检索结果-南通市图书馆

TOM9.2 Is a Calmodulin-Binding protein Critical for TOM Complex Assembly but Not for Mitochondrial protein import in Arabidopsis thaliana

引用

Molecular Plant 2017年第4期10卷 575-589页

作者： Nargis Parvin Chris Carrie Isabelle Pabst Antonia Laber Debabrata Laha Melanie V. Paul Peter Geigenberger Ralf Heermann Kirsten Jung Ute C. Vothknecht Fatima Chigri Department Biology I Botany Ludwig-Maximilians-University Munich GroBhaderner Stra6e 2-4 82152 Martinsried Germany Department Biology 1 Microbiology Ludwig-Maximilians-University Munich Grobhaderner Strabe 2-4 82152 Martinsried Germany Department of Biology Center for Integrated Protein Science (Munich) Ludwig-Maximilians-University Munich 81377 Munich Germany Center for Plant Molecular Biology Plant Physiology University of Tuebingen Auf der Morgenstelle 32 72076 Tuebingen Germany present address: Plant Cell Biology IZMB University of Bonn Kirschallee 153115 Bonn Germany Present address: Center for Plant Molecular Biology Developmental Genetics University of Tubingen Auf der Morgenstelle 32 72076 Tubingen Germany

The translocon on the outer membrane of mitochondria （TOM） facilitates the import of nuclear-encoded proteins. The principal machinery of mitochondrial protein transport seems conserved in eukaryotes; however, divergence in the composition and structure of TOM components has been observed between mammals, yeast, and plants. TOM9, the plant homolog of yeast Tom22, is significantly smaller due to a truncation in the cytosolic receptor domain, and its precise function is not understood. Here we provide evidence showing that TOM9.2 from Arabidopsis thaliana is involved in the formation of mature TOM com- plex, most likely by influencing the assembly of the pore-forming subunit TOM40. Dexamethasone- induced RNAi gene silencing of TOM9.2 results in a severe reduction in the mature TOM complex, and the assembly of newly imported TOM40 into the complex is impaired. Nevertheless, mutant plants are fully viable and no obvious downstream effects of the loss of TOM complex, i.e., on mitochondrial import ca- pacity, were observed. Furthermore, we found that TOM9.2 can bind calmodulin （CAM） in vitro and that CaM impairs the assembly of TOM complex in the isolated wild-type mitochondria, suggesting a regula- tory role of TOM9.2 and a possible integration of TOM assembly into the cellular calcium signaling network.

关键词： protein import plant mitochondria TOM complex calmodulin calcium signaling

来源：

维普期刊数据库评论

在线全文

维普期刊数据库

学校读者我要写书评

暂无评论

The Chloroplast import Receptor Toc90 Partially Restores the Accumulation of Toc159 Client proteins in the Arabidopsis thaliana ppi2 Mutant

引用

Molecular Plant 2011年第2期4卷 252-263页

作者： Sibylle Infanger Sylvain Bischof Andreas Hiltbrunner Birgit Agne Sacha Baginsky Felix Kessler Laboratoire de physiologie vegetale Universite de Neuchatel Rue Emile-Argand 11 2000 Neuchatel Switzerland Department of Biology ETH Zurich Universitatstrasse 2 8092 Zurich Switzerland University of Tubingen Centre for Plant Molecular Biology (ZMBP) Department of Plant Physiology auf der Morgenstelle 1 D-72076 Tubingen Germany Institute of Biochemistry and Biotechnology Martin-Luther-University Halle-Wittenberg Weinbergweg 22 06120 Halle (Saale)

Successful import of hundreds of nucleus-encoded proteins is essential for chloroplast biogenesis. The import of cytosolic precursor proteins relies on the Toc- （translocon at the outer chloroplast membrane） and Tic- （translocon at the inner chloroplast membrane） complexes. In Arabidopsis thaliana, precursor recognition is mainly mediated by outer membrane receptors belonging to two gene families： Toc34/33 and Toc159/132/120/90. The role in import and precursor selectivity of these receptors has been intensively studied, but the function of Toc90 still remains unclear. Here, we report the ability of Toc90 to support the import of Toc159 client proteins. We show that the overexpression of Toc90 partially complements the albino knockout of Toc159 and restores photoautotrophic growth. Several lines of evidence including proteome profiling demonstrate the import and accumulation of proteins essential for chloroplast biogenesis and functionality.

关键词： chloroplast protein import Toc159 substrate specificity proteomics

来源：

维普期刊数据库评论

在线全文

维普期刊数据库

学校读者我要写书评

暂无评论

import Determinants of Organelle-Specific and Dual Targeting Peptides of Mitochondria and Chloroplasts in Arabidopsis thaliana

引用

Molecular Plant 2014年第1期7卷 121-136页

作者： Changrong Ge Erika Spanning Elzbieta Glaser Ake Wieslander Department of Biochemistry and Biophysics Center for Biomembrane Research Stockholm University SE-106 91 Stockholm Sweden Medical Inflammation Research Department of Medical Biochemistry and Biophysics Karolinska Institute SE-171 77 Stockholm Sweden

Most of the mitochondrial and chloroplastic proteins are synthesized in the cytosol as precursor proteins carrying an N-terminal targeting peptide （TP） directing them specifically to a correct organelle. However, there is a group of proteins that are dually targeted to mitochondria and chloroplasts using an ambiguous N-terminal dual targeting peptide （dTP）. Here, we have investigated pattern properties of import determinants of organelle-specific TPs and dTPs combining mathematical multivariate data analysis （MVDA） with in vitro organellar import studies. We have used large datasets of mitochondrial and chloroplastic proteins found in organellar proteomes as well as manually selected data sets of experimentally confirmed organelle-specific TPs and dTPs from Arabidopsis thaliana. Two classes of organelle-specific TPs could be distinguished by MVDA and potential patterns or periodicity in the amino acid sequence contributing to the separation were revealed, dTPs were found to have intermediate sequence features between the organelle-specific TPs. Interestingly, introducing positively charged residues to the dTPs showed clustering towards the mitochondrial TPs in silico and resulted in inhibition of chloroplast, but not mitochondrial import in in vitro organellar import studies. These findings suggest that positive charges in the N-terminal region of TPs may function as an ＇avoidance signal＇ for the chloroplast import.

关键词： dual targeting ambiguous targeting signal mitochondria chloroplast protein import partial least square discriminant analysis Arabidopsis thaliana.

来源：

维普期刊数据库评论

在线全文

维普期刊数据库

学校读者我要写书评

暂无评论

The Chloroplast Outer Envelope Membrane:The Edge of Light and Excitement

引用

Journal of Integrative Plant Biology 2007年第8期49卷 1100-1111页

作者： Kentaro Inoue Department of Plant Sciences College of Agricultural & Environmental SciencesUniversity of CaliforniaOne Shields AvenueDavisCA 95616USA

The chloroplast is surrounded by a double-membrane envelope at which proteins, ions, and numerous metabolites including nucleotides, amino acids, fatty acids, and carbohydrates are exchanged between the two aqueous phases, the cytoplasm and the chloroplast stroma. The chloroplast envelope is also the location where the biosynthesis and accumulation of various lipids take place. By contrast to the inner membrane, which contains a number of specific transporters and acts as the permeability barrier, the chloroplast outer membrane has often been considered a passive compartment derived from the phagosomal membrane. However, the presence of galactoglycerolipids and β-barrel membrane proteins support the common origin of the outer membranes of the chloroplast envelope and extant cyanobacteria. Furthermore, recent progress in the field underlines that the chloroplast outer envelope plays important roles not only for translocation of various molecules, but also for regulation of metabolic activities and signaling processes. The chloroplast outer envelope membrane offers various interesting and challenging questions that are relevant to the understanding of organelle biogenesis, plant growth and development, and also membrane biology in general.

关键词： chloroplast envelope lipid biosynthesis outer membrane protein import putative solute channel

来源：

维普期刊数据库

同方期刊数据库评论

在线全文

学校读者我要写书评

暂无评论

欢迎您,

建议与咨询留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

时间限定

文献类型

馆藏选择

核心期刊

语言

文献类型

帮助

文字说明：

检索规则说明：

检索范例：

分类表

所选分类

限定检索结果

文献类型

馆藏范围

日期分布

学科分类号

主题

机构

作者

语言

在线全文

在线全文

在线全文

在线全文

请选择保存的检索档案：

请选择收藏分类：

通借通还

欢迎您,

建议与咨询 留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

时间限定

文献类型

馆藏选择

核心期刊

语言

文献类型

帮助

文字说明：

检索规则说明：

检索范例：

分类表

所选分类

限定检索结果

文献类型

馆藏范围

日期分布

学科分类号

主题

机构

作者

语言

在线全文

在线全文

在线全文

在线全文

请选择保存的检索档案： 新增检索档案 确定 取消

请选择收藏分类： 新增自定义分类 确定 取消

通借通还

建议与咨询留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

请选择保存的检索档案：

请选择收藏分类：