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A more recent version of this article appeared on January 1, 2002
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Submitted on June 21, 2001
Revised on October 31, 2001
Accepted on October 31, 2001
1 Department of Botany, University of Georgia, Athens, Georgia
* Corresponding author. E-mail address: momany{at}botany.uga.edu.
Members of the septin family of proteins act as organizational scaffolds in areas of cell division and new growth in a variety of organisms. Here we show that in the filamentous fungus Aspergillus nidulans, the septin AspB is important for cellular division, branching, and conidiation both pre- and post-mitotically. AspB localizes postmitotically to the septation site with an underlying polarity that is evident as cytokinesis progresses. This localization at the septation site is dependent on actin and occurs before the crosswall is visible. AspB localizes premitotically as a ring at sites of branching and secondary germ tube emergence. It is the only known branch site marker. In addition, AspB is found at several stages during the development of the asexual reproductive structure, the conidiophore. It localizes transiently to the vesicle-metula and metula-phialide interfaces, and persistently to the phialide-conidiospore interface. A temperature-sensitive mutant of AspB shows phenotypic abnormalities including irregular septa, high numbers of branches, and immature asexual reproductive structures.
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