Correct intron splicing generates a new type of a putative zinc‐binding domain in a transcriptional activator of Aspergillus nidulans

FEBS Letters

Sequeval, Daria²  Mathieu, Martine²  Felenbok, Béatrice²  Kulmburg, Peter²  Scazzocchio, Claudio²  Prangé, Thierry¹ 

[1] Laboratoire pour l'Utilisation du Rayonnement Electromagnètique, Bâtiment 209D, Centre Universitaire Paris-Sud, 91405 Orsay Cedex, France;Institut de Génétique et Microbiologie, Bâtiment 409, Centre Universitaire Paris-Sud, 91405 Orsay Cedex, France

关键词: Zn-binding domain;    Ethanol regulon;    Model building;    Aspergillus nidulans;   

DOI  :  10.1016/0014-5793(91)80193-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown