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J. Biol. Chem., Vol. 277, Issue 17, 14688-14694, April 26, 2002

This Article Full Text Full Text (PDF) All Versions of this Article: 277/17/14688    most recent M200744200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Cziferszky, A. Articles by Kubicek, C. P. Search for Related Content PubMed PubMed Citation Articles by Cziferszky, A. Articles by Kubicek, C. P. Social Bookmarking                      What's this?

Phosphorylation Positively Regulates DNA Binding of the Carbon Catabolite Repressor Cre1 of Hypocrea jecorina (Trichoderma reesei)^*

Angela Cziferszky, Robert L. Mach^§, and Christian P. Kubicek

From the Section for Microbial Biochemistry and Gene Technology, Institute of Chemical Engineering, Technical University of Vienna, Getreidemarkt 9-166, A-1060 Vienna, Austria

Cre1 of the ascomycete Hypocrea jecorina is a Cys₂His₂ zinc finger DNA-binding protein functioning as regulator for carbon catabolite repression. It represents the functional equivalent of yeast Mig1, known to be negatively regulated by the Snf1-kinase at the nuclear import level. We demonstrate that Cre1 is also a phosphoprotein, and identify Ser²⁴¹ within an acidic protein region as phosphorylation target. In contrast to Mig1 phosphorylation is required for DNA binding of Cre1. A S241E mutation mimics phosphorylation, whereas a S241A mutant protein shows phosphorylation-independent DNA binding activity, suggesting that phosphorylation is required to release Cre1 from an inactive conformation involving unphosphorylated Ser²⁴¹. Retransformation of a H. jecorina cre1-non functional mutant with Cre1-S241A leads to permanent carbon catabolite repression in cellobiohydrolase I expression. Contrary to Mig1, the amino acid sequence surrounding Ser²⁴¹ (HSNDEDD) suggests that phosphorylation may occur by a casein kinase II-like protein. This is supported by a mutation of E244V leading to loss of phosphorylation, loss of DNA binding, and gain of carbon catabolite derepression. Our results imply that the regulation of carbon catabolite repression at the level of DNA binding strongly differs between Saccharomyces cerevisiae and H. jecorina.

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