CO2 Transport by PIP2 Aquaporins of Barley

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F14%3A43887739" target="_blank" >RIV/60076658:12310/14:43887739 - isvavai.cz</a>

Výsledek na webu

<a href="http://pcp.oxfordjournals.org/content/55/2/251.full.pdf+html" target="_blank" >http://pcp.oxfordjournals.org/content/55/2/251.full.pdf+html</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1093/pcp/pcu003" target="_blank" >10.1093/pcp/pcu003</a>

Jazyk výsledku

angličtina

Název v původním jazyce

CO2 Transport by PIP2 Aquaporins of Barley

Popis výsledku v původním jazyce

CO2 permeability of plasma membrane intrinsic protein 2 (PIP2) aquaporins of Hordeum vulgare L. was investigated. Five PIP2 members were heterologously expressed in Xenopus laevis oocytes. CO2 permeability was determined by decrease of cytosolic pH in CO2-enriched buffer using a hydrogen ion-selective microelectrode. HvPIP2; 1, HvPIP2; 2, HvPIP2; 3 and HvPIP2; 5 facilitated CO2 transport across the oocyte cell membrane. However, HvPIP2; 4 that is highly homologous to HvPIP2; 3 did not. The isoleucine residue at position 254 of HvPIP2; 3 was conserved in PIP2 aquaporins of barley, except HvPIP2; 4, which possesses methionine instead. CO2 permeability was lost by the substitution of the Ile254 of HvPIP2; 3 by methionine, while water permeability was notaffected. These results suggest that PIP2 aquaporins are permeable to CO2. and the conserved isoleucine at the end of the E-loop is crucial for CO2 selectivity.

Název v anglickém jazyce

CO2 Transport by PIP2 Aquaporins of Barley

Popis výsledku anglicky

CO2 permeability of plasma membrane intrinsic protein 2 (PIP2) aquaporins of Hordeum vulgare L. was investigated. Five PIP2 members were heterologously expressed in Xenopus laevis oocytes. CO2 permeability was determined by decrease of cytosolic pH in CO2-enriched buffer using a hydrogen ion-selective microelectrode. HvPIP2; 1, HvPIP2; 2, HvPIP2; 3 and HvPIP2; 5 facilitated CO2 transport across the oocyte cell membrane. However, HvPIP2; 4 that is highly homologous to HvPIP2; 3 did not. The isoleucine residue at position 254 of HvPIP2; 3 was conserved in PIP2 aquaporins of barley, except HvPIP2; 4, which possesses methionine instead. CO2 permeability was lost by the substitution of the Ile254 of HvPIP2; 3 by methionine, while water permeability was notaffected. These results suggest that PIP2 aquaporins are permeable to CO2. and the conserved isoleucine at the end of the E-loop is crucial for CO2 selectivity.

Druh

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

CEP obor

ED - Fyziologie

OECD FORD obor

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Projekt

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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

Plant and Cell Physiology

ISSN

0032-0781

e-ISSN

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Svazek periodika

55

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

7

Strana od-do

251-257

Kód UT WoS článku

000331400900003

EID výsledku v databázi Scopus

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