Efficient metal-specific transcription activation by Drosophila MTF-1 requires conserved cysteine residues in the carboxy-terminal domain.

ABSTRACT: MTF-1 is a sequence-specific DNA binding protein that activates the transcription of metal responsive genes. The extent of activation is dependent on the nature of the metal challenge. Here we identify separate regions within the Drosophila MTF-1 (dMTF-1) protein that are required for efficient copper- versus cadmium-induced transcription. dMTF-1 contains a number of potential metal binding regions that might allow metal discrimination including a DNA binding domain containing six zinc fingers and a highly conserved cysteine-rich C-terminus. We find that four of the zinc fingers in the DNA binding domain are essential for function but the DNA binding domain does not contribute to the metal discrimination by dMTF-1. We find that the conserved C-terminus of the cysteine-rich domain provides

SUBMITTER: Marr SK 

PROVIDER: S-EPMC3378919 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature