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:
Conference abstracts, posters & presentations
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Title
Author
Year
Number
Poster
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v
Kimihide Muragaki1, Kenji Uehara1, Toru Takahashi2,3, Youhei Yamagata3 and Keietsu Abe1,3*
2011
NULL
n/a
-
v
Ryota Hattori , Mayumi Matsusita-Morita , Sawaki
Tada , Junichiro Marui , Ikuyo Furukawa , Satoshi Suzuki , Hitoshi Amano , Hiroki Ishida , Youhei Yamagata , Michio Takeuchi , Ken-Ichi Kusumoto2011
63)
n/a
-
v
Kiira Vuoristo, Kirsi Bromann, Mervi Toivari, Laura Ruohonen, Tiina Nakari-Setälä
2011
62)
n/a
-
v
Jakob B. Nielsen, Michael L. Nielsen, Christian Rank, Marie L.
Klejnstrup, Paiman Khorsand-Jamal, Dorte M. K. Holm, Bjarne G. Hansen, Jens C. Frisvad, Thomas O. Larsen and Uffe H. Mortensen2011
61)
n/a
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v
Uffe H. Mortensen, Michael L. Nielsen, Jakob B. Nielsen,
Christian Rank, Marie L. Klejnstrup, Dorte K. Holm, Katrine H. Brogaard, Bjarne G. Hansen, Jens C. Frisvad, Thomas O. Larsen2011
NULL
n/a
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v
Marie Louise Klejnstrup*, Morten
Thrane Nielsen, Jens Christian Frisvad, Uffe Mortensen, Thomas Ostenfeld Larsen. Department of Systems Biology,2011
NULL
n/a
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v
Dorte K. Holm, Bjarne G. Hansen, Thomas O. Larsen, Uffe H. Mortensen
2011
NULL
n/a
-
v
.Outi M. Koivistoinen, Peter Richard, Merja Penttilä, Dominik
Mojzita2011
56)
n/a
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v
Thomas O. Larsen*, C.
Rank, M. Klejnstrup, M.L. Nielsen, J.B. Nielsen, D.M.K. Holm, K.H. Brogaard, B. Hansen, J.C. Frisvad and U.H. Mortensen.2011
55)
n/a
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v
Christian Rank*, Marie Louise Klejnstrup, Lene Maj Petersen, Jens Christian Frisvad,
Thomas Ostenfeld Larsen.2011
54)
n/a