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- Publisher Website: 10.1073/pnas.1719645115
- Scopus: eid_2-s2.0-85045098081
- PMID: 29581280
- WOS: WOS:000429540300030
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Article: Chloroplast SRP43 acts as a chaperone for glutamyl-tRNA reductase, the rate-limiting enzyme in tetrapyrrole biosynthesis
Title | Chloroplast SRP43 acts as a chaperone for glutamyl-tRNA reductase, the rate-limiting enzyme in tetrapyrrole biosynthesis |
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Authors | |
Keywords | 5-aminolevulinic acid Chaperone Chloroplast biogenesis Chloroplast signal recognition particle Tetrapyrrole biosynthesis |
Issue Date | 2018 |
Citation | Proceedings of the National Academy of Sciences of the United States of America, 2018, v. 115, n. 15, p. E3588-E3596 How to Cite? |
Abstract | Assembly of light-harvesting complexes requires synchronization of chlorophyll (Chl) biosynthesis with biogenesis of light-harvesting Chl a/b-binding proteins (LHCPs). The chloroplast signal recognition particle (cpSRP) pathway is responsible for transport of nucleus-encoded LHCPs in the stroma of the plastid and their integration into the thylakoid membranes. Correct folding and assembly of LHCPs require the incorporation of Chls, whose biosynthesis must therefore be precisely coordinated with membrane insertion of LHCPs. How the spatiotemporal coordination between the cpSRP machinery and Chl biosynthesis is achieved is poorly understood. In this work, we demonstrate a direct interaction between cpSRP43, the chaperone that mediates LHCP targeting and insertion, and glutamyl-tRNA reductase (GluTR), a rate-limiting enzyme in tetrapyrrole biosynthesis. Concurrent deficiency for cpSRP43 and the GluTR-binding protein (GBP) additively reduces GluTR levels, indicating that cpSRP43 and GBP act nonredundantly to stabilize GluTR. The substrate-binding domain of cpSRP43 binds to the N-terminal region of GluTR, which harbors aggregation-prone motifs, and the chaperone activity of cpSRP43 efficiently prevents aggregation of these regions. Our work thus reveals a function of cpSRP43 in Chl biosynthesis and suggests a striking mechanism for posttranslational coordination of LHCP insertion with Chl biosynthesis. |
Persistent Identifier | http://hdl.handle.net/10722/316493 |
ISSN | 2023 Impact Factor: 9.4 2023 SCImago Journal Rankings: 3.737 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Wang, Peng | - |
dc.contributor.author | Liang, Fu Cheng | - |
dc.contributor.author | Wittmann, Daniel | - |
dc.contributor.author | Siegel, Alex | - |
dc.contributor.author | Shan, Shu Ou | - |
dc.contributor.author | Grimm, Bernhard | - |
dc.date.accessioned | 2022-09-14T11:40:35Z | - |
dc.date.available | 2022-09-14T11:40:35Z | - |
dc.date.issued | 2018 | - |
dc.identifier.citation | Proceedings of the National Academy of Sciences of the United States of America, 2018, v. 115, n. 15, p. E3588-E3596 | - |
dc.identifier.issn | 0027-8424 | - |
dc.identifier.uri | http://hdl.handle.net/10722/316493 | - |
dc.description.abstract | Assembly of light-harvesting complexes requires synchronization of chlorophyll (Chl) biosynthesis with biogenesis of light-harvesting Chl a/b-binding proteins (LHCPs). The chloroplast signal recognition particle (cpSRP) pathway is responsible for transport of nucleus-encoded LHCPs in the stroma of the plastid and their integration into the thylakoid membranes. Correct folding and assembly of LHCPs require the incorporation of Chls, whose biosynthesis must therefore be precisely coordinated with membrane insertion of LHCPs. How the spatiotemporal coordination between the cpSRP machinery and Chl biosynthesis is achieved is poorly understood. In this work, we demonstrate a direct interaction between cpSRP43, the chaperone that mediates LHCP targeting and insertion, and glutamyl-tRNA reductase (GluTR), a rate-limiting enzyme in tetrapyrrole biosynthesis. Concurrent deficiency for cpSRP43 and the GluTR-binding protein (GBP) additively reduces GluTR levels, indicating that cpSRP43 and GBP act nonredundantly to stabilize GluTR. The substrate-binding domain of cpSRP43 binds to the N-terminal region of GluTR, which harbors aggregation-prone motifs, and the chaperone activity of cpSRP43 efficiently prevents aggregation of these regions. Our work thus reveals a function of cpSRP43 in Chl biosynthesis and suggests a striking mechanism for posttranslational coordination of LHCP insertion with Chl biosynthesis. | - |
dc.language | eng | - |
dc.relation.ispartof | Proceedings of the National Academy of Sciences of the United States of America | - |
dc.subject | 5-aminolevulinic acid | - |
dc.subject | Chaperone | - |
dc.subject | Chloroplast biogenesis | - |
dc.subject | Chloroplast signal recognition particle | - |
dc.subject | Tetrapyrrole biosynthesis | - |
dc.title | Chloroplast SRP43 acts as a chaperone for glutamyl-tRNA reductase, the rate-limiting enzyme in tetrapyrrole biosynthesis | - |
dc.type | Article | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1073/pnas.1719645115 | - |
dc.identifier.pmid | 29581280 | - |
dc.identifier.scopus | eid_2-s2.0-85045098081 | - |
dc.identifier.volume | 115 | - |
dc.identifier.issue | 15 | - |
dc.identifier.spage | E3588 | - |
dc.identifier.epage | E3596 | - |
dc.identifier.eissn | 1091-6490 | - |
dc.identifier.isi | WOS:000429540300030 | - |