TY - JOUR
T1 - Characterization of the conserved phosphorylation site in the Aspergillus nidulans response regulator SrrA
AU - Hagiwara, Daisuke
AU - Mizuno, Takeshi
AU - Abe, Keietsu
N1 - Funding Information:
Acknowledgments D. Hagiwara was supported by a research fellowship from the Japan Society for the Promotion of Science. K. Abe was supported in part by grants from the Bio-oriented Technology Research Advancement Institution (BRAIN).
Copyright:
Copyright 2019 Elsevier B.V., All rights reserved.
PY - 2011/4
Y1 - 2011/4
N2 - Ssk1- and Skn7-type response regulators are widely conserved in fungal His-Asp phosphorelay (two-component) signaling systems. SrrA, a Skn7-type RR of Aspergillus nidulans, is implicated not only in oxidative stress responses but also in osmotic adaptation, conidia production (asexual development), inhibition by fungicides, and cell wall stress resistance. Here, we characterized SrrA, focusing on the role of the conserved aspartate residue in the receiver domain, which is essential for phosphorelay function. We constructed strains carrying an SrrA protein in which aspartate residue D385 was replaced with either asparagine (N) or alanine (A). These mutants exhibited normal conidiation and partial oxidative stress resistance. In osmotic adaptation, mutants with substitution at SrrA D385 showed as much sensitivity as ΔsrrA strains, suggesting that SrrA plays a role in osmotic stress adaptation in a phosphorelay-dependent manner. The SrrA D385 substitution mutants showed significant resistance to fungicides and cell wall stresses. These results together led us to conclude that the conserved aspartate residue has a substantial impact on SrrA function, and that SrrA plays a role in several aspects of cellular function via His-Asp phosphorelay circuitry in Aspergillus nidulans.
AB - Ssk1- and Skn7-type response regulators are widely conserved in fungal His-Asp phosphorelay (two-component) signaling systems. SrrA, a Skn7-type RR of Aspergillus nidulans, is implicated not only in oxidative stress responses but also in osmotic adaptation, conidia production (asexual development), inhibition by fungicides, and cell wall stress resistance. Here, we characterized SrrA, focusing on the role of the conserved aspartate residue in the receiver domain, which is essential for phosphorelay function. We constructed strains carrying an SrrA protein in which aspartate residue D385 was replaced with either asparagine (N) or alanine (A). These mutants exhibited normal conidiation and partial oxidative stress resistance. In osmotic adaptation, mutants with substitution at SrrA D385 showed as much sensitivity as ΔsrrA strains, suggesting that SrrA plays a role in osmotic stress adaptation in a phosphorelay-dependent manner. The SrrA D385 substitution mutants showed significant resistance to fungicides and cell wall stresses. These results together led us to conclude that the conserved aspartate residue has a substantial impact on SrrA function, and that SrrA plays a role in several aspects of cellular function via His-Asp phosphorelay circuitry in Aspergillus nidulans.
KW - Cell wall stress
KW - Fungicide resistance
KW - His-Asp phosphorelay
KW - Oxidative stress response
KW - Response regulator
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U2 - 10.1007/s00294-010-0330-2
DO - 10.1007/s00294-010-0330-2
M3 - Article
C2 - 21229249
AN - SCOPUS:79954442820
VL - 57
SP - 103
EP - 114
JO - Current Genetics
JF - Current Genetics
SN - 0172-8083
IS - 2
ER -