Characterization of aquaporin-6 as a nitrate channel in mammalian cells. Requirement of pore-lining residue threonine 63.

A Single-Pore Residue Renders the Arabidopsis Root Anion Channel SLAH2 Highly Nitrate Selective.

In contrast to animal cells, plants use nitrate as a major source of nitrogen. Following the uptake of nitrate, this major macronutrient is fed into the vasculature for long-distance transport. The Arabidopsis thaliana shoot expresses the anion channel SLOW ANION CHANNEL1 (SLAC1) and its homolog SLAC1 HOMOLOGOUS3 (SLAH3), which prefer nitrate as substrate but cannot exclude chloride ions. By co...

Molecular Dynamics Simulation of Water Transportation through Aquaporin-4 in Rat Brain Cells

This paper investigates the mechanism of water transportation through aquaporin-4(AQP4) of ratbrain cells by means of molecular dynamics simulation with CHARMM software. The AQP4 wasembedded into a bilayer made of Dimystroilphosphatylcholine (DMPC). The results illustrate thatwater molecules move through AQP4's channel with change of orientation of oxygen of eachwater molecule.

Qiang Shan , Justine L . Haddrill and Joseph Receptors AGlycine and GABA ) in the ′ Pore - lining Threonine Residue ( T 6 Comparative Surface Accessibility of a

Replacement of threonine-55 with glycine decreases the reduction rate of OsTrx20 by glutathione

Thioredoxins (Trxs) are small ubiquitous oxidoreductase proteins with two redox-active Cys residues in a conserved active site (WCG/PPC) that regulate numerous target proteins via thiol/disulfide exchanges in the cells of prokaryotes and eukaryotes. The isoforms OsTrx23 with a typical active site (WCGPC) and OsTrx20 with an atypical active site (WCTPC) are two  Trx h- type isoforms in rice that ...

Characterization of a new vacuolar membrane aquaporin sensitive to mercury at a unique site.

The membranes of plant and animal cells contain aquaporins, proteins that facilitate the transport of water. In plants, aquaporins are found in the vacuolar membrane (tonoplast) and the plasma membrane. Many aquaporins are mercury sensitive, and in AQP1, a mercury-sensitive cysteine residue (Cys-189) is present adjacent to a conserved Asn-Pro-Ala motif. Here, we report the molecular analysis of...