pnut, Sep2, and Sep1. Hydrodynamic and sequence data suggest that the complex is composed of a heterotrimer of homodimers. The complex copurifies with one molecule of bound guanine nucleotide per septin polypeptide. It binds and hydrolyzes exogenously added GTP. These observations together with conserved sequence motifs identify the septins as members of the GTPase superfamily. We discuss a model of filament structure and speculate as to how the filaments are organized within cells.

PMID:
8636235
PMCID:
PMC2120824
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center