For each citation that was shared on social media (LinkedIn, Facebook, or Twitter) with the “@GenScript” tag, the author will be rewarded with a $10 Amazon gift card or 2,000 GS points.

The transmembrane domain 6 of vacuolar H(+)-pyrophosphatase mediates protein targeting and proton transport.

Biochim Biophys Acta.. 2011-01;  1807(1):59-67
Pan YJ, Lee CH, Hsu SH, Huang YT, Lee CH, Liu TH, Chen YW, Lin SM, Pan RL. Department of Life Science and Institute of Bioinformatics and Structural Biology, College of Life Science, National Tsing Hua University, Hsin Chu 30043, Taiwan, Republic of China
Products/Services Used Details Operation


Vacuolar H+-pyrophosphatase (V-PPase; EC plays a significant role in the maintenance of the pH in cytoplasm and vacuoles via proton translocation from the cytosol to the vacuolar lumen at the expense of PPi hydrolysis. The topology of V-PPase as predicted by TopPred II suggests that the catalytic site is putatively located in loop e and exposed to the cytosol. The adjacent transmembrane domain 6 (TM6) is highly conserved and believed to participate in the catalytic function and conformational stability of V-PPase. In this study, alanine-scanning mutagenesis along TM6 of the mung bean V-PPase was carried out to identify its structural and functional role. Mutants Y299A, A306S and L317A exhibited gross i... More


Proton translocation; Tonoplast; Vacuole; Vacuolar H+-pyrophosphatase; Site-directed mutagenesis