ArticleMolecular biology of the cell1997
A folded protein can be transported across the chloroplast envelope and thylakoid membranes.
Article in Molecular biology of the cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 175 citations in OpenAlex.
- GREEN FLUORESCENT PROTEIN variants with enhanced folding are more efficiently imported into chloroplasts.Plant physiology · 2022Article
- Electrochromic shift supports the membrane destabilization model of Tat-mediated transport and shows ion leakage during Sec transport.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Transport of Folded Proteins by the Tat System.The protein journal · 2019Review
- The Twin-Arginine Pathway for Protein Secretion.EcoSal Plus · 2019Review
- Evaluating the Functional Pore Size of Chloroplast TOC and TIC Protein Translocons: Import of Folded Proteins.The Plant cell · 2018Article
- The Tat protein transport system: intriguing questions and conundrums.FEMS microbiology letters · 2018Review
- Probing the quality control mechanism of theThe Journal of biological chemistry · 2018Article
- How to achieve Tat transport with alien TatA.Scientific reports · 2017Article
- Chloroplast Hsp93 Directly Binds to Transit Peptides at an Early Stage of the Preprotein Import Process.Plant physiology · 2016Article
- New insights into the mechanism of chloroplast protein import and its integration with protein quality control, organelle biogenesis and development.Journal of molecular biology · 2015Review
- Evolution of a plant-specific copper chaperone family for chloroplast copper homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Effect of cargo size and shape on the transport efficiency of the bacterial Tat translocase.FEBS letters · 2013Article
- Energetic cost of protein import across the envelope membranes of chloroplasts.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Cell adhesion molecule DdCAD-1 is imported into contractile vacuoles by membrane invagination in a Ca2+- and conformation-dependent manner.The Journal of biological chemistry · 2009Article
- A stromal pool of TatA promotes Tat-dependent protein transport across the thylakoid membrane.The Journal of biological chemistry · 2008Article
- The 1.38 A crystal structure of DmsD protein from Salmonella typhimurium, a proofreading chaperone on the Tat pathway.Proteins · 2008Article
- The chloroplast Tat pathway utilizes the transmembrane electric potential as an energy source.Biophysical journal · 2007Article
- A scFv antibody mutant isolated in a genetic screen for improved export via the twin arginine transporter pathway exhibits faster folding.Journal of molecular biology · 2007Article
- Large-scale translocation reversal within the thylakoid Tat system in vivo.The Journal of cell biology · 2005Article
- A little help from my friends: quality control of presecretory proteins in bacteria.Journal of bacteriology · 2004Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many thylakoid lumenal proteins are nuclear encoded, cytosolically synthesized, and reach their functional location after posttranslational targeting across two chloroplast envelope membranes and the thylakoid membrane via proteinaceous transport systems. To study whether these transmembrane transport machineries can translocate folded structures, we overexpressed the 17-kDa subunit of the oxygen-evolving complex of photosystem II (prOE17) that had been modified to contain a unique C-terminal cysteine. This allowed us to chemically link a terminal 6.5-kDa bovine pancreatic trypsin inhibitor (BPTI) moiety to prOE17 to create the chimeric protein prOE17-BPTI. Redox reagents and an irreversible sulfhydryl-specific cross-linker, bis-maleimidohexane, were used to manipulate the structure of BPTI. Import of prOE17-BPTI into isolated chloroplasts and thylakoids demonstrates that the small tightly folded BPTI domain is carried across both the chloroplast envelopes and the delta pH-dependent transmembrane transporter of the thylakoid membrane when linked to the correctly targeted OE17 precursor. Transport proceeded even when the BPTI moiety was internally cross-linked into a protease-resistant form. These data indicate that unfolding is not a ubiquitous requirement for protein translocation and that at least some domains of targeted proteins can maintain a nonlinear structure during their translocation into and within chloroplasts.
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