Τίτλος:
Genetic and cellular characterization of MscS-like putative channels in the filamentous fungus Aspergillus nidulans
Γλώσσες Τεκμηρίου:
Αγγλικά
Περίληψη:
Mechanosensitive ion channels are integral membrane proteins ubiquitously present in bacteria, archaea, and eukarya. They act as molecular sensors of mechanical stress to serve vital functions such as touch, hearing, osmotic pressure, proprioception and balance, while their malfunction is often associated with pathologies. Amongst them, the structurally distinct MscL and MscS channels from bacteria are the most extensively studied. MscS-like channels have been found in plants and Schizosaccharomyces pombe, where they regulate intracellular Ca2+ and cell volume under hypo-osmotic conditions. Here we characterize two MscS-like putative channels, named MscA and MscB, from the model filamentous fungus Aspergillus nidulans. Orthologues of MscA and MscB are present in most fungi, including relative plant and animal pathogens. MscA/MscB and other fungal MscS-like proteins share the three transmembrane helices and the extended C-terminal cytosolic domain that form the structural fingerprint of MscS-like channels with at least three additional transmembrane segments than Escherichia coli MscS. We show that MscA and MscB localize in Endoplasmic Reticulum and the Plasma Membrane, respectively, whereas their overexpression leads to increased CaCl2 toxicity or/and reduction of asexual spore formation. Our findings contribute to understanding the role of MscS-like channels in filamentous fungi and relative pathogens. © 2022 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group.
Συγγραφείς:
Dionysopoulou, M.
Yan, N.
Wang, B.
Pliotas, C.
Diallinas, G.
Εκδότης:
Taylor and Francis Ltd.
Λέξεις-κλειδιά:
calcium chloride; flyc1 channel protein; fungal protein; genomic DNA; green fluorescent protein; ion channel; membrane protein; msca channel protein; mscb channel protein; mscm channel protein; mscs channel protein; mscs like channel protein; msl1 channel protein; msl10 channel protein; msl2 channel protein; msl9 channel protein; msy1 channel protein; msy2 channel protein; sodium chloride; unclassified drug; Escherichia coli protein; ion channel; MscL protein, E coli; MscS protein, E coli, alpha fold modeling; amino terminal sequence; Article; asexual spore; Aspergillus nidulans; carboxy terminal sequence; cell membrane; cellular characterization; computer model; controlled study; DNA extraction; endoplasmic reticulum; epifluorescence microscopy; Escherichia coli; fungus growth; gene overexpression; genetic characterization; growth rate; investigative procedures; multiple sequence alignment; nonhuman; phenotype; phylogeny; polymerase chain reaction; sequence alignment; subcellular localization; bacterium; genetics; mechanotransduction; metabolism; osmotic pressure; physiology, Aspergillus nidulans; Bacteria; Escherichia coli; Escherichia coli Proteins; Ion Channels; Mechanotransduction, Cellular; Osmotic Pressure
DOI:
10.1080/19336950.2022.2098661
