CO2 Transport by PIP2 Aquaporins of Barley

Result code in 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>
Result on the web
<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>

Result language
angličtina
Original language name
CO2 Transport by PIP2 Aquaporins of Barley
Original language description
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.
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
ED - Physiology
OECD FORD branch
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Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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