A transient receptor potential-like calcium ion channel in the filamentous fungus Aspergillus nidulans

Author:

Hognchen Wang, Qiuyi Chen, Shizhu Zhang

Author address:

University of Nanjing normal, Institute of life sciences, Nanjing, China

Full conference title:

15th European Conference on Fungal Genetics 2020

Date: 20 June 2020

Abstract:

The Transient Receptor Potential (TRP) proteins constitute a superfamily which encodes transmembrane ion channels with very diverse permeation and gating properties. In mammals, this ion channel is best known as a sensor for environmental irritants giving rise to somatosensory modalities, such as pain, cold and itch, and other protective responses. According to bioinformatics analysis, filamentous fungi have putative TRP channels-encoded genes but their functions have remained elusive yet. Here, we reported functions of a putative TRP-like calcium ion channel in the filamentous fungus Aspergillus nidulans. Hydrophilicity and domain prediction indicated that the AN9146 encodes a protein that contains six TM domains with long N and C termini similar to the topology predicted for some members of the TRP family, so referred as TrpA. Deletion of trpA resulted in a sharp reduction in the number of conidial production at 37° , suggesting trpA may involve in response to high temperature. However, these defects in mutants can be rescued to the level of wild-type by adding extra-cellular Ca2+. Moreover, the fact that the phenotypic defects are exacerbated by double deletions of TrpA with either of identified high affinity calcium channel CchA, MidA or calcium P-type ATPase PmrA, suggest that TrpA probably plays an important role in high-affinity calcium transportation. Interestingly, we found TrpA’s localization was dynamic. When hyphal cells were cultured under the normal condition, majority of them localized in the membrane of vesicles along with the vesicle secretion network. However, when treated with the cell-wall disruption reagent-congo red, TrpA could translocate to plasma membrane. Therefore, together with data for the trpA deletion mutant showed more sensitive to congo red and caspofungin than that of wild type, this information implies that TrpA may also works as a plasma-membrane ion channel which involves the cell-wall integration. Further detail data are ongoing.

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Link Conference abstract: 

ECFG 15

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