Functional identification of the glycerol permease activity of Arabidopsis thaliana NLM1 and NLM2 proteins by heterologous expression in Saccharomyces cerevisiae

被引:73
作者
Weig, AR [1 ]
Jakob, C [1 ]
机构
[1] Univ Bayreuth, Inst Plant Physiol, D-95440 Bayreuth, Germany
关键词
major intrinsic protein; aquaporin; aquaglyceroporin; water transport; glycerol transport; heterologous expression;
D O I
10.1016/S0014-5793(00)02027-5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 FPSL 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 mas 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. (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:293 / 298
页数:6
相关论文
共 24 条
[1]   The aquaporins, blueprints for cellular plumbing systems [J].
Agre, P ;
Bonhivers, M ;
Borgnia, MJ .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (24) :14659-14662
[2]   The Nicotiana tabacum plasma membrane aquaporin NtAQP1 is mercury-insensitive and permeable for glycerol [J].
Biela, A ;
Grote, K ;
Otto, B ;
Hoth, S ;
Hedrich, R ;
Kaldenhoff, R .
PLANT JOURNAL, 1999, 18 (05) :565-570
[3]   Aquaporins in Saccharomyces -: Genetic and functional distinctions between laboratory and wild-type strains [J].
Bonhivers, M ;
Carbrey, JM ;
Gould, SJ ;
Agren, P .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (42) :27565-27572
[4]   Cellular and molecular biology of the aquaporin water channels [J].
Borgnia, M ;
Nielsen, S ;
Engel, A ;
Agre, P .
ANNUAL REVIEW OF BIOCHEMISTRY, 1999, 68 :425-458
[5]   Oligomerization state of MIP proteins expressed in Xenopus oocytes as revealed by freeze-fracture electron-microscopy analysis [J].
Bron, P ;
Lagrée, V ;
Froger, A ;
Rolland, JP ;
Hubert, JF ;
Delamarche, C ;
Deschamps, S ;
Pellerin, I ;
Thomas, D ;
Haase, W .
JOURNAL OF STRUCTURAL BIOLOGY, 1999, 128 (03) :287-296
[6]   Purification and functional reconstitution of soybean nodulin 26. An aquaporin with water and glycerol transport properties [J].
Dean, RM ;
Rivers, RL ;
Zeidel, ML ;
Roberts, DM .
BIOCHEMISTRY, 1999, 38 (01) :347-353
[7]   AN MF ALPHA-1-SUC2 (ALPHA-FACTOR-INVERTASE) GENE FUSION FOR STUDY OF PROTEIN LOCALIZATION AND GENE-EXPRESSION IN YEAST [J].
EMR, SD ;
SCHEKMAN, R ;
FLESSEL, MC ;
THORNER, J .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1983, 80 (23) :7080-7084
[8]   NODULIN-26, A PERIBACTEROID MEMBRANE NODULIN IS EXPRESSED INDEPENDENTLY OF THE DEVELOPMENT OF THE PERIBACTEROID COMPARTMENT [J].
FORTIN, MG ;
MORRISON, NA ;
VERMA, DPS .
NUCLEIC ACIDS RESEARCH, 1987, 15 (02) :813-824
[9]   Prediction of functional residues in water channels and related proteins [J].
Froger, A ;
Tallur, B ;
Thomas, D ;
Delamarche, C .
PROTEIN SCIENCE, 1998, 7 (06) :1458-1468
[10]   Aquaporin Nt-TIPa can account for the high permeability of tobacco cell vacuolar membrane to small neutral solutes [J].
Gerbeau, P ;
Güclü, J ;
Ripoche, P ;
Maurel, C .
PLANT JOURNAL, 1999, 18 (06) :577-587