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Isolation and characterization of a calmodulin-encoding cDNA from the pathogenic fungus Histoplasma capsulatum

We describe in this paper the isolation and complete sequence of a calmodulin (CaM) encoding cDNA from the dimorphic pathogenic fungus Histoplasma capsulatum (GenBank accession U12505). The deduced amino acid sequence was identical to the CaM of Aspergillus nidulans and had only one amino acid diffe...

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Bibliographic Details
Published in:Journal of medical and veterinary mycology 1996, Vol.34 (3), p.163-169
Main Authors: El-Rady, J., Shearer, G.
Format: Article
Language:English
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Summary:We describe in this paper the isolation and complete sequence of a calmodulin (CaM) encoding cDNA from the dimorphic pathogenic fungus Histoplasma capsulatum (GenBank accession U12505). The deduced amino acid sequence was identical to the CaM of Aspergillus nidulans and had only one amino acid difference from the CaM of Neurospora crassa. Saccharomyces cerevisiae CaM, however, has only about 60% amino acid identity compared with H. capsulatum. These data further support the close relationship of Histoplasma to the filamentous ascomycetes. Histoplasma CaM was expressed as a single major transcript of approximately 1200 nt. in both the yeast and mould growth forms. CaM mRNA levels were approximately two-fold greater in the yeast than in the mould form of the organism. Southern blot analysis indicated that the H. capsulatum CaM gene is present in a single copy.
ISSN:1369-3786
0268-1218
1460-2709
DOI:10.1080/02681219680000271