Single amino acid substitutions in the selectivity filter render NbXIP1;1α aquaporin water permeable.

ABSTRACT:

Background

Aquaporins (AQPs) are integral membrane proteins that facilitate transport of water and/or other small neutral solutes across membranes in all forms of life. The X Intrinsic Proteins (XIPs) are the most recently recognized and the least characterized aquaporin subfamily in higher plants. XIP1s have been shown to be impermeable to water but permeable to boric acid, glycerol, hydrogen peroxide and urea. However, uncertainty regarding the determinants for selectivity and lack of an activity that is easy to quantify have hindered functional investigations. In an effort to resolve these issues, we set out to introduce water permeability in Nicotiana benthamiana XIP1;1α (NbXIP1;1α), by exchanging amino acid residues of predicted alternative aromatic/arginine (ar/R) selectivity

SUBMITTER: Ampah-Korsah H 

PROVIDER: S-EPMC5345251 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature