期刊
MOLECULAR PLANT
卷 2, 期 6, 页码 1397-1409出版社
CELL PRESS
DOI: 10.1093/mp/ssp079
关键词
Arabidopsis; chloroplast; import; protein targeting; Tic55
资金
- Carl Tryggers Foundation
- Swedish Research Councils FORMAS
- Royal Swedish Academy of Sciences
- Biotechnology and Biological Sciences Research Council
- Royal Society Rosenheim Research Fellowship
- Biotechnology and Biological Sciences Research Council [BB/F020325/1] Funding Source: researchfish
- BBSRC [BB/F020325/1] Funding Source: UKRI
The Tic55 (Translocon at the inner envelope membrane of chloroplasts, 55 kDa) protein was identified in pea as a putative regulator, possibly linking chloroplast protein import to the redox state of the photosynthetic machinery. Two Tic55 homologs have been proposed to exist in Arabidopsis: atTic55-II and AtPTC52 (Protochlorophyllide-dependent Translocon Component, 52 kDa; has also been called atTic55-IV). Our phylogenetic analysis shows that atTic55-II is an ortholog of psTic55 from pea (Pisum sativum), and that AtPTC52 is a more distant homolog of the two. AtPTC52 was included in this study to rule out possible functional links between the proteins in Arabidopsis. No detectable mutant phenotypes were found in two independent T-DNA knockout mutant plant lines for each Arabidopsis protein, when compared with wild-type: visible appearance, chlorophyll content, photosynthetic performance, and chloroplast protein import, for example, were all normal. Both wild-type and tic55-II mutant chloroplasts exhibited deficient protein import when treated with diethylpyrocarbonate, indicating that Tic55 is not the sole target of this reagent in relation to protein import. Furthermore, ptc52 mutant chloroplasts were not defective with respect to pPORA import, which was previously reported to involve PTC52 in barley. Thus, we conclude that atTic55-II and AtPTC52 are not strictly required for functional protein import in Arabidopsis.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据