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Applied and Environmental Microbiology, April 2002, p. 2036-2039, Vol. 68, No. 4
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.4.2036-2039.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Fasciclin Domain Proteins Are Present in Nostoc Symbionts of Lichens

Per Paulsrud and Peter Lindblad*

Department of Physiological Botany, Evolutionary Biology Centre, Uppsala University, SE-752 36 Uppsala, Sweden

Received 15 October 2001/ Accepted 4 January 2002

Differences in the soluble protein fraction between the freshly isolated cyanobiont of lichen Peltigera membranacea, the corresponding free-living strain, and Nostoc punctiforme were analyzed. One protein, which was among the most prominent proteins of the freshly isolated cyanobiont, was expressed at a lower level in the corresponding free-living strain and was not detected at all on the two-dimensional gels of N. punctiforme. This protein was partially sequenced, and the corresponding open reading frame (ORF) in the N. punctiforme genome was identified. This ORF contains a fasciclin domain typical of a class of surface-associated proteins involved in cell adhesion. Similar fasciclin motif-containing genes have previously been shown to be symbiotically induced in other symbiotic systems.

* Corresponding author. Mailing address: Department of Physiological Botany, Evolutionary Biology Centre, Uppsala University, Villavägen 6, SE-752 36 Uppsala, Sweden. Phone and fax: 46-184712826. E-mail: peter.lindblad{at}ebc.uu.se.

Applied and Environmental Microbiology, April 2002, p. 2036-2039, Vol. 68, No. 4
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.4.2036-2039.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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  • Johnson, K. L., Jones, B. J., Bacic, A., Schultz, C. J. (2003). The Fasciclin-Like Arabinogalactan Proteins of Arabidopsis. A Multigene Family of Putative Cell Adhesion Molecules. Plant Physiol. 133: 1911-1925 [Abstract] [Full Text]  


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