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Department of Genetics, University of Warsaw Pawi
skiego 5a, 02-106 Warsaw, Poland
Institute of Biochemistry and Biophysics, Polish Academy of Sciences Pawi
skiego 5a, 02-106 Warsaw, Poland
Author for correspondence: Ewa Bartnik. Tel: +48 22 6597072 ext. 2247. Fax: +48 22 6584754. e-mail: ebartnik@:ibbrain.ibb.waw.pl
ABSTRACT
The genomic and cDNA copy of the TATA-binding protein (TBP) gene from the filamentous fungus Aspergillus nidulans have been cloned. The gene is interrupted by four introns, one of which is in the long 5' untranslated region of 615 bp. The transcription initiation site was established and the levels of mRNA were analysed under diverse growth conditions and found to vary severalfold. The gene encodes a protein of 268 amino acids composed of an N-terminal domain of 88 amino acids with no significant homology to other TBPs and a C-terminal domain of 180 amino acids with about 95% homology to other fungal TBPs. A cDNA clone under the yeast ADH1 promoter was able to substitute for the yeast TBP gene in vivo; however, the transformants obtained grew poorly at 35°C and on galactose and glycerol at 30°C, though they could grow in the presence of copper ions or aminotriazole at this temperature. This phenotype may be the result of altered function of A. nidulans TBP in certain yeast transcription activation pathways.
Present address: Visual Sciences, RSBS, The Australian National University, Canberra ACT 0200, Australia.
This article has been cited by other articles:
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P. Leng, P. E. Carter, and A. J. P. Brown The TATA-Binding Protein (TBP) from the Human Fungal Pathogen Candida albicans Can Complement Defects in Human and Yeast TBPs J. Bacteriol., April 1, 1998; 180(7): 1771 - 1776. [Abstract] [Full Text] |
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