Acyrthosiphon pisum AQP2: a multifunctional insect aquaglyceroporin

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081766%3A_____%2F12%3A00370467" target="_blank" >RIV/68081766:_____/12:00370467 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.bbamem.2011.11.032" target="_blank" >http://dx.doi.org/10.1016/j.bbamem.2011.11.032</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bbamem.2011.11.032" target="_blank" >10.1016/j.bbamem.2011.11.032</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Acyrthosiphon pisum AQP2: a multifunctional insect aquaglyceroporin

Popis výsledku v původním jazyce

Annotation of the recently sequenced genome of the pea aphid (Acyrthosiphon pisum) identified a gene ApAQP2 (ACYPI009194, Gene ID: 100168499) with homology to the Major Intrinsic Protein/aquaporin superfamily of membrane channel proteins. Phylogenetic analysis suggests that ApAQP2 is a member of an insect-specific clade of this superfamily. Water permeability analyses show that the ApAQP2 protein exhibits a robust mercury-insensitive aquaporin activity. However unlike the water-specific ApAQP1 protein,ApAQP2 forms a multifunctional transport channel that shows a wide permeability profile to a range of linear polyols. Gene expression analysis indicates that ApAQP2 is highly expressed in the insect bacteriocytes and the fat body. Overall the results demonstrate that ApAQP2 is a novel insect aquaglyceroporin which may be involved in water and polyol transport in support of the Buchnera symbiosis and aphid osmoregulation.

Název v anglickém jazyce

Acyrthosiphon pisum AQP2: a multifunctional insect aquaglyceroporin

Popis výsledku anglicky

Annotation of the recently sequenced genome of the pea aphid (Acyrthosiphon pisum) identified a gene ApAQP2 (ACYPI009194, Gene ID: 100168499) with homology to the Major Intrinsic Protein/aquaporin superfamily of membrane channel proteins. Phylogenetic analysis suggests that ApAQP2 is a member of an insect-specific clade of this superfamily. Water permeability analyses show that the ApAQP2 protein exhibits a robust mercury-insensitive aquaporin activity. However unlike the water-specific ApAQP1 protein,ApAQP2 forms a multifunctional transport channel that shows a wide permeability profile to a range of linear polyols. Gene expression analysis indicates that ApAQP2 is highly expressed in the insect bacteriocytes and the fat body. Overall the results demonstrate that ApAQP2 is a novel insect aquaglyceroporin which may be involved in water and polyol transport in support of the Buchnera symbiosis and aphid osmoregulation.

Druh

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

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

—

Projekt

—

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2012

Kód důvěrnosti údajů

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

Název periodika

Biochimica Et Biophysica Acta-Biomembranes

ISSN

0005-2736

e-ISSN

—

Svazek periodika

1818

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

9

Strana od-do

627-635

Kód UT WoS článku

000301155600031

EID výsledku v databázi Scopus

—