Functional Analysis of Water Channels in Barley Roots
Author(s) -
Maki Katsuhara,
Yoshiko Akiyama,
Kazuki Koshio,
Mineo Shibasaka,
Kunihiro Kasamo
Publication year - 2002
Publication title -
plant and cell physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.975
H-Index - 152
eISSN - 1471-9053
pISSN - 0032-0781
DOI - 10.1093/pcp/pcf102
Subject(s) - botany , chemistry , biology
We identified three genes homologous to water channels in the plasma membrane type subfamily from roots of barley seedlings. These genes were designated HvPIP2;1, HvPIP1;3, and HvPIP1;5 after comparison to Arabidopsis aquaporins. Competitive reverse transcription (RT)-PCR was applied in order to distinguish and to quantify their transcripts. The HvPIP2;1 transcript was the most abundant among the three in roots. Salt stress (200 mM NaCl) down-regulated HvPIP2;1 (transcript and protein), but had almost no effect on the expressions of HvPIP1;3, or HvPIP1;5. Approximately equal amounts of the transcripts of the three were detected in shoots, and salt stress enhanced the expression of HvPIP2;1 but not of HvPIP1;3, or HvPIP1;5. HvPIP2;1 protein was confirmed to be localized in the plasma membrane. Functional expression of HvPIP2;1 in Xenopus oocytes confirmed that HvPIP2;1 encoded an aquaporin that transports water. This water permeability was reduced by HgCl(2), which is a typical water channel inhibitor. This activity was not modified by some inhibitors against protein kinase and protein phosphatase.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom