Mechanistic Studies of the Genetically Encoded Fluorescent Protein Voltage Probe ArcLight

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F14%3A43887570" target="_blank" >RIV/60076658:12310/14:43887570 - isvavai.cz</a>

Výsledek na webu

<a href="http://www.plosone.org/article/Authors/info:doi/10.1371/journal.pone.0113873" target="_blank" >http://www.plosone.org/article/Authors/info:doi/10.1371/journal.pone.0113873</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1371/journal.pone.0113873" target="_blank" >10.1371/journal.pone.0113873</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Mechanistic Studies of the Genetically Encoded Fluorescent Protein Voltage Probe ArcLight

Popis výsledku v původním jazyce

ArcLight, a genetically encoded fluorescent protein voltage probe with a large Delta F/Delta V, is a fusion between the voltage sensing domain of the Ciona instestinalis voltage sensitive phosphatase and super ecliptic pHluorin carrying a single mutation(A227D in the fluorescent protein). Without this mutation the probe produces only a very small change in fluorescence in response to voltage deflections (similar to 1%). The large signal afforded by this mutation allows optical detection of action potentials and sub-threshold electrical events in single-trials in vitro and in vivo. However, it is unclear how this single mutation produces a probe with such a large modulation of its fluorescence output with changes in membrane potential. In this study, we identified which residues in super ecliptic pHluorin (vs eGFP) are critical for the ArcLight response, as a similarly constructed probe based on eGFP also exhibits large response amplitude if it carries these critical residues. We found

Název v anglickém jazyce

Mechanistic Studies of the Genetically Encoded Fluorescent Protein Voltage Probe ArcLight

Popis výsledku anglicky

ArcLight, a genetically encoded fluorescent protein voltage probe with a large Delta F/Delta V, is a fusion between the voltage sensing domain of the Ciona instestinalis voltage sensitive phosphatase and super ecliptic pHluorin carrying a single mutation(A227D in the fluorescent protein). Without this mutation the probe produces only a very small change in fluorescence in response to voltage deflections (similar to 1%). The large signal afforded by this mutation allows optical detection of action potentials and sub-threshold electrical events in single-trials in vitro and in vivo. However, it is unclear how this single mutation produces a probe with such a large modulation of its fluorescence output with changes in membrane potential. In this study, we identified which residues in super ecliptic pHluorin (vs eGFP) are critical for the ArcLight response, as a similarly constructed probe based on eGFP also exhibits large response amplitude if it carries these critical residues. We found

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2014

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

PLoS One

ISSN

1932-6203

e-ISSN

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Svazek periodika

9

Číslo periodika v rámci svazku

11

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

21

Strana od-do

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Kód UT WoS článku

000346766900077

EID výsledku v databázi Scopus

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