Title data
Weig, Alfons ; Jakob, Christiane:
Functional identification of the glycerol permease activity of Arabidopsis thaliana NLM1 and NLM2 proteins by heterologous expression in Saccharomyces cerevisiae.
In: FEBS Letters.
Vol. 481
(2000)
Issue 3
.
- pp. 293-298.
ISSN 1873-3468
DOI: https://doi.org/10.1016/S0014-5793(00)02027-5
Abstract in another language
NLM proteins (NOD26-like major intrinsic proteins) from plants contain amino acid sequence signatures which can be found in aquaporins including plant plasma membrane intrinsic proteins and tonoplast intrinsic proteins and glycerol permeases such as the Escherichia coli GlpF and the yeast FPS1 proteins. Heterologous expression of two members of the NLM subgroup from Arabidopsis thaliana (AtNLM1 and AtNLM2) in baker's yeast demonstrated the glycerol permease activity in addition to the previously described aquaporin activity of AtNLM1. The transport was non-saturable up to 100 mM extracellular glycerol concentration. Longer-chain sugar alcohols did not compete with the transport of radiolabelled glycerol and hexoses were also not transported through the pore.
Further data
Item Type: | Article in a journal |
---|---|
Refereed: | Yes |
Additional notes: | BAYCEER21874 |
Keywords: | MIP; aquaporin; AtNLM; AtNLM1; AtNLM2; Glycerol Transport; Heterologous Expression; water transport; Plants; AtNIP2-1 |
Institutions of the University: | Faculties Faculties > Faculty of Biology, Chemistry and Earth Sciences Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology > Chair Plant Physiology Research Institutions Research Institutions > Research Centres Research Institutions > Research Centres > Bayreuth Center of Ecology and Environmental Research- BayCEER |
Result of work at the UBT: | Yes |
DDC Subjects: | 500 Science 500 Science > 570 Life sciences, biology |
Date Deposited: | 21 May 2014 09:06 |
Last Modified: | 11 Mar 2016 09:58 |
URI: | https://eref.uni-bayreuth.de/id/eprint/395 |