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Cytosolic HSP90 Cochaperones HOP and FKBP Interact with Freshly Synthesized Chloroplast Preproteins of Arabidopsis

Molecular Plant 2011年第6期4卷 1133-1145页

作者： Christine Fellerer Regina Schweiger Katharina Schongruber Jurgen Soil Serena Schwenker Department of Biology 1 Botany Ludwig-Maximilians-Universitat Munchen Grobhaderner Strasse 2-4 D-82152 Planegg-Martinsried Germany Munich Center for Integrated Protein Science CiPSM Ludwig-Maximilians-Universitut Munchen Feodor-Lynen-Strasse 25 D-81377 Munich Germany

Most chloroplast and mitochondrial proteins are synthesized in the cytosol of the plant cell and have to be imported into the organelles post-translationally. Molecular chaperones play an important role in preventing protein aggregation of freshly translated preproteins and assist in maintaining the preproteins in an import competent state. Pre- proteins can associate with HSP70, HSP90, and 14-3-3 proteins in the cytosol. In this study, we analyzed a large set of wheat germ-translated chloroplast preproteins with respect to their chaperone binding. Our results demonstrate that the formation of distinct 14-3-3 or HSP90 containing preprotein complexes is a common feature in post-translational protein transport in addition to preproteins that seem to interact solely with HSP70. We were able to identify a diverse and extensive class of preproteins as HSP90 substrates, thus providing a tool for the investigation of HSP90 client protein association. The analyses of chimeric HSP90 and 14-3-3 binding preproteins with exchanged transit peptides indicate an involvement of both the transit peptide and the mature part of the proteins, in HSP90 binding. We identified two partner components of the HSP90 cycle, which were present in the preprotein containing high-molecular-weight complexes, the HSP70/HSP90 organizing protein HOP, as well as the immunophilin FKBP73. The results establish chloroplast preproteins as a general class of HSP90 client proteins in plants using HOP and FKBP as novel cochaperones.

关键词： Wheat germ in vitro translation chloroplast import chaperone.

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Cell-free synthesis of stable isotope-labeled internal standards for targeted quantitative proteomics

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Synthetic and Systems Biotechnology 2018年第2期3卷 97-104页

作者： Ryohei Narumi Keiko Masuda Takeshi Tomonaga Jun Adachi Hiroki RUeda Yoshihiro Shimizu Laboratory of Proteome Research National Institutes of Biomedical InnovationHealth and Nutrition7-6-8Satio-AsagiIbarakiOsaka 567-0085Japan Laboratory for Single Cell Mass Spectrometry RIKEN Quantitative Biology Center(QBiC)6-2-3FuruedaiSuitaOsaka 565-0874Japan Department of Systems Pharmacology Graduate School of MedicineThe University of Tokyo7-3-1 HongoBunkyo-kuTokyo 113-0033Japan Laboratory for Synthetic Biology RIKEN Quantitative Biology Center(QBiC)6-2-3FuruedaiSuitaOsaka 565-0874Japan Laboratory for Cell-Free Protein Synthesis RIKEN Quantitative Biology Center(QBiC)6-2-3FuruedaiSuitaOsaka 565-0874Japan

High-sensitivity mass spectrometry approaches using selected reaction monitoring(SRM)or multiple reaction monitoring(MRM)methods are powerful tools for targeted quantitative proteomics-based investigation of dynamics in specific biological *** high-sensitivity detection of lowabundance proteins and their quantification using this technique employ stable isotope-labeled peptide internal ***,there are various ways for preparing standards,including chemical peptide synthesis,cellular protein expression,and cell-free protein or peptide ***-free protein synthesis(CFPS)or in vitro translation(IVT)systems in particular provide high-throughput and low-cost preparation methods,and various cell types and reconstituted forms are now commercially ***,we review the use of such systems for precise and reliable protein quantification.

关键词： Absolute quantification Mass spectrometry Cell-free protein synthesis system in vitro translation Targeted quantitative proteomics PURE system

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Yeast knockout library allows for efficient testing of genomic mutations for cell-free protein synthesis

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Synthetic and Systems Biotechnology 2016年第1期1卷 2-6页

作者： Jennifer *** Lauren G.Clark Alaksh Choudhury C.Eric Hodgman Michael C.Jewett Department of Chemical and Biological Engineering Northwestern University2145 Sheridan RoadEvanstonIL 60208-3120USA Chemistry of Life Processes Institute 2170 Campus DriveEvanstonIL 60208-3120USA Masters in Biotechnology Program Northwestern University2145 Sheridan RoadEvanstonIL 60208-3120USA Robert H.Lurie Comprehensive Cancer Center Northwestern University676 N.St Clair StSuite 1200ChicagoIL 60611-3068USA Simpson Querrey Institute Northwestern University303 E.Superior StSuite 11-131ChicagoIL 60611-2875USA

Cell-free protein synthesis(CFPS)systems from crude lysates have benefitted from modifications to their enzyme *** example,functionally deleting enzymes in the source strain that are deleterious to CFPS can improve protein synthesis ***,making such modifications can take substantial *** a proof-of-concept to accelerate prototyping capabilities,we assessed the feasibility of using the yeast knockout collection to identify negative effectors in a Saccharomyces cerevisiae CFPS *** analyzed extracts made from six deletion strains that targeted the single deletion of potentially negative effectors(e.g.,nucleases).We found a statistically significant increase in luciferase yields upon loss of function of GCN3,PEP4,PPT1,NGL3,and XRN1 with a maximum increase of over 6-fold as compared to the wild *** work has implications for yeast CFPS and for rapidly prototyping strains to enable cell-free synthetic biology applications.

关键词： Cell-free protein synthesis Saccharomyces cerevisiae Synthetic biology in vitro translation Cell-free biology Protein expression

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