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Correct intron splicing generates a new type of a putative zinc‐binding domain in a transcriptional activator of Aspergillus nidulans
Author(s) -
Kulmburg Peter,
Prangé Thierry,
Mathieu Martine,
Sequeval Daria,
Scazzocchio Claudio,
Felenbok Béatrice
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80193-7
Subject(s) - aspergillus nidulans , helix turn helix , zinc finger , dna binding domain , rna splicing , intron , dna , binding domain , sequence motif , biology , binding site , alpha helix , genetics , transcription factor , biochemistry , chemistry , dna binding protein , protein structure , gene , rna , mutant
alcR is the pathway‐specific transcriptional activator of the ethanol regulon in the filamentous fungus, Aspergillus nidulans . The deduced amino acid sequence of a cDNA clone, including the 5′ part of the alcR ‐mRNA, shows that a putative Zn‐binding of the all‐cysteine class, exemplified by GAL4 is present. This structure presents some striking features. At variance with other structures of this class, the binding domain is strongly asymmetrical. Model building indicates that the zinc‐binding motif of alcR could adopt an helix‐turn‐helix structure. We propose that the DNA binding motif of alcR could participate in two types of DNA‐binding structures: the zinc‐cluster and the helix‐turn‐helix.