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RESEARCH PAPER

Zipper-like interaction between proteins in adjacent daughter cells mediates protein localization

¹ Division of Biological Sciences, University of California San Diego, La Jolla, California 92093-0377, USA; ² Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, Georgia 30322, USA

Protein localization is crucial for cellular morphogenesis and intracellular signal transduction cascades. Here we describe an interaction between two membrane proteins expressed in different cells of the Bacillus subtilis sporangium, the mother cell protein SpoIIIAH and the forespore protein SpoIIQ. We used affinity chromatography, coimmunoprecipitation, and the yeast two-hybrid system to demonstrate that the extracellular domains of these proteins interact, tethering SpoIIIAH to the sporulation septum, and directing its assembly with SpoIIQ into helical arcs and foci around the forespore. We also demonstrate that this interaction can direct proteins made in the same cell to active division sites, as when SpoIIQ is made in the mother cell, it localizes to nascent septa in a SpoIIIAH-dependent manner. Both SpoIIIAH and SpoIIQ are necessary for activation of the second forespore-specific transcription factor (^G) after engulfment, and we propose that the SpoIIIAH-SpoIIQ complex contributes to a morphological checkpoint coupling ^G activation to engulfment. In keeping with this hypothesis, SpoIIIAH localization depends on the first step of engulfment, septal thinning. The SpoIIQ-SpoIIIAH complex reaches from the mother cell cytoplasm to the forespore cytoplasm and is ideally positioned to govern the activity of engulfment-dependent transcription factors.

[Keywords: Sporulation; protein localization; signal transduction; bacterial development]

Received August 20, 2004; revised version accepted October 4, 2004.

Article and publication are at http://www.genesdev.org/cgi/doi/10.1101/gad.1252704.

³ These authors contributed equally to this work.

⁴ Corresponding author.
E-MAIL kpogliano{at}ucsd.edu; FAX (858) 822-1431.

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