ArticleThe Journal of biological chemistry2011
Interaction studies between the chloroplast signal recognition particle subunit cpSRP43 and the full-length translocase Alb3 reveal a membrane-embedded binding region in Alb3 protein.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Switchable client specificity in a dual functional chaperone coordinates light-harvesting complex biogenesis.Science advances · 2025Article
- GET3B is involved in chloroplast biogenesis and interacts with the thylakoidal ALB3 and ALB4 insertases.Plant cell reports · 2025Article
- Targeting signals required for protein sorting to sub-chloroplast compartments.Plant cell reports · 2024Review
- The role of chloroplast SRP54 domains and its C-terminal tail region in post- and co-translational protein transport in vivo.Journal of experimental botany · 2024Article
- OsALB3 Is Required for Chloroplast Development by Promoting the Accumulation of Light-Harvesting Chlorophyll-Binding Proteins in Rice.Plants (Basel, Switzerland) · 2023Article
- Chloroplast SRP43 autonomously protects chlorophyll biosynthesis proteins against heat shock.Nature plants · 2021Article
- Chloroplast Ribosomes Interact With the Insertase Alb3 in the Thylakoid Membrane.Frontiers in plant science · 2021Article
- A Disorder-to-Order Transition Activates an ATP-Independent Membrane Protein Chaperone.Journal of molecular biology · 2020Article
- Posttranslational insertion of small membrane proteins by the bacterial signal recognition particle.PLoS biology · 2020Article
- Loss of ALBINO3b Insertase Results in Truncated Light-Harvesting Antenna in Diatoms.Plant physiology · 2019Article
- Molecular mechanism of SRP-dependent light-harvesting protein transport to the thylakoid membrane in plants.Photosynthesis research · 2018Review
- The rice white green leaf 2 gene causes defects in chloroplast development and affects the plastid ribosomal protein S9.Rice (New York, N.Y.) · 2018Article
- Two distinct sites of client protein interaction with the chaperone cpSRP43.The Journal of biological chemistry · 2018Article
- 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
- Suppressors of the Chloroplast Protein Import MutantThe Plant cell · 2017Article
- 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
- Functional Update of the Auxiliary Proteins PsbW, PsbY, HCF136, PsbN, TerC and ALB3 in Maintenance and Assembly of PSII.Frontiers in plant science · 2016Review
- Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction.Nature communications · 2015Article
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4 authors.
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Abstract
Posttranslational targeting of the light-harvesting chlorophyll a,b-binding proteins depends on the function of the chloroplast signal recognition particle, its receptor cpFtsY, and the translocase Alb3. The thylakoid membrane protein Alb3 of Arabidopsis chloroplasts belongs to the evolutionarily conserved YidC/Oxa1/Alb3 protein family; the members of this family facilitate the insertion, folding, and assembly of membrane proteins in bacteria, mitochondria, and chloroplasts. Here, we analyzed the interaction sites of full-length Alb3 with the cpSRP pathway component cpSRP43 by using in vitro and in vivo studies. Bimolecular fluorescence complementation and Alb3 proteoliposome studies showed that the interaction of cpSRP43 is dependent on a binding domain in the C terminus of Alb3 as well as an additional membrane-embedded binding site in the fifth transmembrane domain (TMD5) of Alb3. The C-terminal binding domain was mapped to residues 374-388, and the binding domain within TMD5 was mapped to residues 314-318 located close to the luminal end of TMD5. A direct binding between cpSRP43 and these binding motifs was shown by pepspot analysis. Further studies using blue-native gel electrophoresis revealed that full-length Alb3 is able to form dimers. This finding and the identification of a membrane-embedded cpSRP43 binding site in Alb3 support a model in which cpSRP43 inserts into a dimeric Alb3 translocation pore during cpSRP-dependent delivery of light-harvesting chlorophyll a,b-binding proteins.
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