HP30-2, a mitochondrial PRAT protein for import of signal sequence-less precursor proteins in Arabidopsis thaliana

作     者：Claudia Rossig John Gray Oscar Valdes Sachin Rustgi Diter von Wettstein Christiane Reinbothe Steffen Reinbothe 

作者机构：Laboratory of Plant Molecular Genetics and Laboratory of Environmental and Systems Biology Grenoble-Alpes-University Grenoble France Department of Biological Sciences University of Toledo 2801 West Bancroft Street Toledo OH 43606 USA Department of Plant and Environmental Sciences Pee Dee Research and Education Center Clemson University Florence SC 29506 USA Department of Crop and Soil Sciences Washington State University Pullman WA 99164-6420 USA 

出 版 物：《Journal of Integrative Plant Biology》 (植物学报（英文版）)

年 卷 期：2017年第59卷第8期

页      面：535-551页

核心收录：

学科分类：0710[理学-生物学] 071001[理学-植物学] 07[理学] 0901[农学-作物学] 0703[理学-化学] 0902[农学-园艺学] 

基　　金：supported by the Chaire d’Excellence Program of the French Ministry of National Education and Research(to CR) 

主　　题：of as et in HP30-2,a mitochondrial PRAT protein for import of signal sequence-less precursor proteins in Arabidopsis thaliana for Figure NDC were TIM RNAi that 

摘      要：Chloroplasts and mitochondria contain a family of putative preprotein and amino acid transporters designated PRAT. Here, we analyzed the role of two previously characterized PRAT protein family members, encoded by At3g49560 （HP30） and At5g24650 （HP30-2）, in planta using a combination of genetic, cell biological and biochemical approaches. Expression studies and green fluorescent protein tagging identified HP30-2 both in chloroplasts and mitochondria, whereas HP30 was located exclusively in chloroplasts. Biochemical evidence was obtained for an association of mitochondrial HP30-2 with two distinct protein complexes, one containing the inner membrane translocase TIM22 and the other containing an alternative NAD（P）H dehydrogenase subunit （NDCI） implicated in a respiratory complex 1-1ike electron trans- port chain. Through its association with TIM22, HP30-2 is involved in the uptake of carrier proteins and other, hydrophobic membrane proteins lacking cleavable N H2-terminal presequences, whereas HP30-2＇s interaction with NDC1 may permit controlling mitochondrial biogenesis and activity.