| Literature DB >> 21553327 |
Janaína S Freitas1, Emiliana M Silva, Juliana Leal, Diana E Gras, Nilce M Martinez-Rossi, Lucilene Delazari Dos Santos, Mario S Palma, Antonio Rossi.
Abstract
Heat shock proteins are molecular chaperones linked to a myriad of physiological functions in both prokaryotes and eukaryotes. In this study, we show that the Aspergillus nidulans hsp30 (ANID_03555.1), hsp70 (ANID_05129.1), and hsp90 (ANID_08269.1) genes are preferentially expressed in an acidic milieu, whose expression is dependent on the palA (+) background under optimal temperature for fungal growth. Heat shock induction of these three hsp genes showed different patterns in response to extracellular pH changes in the palA(+) background. However, their accumulation upon heating for 2 h was almost unaffected by ambient pH changes in the palA (-) background. The PalA protein is a member of a conserved signaling cascade that is involved in the pH-mediated regulation of gene expression. Moreover, we identified several genes whose expression at pH 5.0 is also dependent on the palA (+) background. These results reveal novel aspects of the heat- and pH-sensing networks of A. nidulans.Entities:
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Year: 2011 PMID: 21553327 PMCID: PMC3156257 DOI: 10.1007/s12192-011-0267-5
Source DB: PubMed Journal: Cell Stress Chaperones ISSN: 1355-8145 Impact factor: 3.667