FEBS Letters | |
Functional selectivity for glycerol of the nodulin 26 subfamily of plant membrane intrinsic proteins | |
Roberts, Daniel M1  Wills, David M1  Guenther, James F1  Wallace, Ian S1  | |
[1] Department of Biochemistry and Cellular and Molecular Biology, The University of Tennessee, Knoxville, TN 37996, USA | |
关键词: Aquaporin; Major intrinsic protein family; Nitrogen fixation; | |
DOI : 10.1016/S0014-5793(02)02955-1 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
The nodulin-like intrinsic protein (NIP) subfamily of water and solute channels in plants is named for nodulin 26 of legume nodules. Two NIPs, soybean nodulin 26 and Lotus japonicus LIMP2, show a distinct functional profile with a low intrinsic osmotic water permeability (P f) and the ability to flux uncharged polyols such as glycerol. NIPs have a conserved signature sequence within the ‘aromatic/arginine’ region that forms the selectivity filter for major intrinsic proteins. This sequence is a hybrid of glyceroporin and aquaporin residues as well as exhibiting substitutions unique to the NIP subfamily. Site-directed mutagenesis of a conserved tryptophan in helix 2 of LIMP2 shows that this is a major determinant of glycerol selectivity.
【 授权许可】
Unknown
【 预 览 】
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RO201912020311984ZK.pdf | 231KB | download |