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Molecular and Cellular Biology, October 2002, p. 6906-6920, Vol. 22, No. 19
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.19.6906-6920.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Bni5p, a Septin-Interacting Protein, Is Required for Normal Septin Function and Cytokinesis in Saccharomyces cerevisiae

Philip R. Lee,1 Sukgil Song,1 Hyeon-Su Ro,1 Chong J. Park,1 John Lippincott,2 Rong Li,2 John R. Pringle,3 Claudio De Virgilio,3,{dagger} Mark S. Longtine,4 and Kyung S. Lee1*

Laboratory of Metabolism, Center for Cancer Research, National Cancer Institute, Bethesda, Maryland 20892,1 Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115,2 Department of Biology and Program in Molecular Biology and Biotechnology, University of North Carolina, Chapel Hill, North Carolina 27599,3 Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, Oklahoma 740784

Received 14 March 2002/ Returned for modification 23 April 2002/ Accepted 1 July 2002

In the budding yeast Saccharomyces cerevisiae, the Cdc3p, Cdc10p, Cdc11p, Cdc12p, and Sep7p/Shs1p septins assemble early in the cell cycle in a ring that marks the future cytokinetic site. The septins appear to be major structural components of a set of filaments at the mother-bud neck and function as a scaffold for recruiting proteins involved in cytokinesis and other processes. We isolated a novel gene, BNI5, as a dosage suppressor of the cdc12-6 growth defect. Overexpression of BNI5 also suppressed the growth defects of cdc10-1, cdc11-6, and sep7{Delta} strains. Loss of BNI5 resulted in a cytokinesis defect, as evidenced by the formation of connected cells with shared cytoplasms, and deletion of BNI5 in a cdc3-6, cdc10-1, cdc11-6, cdc12-6, or sep7{Delta} mutant strain resulted in enhanced defects in septin localization and cytokinesis. Bni5p localizes to the mother-bud neck in a septin-dependent manner shortly after bud emergence and disappears from the neck approximately 2 to 3 min before spindle disassembly. Two-hybrid, in vitro binding, and protein-localization studies suggest that Bni5p interacts with the N-terminal domain of Cdc11p, which also appears to be sufficient for the localization of Cdc11p, its interaction with other septins, and other critical aspects of its function. Our data suggest that the Bni5p-septin interaction is important for septin ring stability and function, which is in turn critical for normal cytokinesis.

* Corresponding author. Mailing address: Laboratory of Metabolism, Center for Cancer Research, National Cancer Institute, NIH, 9000 Rockville Pike, Bldg. 37, Rm. 3D25, Bethesda, MD 20892. Phone: (301) 496-9635. Fax: (301) 496-8419. E-mail: kyunglee{at}pop.nci.nih.gov or kslee{at}helix.nih.gov.

{dagger} Present address: Department of Medical Biochemistry, University of Geneva, Geneva, Switzerland.

Molecular and Cellular Biology, October 2002, p. 6906-6920, Vol. 22, No. 19
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.19.6906-6920.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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