ArticleThe Journal of cell biology1999
Stromal processing peptidase binds transit peptides and initiates their ATP-dependent turnover in chloroplasts.
Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 99 citations in OpenAlex.
- Septin-mediated coupling of protein import and division during chloroplast evolution.bioRxiv : the preprint server for biology · 2026Article
- Plant plastids: from evolutionary origins to functional specialization and organelle interactions.Journal of experimental botany · 2025Review
- MULoc-target: Targeting peptide classification and detection using a protein language model.Briefings in bioinformatics · 2025Article
- Arabidopsis conditional photosynthesis mutants abc1k1 and var2 accumulate partially processed thylakoid preproteins and are defective in chloroplast biogenesis.Communications biology · 2025Article
- Large-scale top-down proteomics of the Arabidopsis thaliana leaf and chloroplast proteomes.Proteomics · 2023Article
- Chloroplast proteostasis: A story of birth, life, and death.Plant communications · 2023Review
- The roles of plant proteases and protease inhibitors in drought response: a review.Frontiers in plant science · 2023Review
- Understanding protein import in diverse non-green plastids.Frontiers in genetics · 2023Review
- Molecular mechanism of SRP-dependent light-harvesting protein transport to the thylakoid membrane in plants.Photosynthesis research · 2018Review
- Evolution and Design Principles of the Diverse Chloroplast Transit Peptides.Molecules and cells · 2018Review
- Chloroplast Proteases: Updates on Proteolysis within and across Suborganellar Compartments.Plant physiology · 2016Review
- Cucumber Necrosis Virus Recruits Cellular Heat Shock Protein 70 Homologs at Several Stages of Infection.Journal of virology · 2015Article
- The Arabidopsis Chloroplast Stromal N-Terminome: Complexities of Amino-Terminal Protein Maturation and Stability.Plant physiology · 2015Article
- Quantitative analysis of the chloroplast molecular chaperone ClpC/Hsp93 in Arabidopsis reveals new insights into its localization, interaction with the Clp proteolytic core, and functional importance.The Journal of biological chemistry · 2014Article
- The RNA-binding protein RNP29 is an unusual Toc159 transport substrate.Frontiers in plant science · 2014Article
- Organellar oligopeptidase (OOP) provides a complementary pathway for targeting peptide degradation in mitochondria and chloroplasts.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Modified Clp protease complex in the ClpP3 null mutant and consequences for chloroplast development and function in Arabidopsis.Plant physiology · 2013Article
- Plastid proteome assembly without Toc159: photosynthetic protein import and accumulation of N-acetylated plastid precursor proteins.The Plant cell · 2011Article
- Deletion of an organellar peptidasome PreP affects early development in Arabidopsis thaliana.Plant molecular biology · 2009Article
- Multiple sequence motifs in the rubisco small subunit transit peptide independently contribute to Toc159-dependent import of proteins into chloroplasts.Plant physiology · 2009Article
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
A stromal processing peptidase (SPP) cleaves a broad range of precursors targeted to the chloroplast, yielding proteins for numerous biosynthetic pathways in different compartments. SPP contains a signature zinc-binding motif, His-X-X-Glu-His, that places it in a metallopeptidase family which includes the mitochondrial processing peptidase. Here, we have investigated the mechanism of cleavage by SPP, a late, yet key event in the import pathway. Recombinant SPP removed the transit peptide from a variety of precursors in a single endoproteolytic step. Whereas the mature protein was immediately released, the transit peptide remained bound to SPP. SPP converted the transit peptide to a subfragment form that it no longer recognized. We conclude that SPP contains a specific binding site for the transit peptide and additional proteolysis by SPP triggers its release. A stable interaction between SPP and an intact transit peptide was directly demonstrated using a newly developed binding assay. Unlike recombinant SPP, a chloroplast extract rapidly degraded both the transit peptide and subfragment. A new degradative activity, distinguishable from SPP, was identified that is ATP- and metal-dependent. Our results indicate a regulated sequence of events as SPP functions during precursor import, and demonstrate a previously unrecognized ATP-requirement for transit peptide turnover.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.