https://scholars.lib.ntu.edu.tw/handle/123456789/624874
標題: | In search of tail-anchored protein machinery in plants: Reevaluating the role of arsenite transporters | 作者: | MANUEL MAESTRE-REYNA Wu S.-M Chang Y.-C Chen C.-C Maestre-Reyna A Wang A.H.-J Chang H.-Y. |
公開日期: | 2017 | 卷: | 7 | 來源出版物: | Scientific Reports | 摘要: | Although the mechanisms underlying selective targeting of tail-anchored (TA) membrane proteins are well established in mammalian and yeast cells, little is known about their role in mediating intracellular membrane trafficking in plant cells. However, a recent study suggested that, in green algae, arsenite transporters located in the cytosol (ArsA1 and ArsA2) control the insertion of TA proteins into the membrane-bound organelles. In the present work, we overproduced and purified these hydrophilic proteins to near homogeneity. The analysis of their catalytic properties clearly demonstrates that C. reinhardtii ArsA proteins exhibit oxyanion-independent ATPase activity, as neither arsenite nor antimonite showed strong effects. Co-expression of ArsA proteins with TA-transmembrane regions showed not only that the former interact with the latter, but that ArsA1 does not share the same ligand specificity as ArsA2. Together with a structural model and molecular dynamics simulations, we propose that C. reinhadtii ArsA proteins are not arsenite transporters, but a TA-protein targeting factor. Further, we propose that ArsA targeting specificity is achieved at the ligand level, with ArsA1 mainly carrying TA-proteins to the chloroplast, while ArsA2 to the endoplasmic reticulum. © 2017 The Author(s). |
URI: | https://www.scopus.com/inward/record.uri?eid=2-s2.0-85017109097&doi=10.1038%2fsrep46022&partnerID=40&md5=51936ff2020cedba41d61b7b683d1580 https://scholars.lib.ntu.edu.tw/handle/123456789/624874 |
ISSN: | 20452322 | DOI: | 10.1038/srep46022 | SDG/關鍵字: | arsenite transporting adenosine triphosphatase; arsenous acid derivative; membrane protein; plant protein; amino acid sequence; chemistry; Chlamydomonas; enzyme specificity; metabolism; molecular model; sequence alignment; Amino Acid Sequence; Arsenite Transporting ATPases; Arsenites; Chlamydomonas; Membrane Proteins; Models, Molecular; Plant Proteins; Sequence Alignment; Substrate Specificity |
顯示於: | 化學系 |
在 IR 系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。