Expression of genes encoding laccase and manganese-dependent peroxidase in the fungus Ceriporiopsis subvermispora is mediated by an ACE1-like copper-fist transcription factor
The effect of copper on the expression of genes encoding the ligninolytic enzymes laccase ( lcs) and manganese peroxidase ( mnp) in Ceriporiopsis subvermispora was evaluated. This metal increased transcript levels of lcs, mnp1 and mnp2. This finding was not unexpected in the case of lcs, since its p...
Saved in:
Published in | Fungal genetics and biology Vol. 46; no. 1; pp. 104 - 111 |
---|---|
Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
2009
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | The effect of copper on the expression of genes encoding the ligninolytic enzymes laccase (
lcs) and manganese peroxidase (
mnp) in
Ceriporiopsis subvermispora was evaluated. This metal increased transcript levels of
lcs,
mnp1 and
mnp2. This finding was not unexpected in the case of
lcs, since its promoter contains a putative ACE element. Originally characterized in the yeast
Saccharomyces cerevisiae, ACE is the target sequence of the ACE1 copper-responsive transcription factor in this microorganism. Analysis of the promoter regions of
mnp genes revealed the presence of formerly unnoticed ACE elements. Based on the
ace1 gene from
Phanerochaete chrysosporium, we isolated and characterized an ACE1-like transcription factor from
C. subvermispora (Cs-ACE1) through complementation of a
S. cerevisiae ace1Δ strain. Surprisingly, ACE1 factors from both basidiomycetes exhibit substantial differences, not only structurally but also in their ability to complement the aforementioned yeast strain. Specific binding of Cs-ACE1 to its cognate DNA sequence was confirmed by electrophoretic mobility-shift assays. |
---|---|
Bibliography: | http://dx.doi.org/10.1016/j.fgb.2008.10.002 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1087-1845 1096-0937 1096-0937 |
DOI: | 10.1016/j.fgb.2008.10.002 |