The TBP gene from Aspergillus nidulans

Structure and expression in Saccharomyces cerevisiae

R Kucharski, E Bartnik

Research output: Contribution to journalArticle

9 Citations (Scopus)

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 ADHl 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.
Original languageEnglish
Pages (from-to)1263-1270
Number of pages8
JournalJournal of General Microbiology
Volume143
DOIs
Publication statusPublished - Apr 1997
Externally publishedYes

Cite this

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title = "The TBP gene from Aspergillus nidulans: Structure and expression in Saccharomyces cerevisiae",
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 ADHl 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.",
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year = "1997",
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The TBP gene from Aspergillus nidulans : Structure and expression in Saccharomyces cerevisiae. / Kucharski, R; Bartnik, E.

In: Journal of General Microbiology, Vol. 143, 04.1997, p. 1263-1270.

Research output: Contribution to journalArticle

TY - JOUR

T1 - The TBP gene from Aspergillus nidulans

T2 - Structure and expression in Saccharomyces cerevisiae

AU - Kucharski, R

AU - Bartnik, E

PY - 1997/4

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AB - 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 ADHl 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.

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