ArticleNature communications2015
Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 28 citations in OpenAlex.
- Coordinated cpSRP43 and cpSRP54 Abundance Is Essential for Tetrapyrrole Biosynthesis While cpSRP43 Is Independent of Retrograde Signaling.Plants (Basel, Switzerland) · 2025Article
- Alkali cation-π interactions in aqueous systems, modulating supramolecular stereoisomerism of nanoscopic metal-organic capsules.Nature communications · 2024Article
- cpSRP43 Is Both Highly Flexible and Stable: Structural Insights Using a Combined Experimental and Computational Approach.Journal of chemical information and modeling · 2023Article
- Post-translational regulation of metabolic checkpoints in plant tetrapyrrole biosynthesis.Journal of experimental botany · 2022Review
- Transient local secondary structure in the intrinsically disordered C-term of the Albino3 insertase.Biophysical journal · 2021Article
- The zinc-finger protein Red1 orchestrates MTREC submodules and binds the Mtl1 helicase arch domain.Nature communications · 2021Article
- Chloroplast Ribosomes Interact With the Insertase Alb3 in the Thylakoid Membrane.Frontiers in plant science · 2021Article
- Protein Targeting Into the Thylakoid Membrane Through Different Pathways.Frontiers in physiology · 2021Review
- A Disorder-to-Order Transition Activates an ATP-Independent Membrane Protein Chaperone.Journal of molecular biology · 2020Article
- Molecular mechanism of SRP-dependent light-harvesting protein transport to the thylakoid membrane in plants.Photosynthesis research · 2018Review
- Chloroplast SRP43 acts as a chaperone for glutamyl-tRNA reductase, the rate-limiting enzyme in tetrapyrrole biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Deletion of the chloroplast LTD protein impedes LHCI import and PSI-LHCI assembly in Chlamydomonas reinhardtii.Journal of experimental botany · 2018Article
- Anionic Phospholipids and the Albino3 Translocase Activate Signal Recognition Particle-Receptor Interaction during Light-harvesting Chlorophyll a/b-binding Protein Targeting.The Journal of biological chemistry · 2017Article
- Conformational dynamics of a membrane protein chaperone enables spatially regulated substrate capture and release.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Canonical membrane protein biogenesis requires co-translational delivery of ribosome-associated proteins to the Sec translocase and depends on the signal recognition particle (SRP) and its receptor (SR). In contrast, high-throughput delivery of abundant light-harvesting chlorophyll a,b-binding proteins (LHCPs) in chloroplasts to the Alb3 insertase occurs post-translationally via a soluble transit complex including the cpSRP43/cpSRP54 heterodimer (cpSRP). Here we describe the molecular mechanisms of tethering cpSRP to the Alb3 insertase by specific interaction of cpSRP43 chromodomain 3 with a linear motif in the Alb3 C-terminal tail. Combining NMR spectroscopy, X-ray crystallography and biochemical analyses, we dissect the structural basis for selectivity of chromodomains 2 and 3 for their respective ligands cpSRP54 and Alb3, respectively. Negative cooperativity in ligand binding can be explained by dynamics in the chromodomain interface. Our study provides a model for membrane recruitment of the transit complex and may serve as a prototype for a functional gain by the tandem arrangement of chromodomains.
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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.