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20231226043425.0 |
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231226s2023 xx |||||o 00| ||eng c |
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|a 10.1111/nph.18658
|2 doi
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|a pubmed24n1165.xml
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|a (DE-627)NLM349773106
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|a (NLM)36464797
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
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|a Hou, Yu
|e verfasserin
|4 aut
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|a A cyclic lipopeptide produced by an antagonistic bacterium relies on its tail and transient receptor potential-type Ca2+ channels to immobilize a green alga
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|c 2023
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 03.02.2023
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|a Date Revised 08.02.2023
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a © 2022 The Authors New Phytologist © 2022 New Phytologist Foundation.
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|a The antagonistic bacterium Pseudomonas protegens secretes the cyclic lipopeptide (CLiP) orfamide A, which triggers a Ca2+ signal causing rapid deflagellation of the microalga Chlamydomonas reinhardtii. We performed chemical synthesis of orfamide A derivatives and used an aequorin reporter line to measure their Ca2+ responses. Immobilization of algae was studied using a modulator and mutants of transient receptor potential (TRP)-type channels. By investigating targeted synthetic orfamide A derivatives, we found that N-terminal amino acids of the linear part and the terminal fatty acid region are important for the specificity of the Ca2+ -signal causing deflagellation. Molecular editing indicates that at least two distinct Ca2+ -signaling pathways are triggered. One is involved in deflagellation (Thr3 change, fatty acid tail shortened by 4C), whereas the other still causes an increase in cytosolic Ca2+ in the algal cells, but does not cause substantial deflagellation (Leu1 change, fatty acid hydroxylation, fatty acid changes by 2C). Using mutants, we define four TRP-type channels that are involved in orfamide A signaling; only one (ADF1) responds additionally to low pH. These results suggest that the linear part of the CLiP plays one major role in Ca2+ signaling, and that orfamide A uses a network of algal TRP-type channels for deflagellation
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a ADF1
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|a Ca2+ channels
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|a Chlamydomonas reinhardtii
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|a Pseudomonas protegens
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|a cilia/flagella
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|a cyclic lipopeptides
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| 650 |
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|a Lipopeptides
|2 NLM
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| 700 |
1 |
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|a Bando, Yuko
|e verfasserin
|4 aut
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| 700 |
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|a Carrasco Flores, David
|e verfasserin
|4 aut
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| 700 |
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|a Hotter, Vivien
|e verfasserin
|4 aut
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| 700 |
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|a Das, Ritam
|e verfasserin
|4 aut
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| 700 |
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|a Schiweck, Bastian
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Melzer, Tommy
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Arndt, Hans-Dieter
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Mittag, Maria
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t The New phytologist
|d 1979
|g 237(2023), 5 vom: 15. März, Seite 1620-1635
|w (DE-627)NLM09818248X
|x 1469-8137
|7 nnns
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| 773 |
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|g volume:237
|g year:2023
|g number:5
|g day:15
|g month:03
|g pages:1620-1635
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| 856 |
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|u http://dx.doi.org/10.1111/nph.18658
|3 Volltext
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|d 237
|j 2023
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|c 03
|h 1620-1635
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