@article{ARTIKA_2010, title={Structural and Functional Analysis of FLAG Tagged-Subunit 8 of Yeast Saccharomyces cerevisiae Mitochondrial ATP Synthase}, volume={1}, url={https://jurnal.permi.or.id/index.php/mionline/article/view/39}, DOI={10.5454/mi.1.1.8}, abstractNote={<p class="MsoNormal" style="text-align: left; text-indent: 0in; margin: 0in 0in 0pt; mso-layout-grid-align: none;" align="left"><span style="font-family: "Times New Roman","serif"; font-size: 12pt; mso-bidi-font-weight: bold; mso-no-proof: no;">Yeast mitochondrial ATP synthase is a multisubunit complex composed of at least 17 different subunits. Subunit 8 of yeast mitochondrial ATP synthase is a hydrophobic protein of 48 amino acids encoded by the mitochondrial <em>ATP8 </em>gene. Although ATP synthase from eukaryotes and prokaryotes shows a similar basic structure, no homologue of subunit 8 is found in prokaryotes such as <em>Escherichia coli</em>. Subunit 8 has three distinct domains; an N-terminal domain, a central hydrophobic domain and a C-terminal domain. In order to elucidate its structure and function, a set of nuclear genes encoding subunit 8 variants was designed to incorporate a FLAG tag at the C-terminus and a mitochondrial signal peptide at the N-terminus. Each gene was cloned into a yeast expression vector and then allotopically expressed in a yeast strain lacking endogenous subunit 8. Structural and functional analysis showed that the hydrophobic character of the central hydrophobic domain of subunit 8 is critical for the ATP synthase function. Subunit 8 is sensitive to charge manipulation at the C-terminus. The positively charged residues at the C-terminal domain are important for subunit 8 assembly and hence its function.</span><span style="font-family: "Times New Roman","serif"; font-size: 12pt;"></span></p>}, number={1}, journal={Microbiology Indonesia}, author={ARTIKA, I MADE}, year={2010}, month={Mar.}, pages={8} }