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Functional identification of the glycerol permease activity of Arabidopsis thaliana NLM1 and NLM2 proteins by heterologous expression in Saccharomyces cerevisiae
Author(s) -
Weig Alfons R.,
Jakob Christiane
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02027-5
Subject(s) - aquaporin , permease , biochemistry , heterologous expression , glycerol , arabidopsis thaliana , yeast , saccharomyces cerevisiae , biology , escherichia coli , arabidopsis , heterologous , amino acid , chemistry , gene , recombinant dna , mutant
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.