A Disorder-to-Order Transition Activates an ATP-Independent Membrane Protein Chaperone

Siegel, Alex; McAvoy, Camille Z.; Lam, Vinh; Liang, Fu‐Cheng; Kroon, Gerard; Miaou, Emily; Griffin, Patrick R.; Wright, Peter E.; Shan, Shu‐ou

doi:10.1016/j.jmb.2020.11.007

Cited by 9 publications

(10 citation statements)

References 76 publications

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“…4b-4e). Unexpectedly, although cpSRP43-SBD exhibits slightly higher chaperone activity on LHCP than full-length, mature cpSRP43 (cpSRP43-FL) does 27,28 , its chaperone activity towards GluTR, CHLH and GUN4 was more than 20-fold lower than that of cpSRP43-FL (Fig. 4b-4e).…”

Section: Cpsrp43 Protects Mature Tbs Proteins From Heat-induced Aggre...mentioning

confidence: 92%

“…Two C-terminal chromodomains, CD2 and CD3, mediate interactions with cpSRP54 and Alb3, respectively [35][36][37] . Previous biophysical work showed that the SBD, CD2, or CD3 domains fold independently, and deletion of one does not lead to unfolding of the other domains 27,28,40 . We examined the structural requirements for cpSRP43's chaperone activity towards TBS proteins.…”

Section: Cpsrp43 Protects Mature Tbs Proteins From Heat-induced Aggre...mentioning

confidence: 99%

“…The chaperone activity of cpSRP43 on LHCPs is stimulated by cpSRP54-dependent allosteric regulation 27,28 . The RRKRp10 segment of the cpSRP54M domain (designated cpSRP54M peptide) binds to CD2 and triggers a conformational change in cpSRP43-SBD, thereby enhancing its chaperone activity towards LHCP by 6-fold and restoring the activity of multiple chaperone-defective mutants (Supplementary Fig.…”

Section: Cpsrp54 Inhibits the Chaperone Activity Of Cpsrp43 Towards T...mentioning

confidence: 99%

“…The RRKRp10 segment of the cpSRP54M domain (designated cpSRP54M peptide) binds to CD2 and triggers a conformational change in cpSRP43-SBD, thereby enhancing its chaperone activity towards LHCP by 6-fold and restoring the activity of multiple chaperone-defective mutants (Supplementary Fig. 7) 27,28 . Surprisingly, the cpSRP54M peptide substantially diminished the efficacy of cpSRP43 in preventing heatinduced aggregation of GluTR, CHLH and GUN4 in vitro (Fig.…”

Section: Cpsrp54 Inhibits the Chaperone Activity Of Cpsrp43 Towards T...mentioning

confidence: 99%

“…LHCPs imported into the stroma of chloroplasts are kept soluble by forming a 'transit complex' with the cpSRP, which itself consists of the subunits cpSRP43 and cpSRP54 24,25 . cpSRP43 is an ATP-independent chaperone that is responsible for protecting LHCPs from aggregation 26 , while cpSRP54 serves to allosterically activates its LHCP-targeted chaperone activity 27,28 . cpSRP54 also mediates interaction of the cpSRP complex with the SRP receptor cpFtsY to deliver LHCPs to the translocase Albino 3 (Alb3) at the thylakoid membrane 29,30 .…”

Section: Introductionmentioning

confidence: 99%

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Chloroplast SRP43 autonomously protects chlorophyll biosynthesis proteins against heat shock

Siegel

Shan

et al. 2021

Nat. Plants

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The assembly of light-harvesting chlorophyll-binding proteins (LHCPs) is coordinated with chlorophyll biosynthesis during chloroplast development. The ATP-independent chaperone known as chloroplast signal recognition particle 43 (cpSRP43) mediates post-translational LHCP targeting to the thylakoid membrane, and also participates in tetrapyrrole biosynthesis (TBS). How these distinct actions of cpSRP43 are controlled has remained unclear. Here, we demonstrate that cpSRP43 effectively protects several TBS proteins from heat-induced aggregation and enhances their stability during leaf greening and heat shock. While the substrate-binding domain (SBD) of cpSRP43 is sufficient for chaperoning LHCPs, stabilization of TBS clients requires the chromodomain 2 of the protein. Strikingly, cpSRP54 -which activates cpSRP43's LHCP-targeted function -inhibits the chaperone activity of cpSRP43 towards TBS proteins. High temperature weakens the interaction of cpSRP54 with cpSRP43, thus freeing cpSRP43 to interact with and protect the integrity of TBS proteins. Our data indicate that the temperature-sensitivity of the cpSRP43-cpSRP54 complex enables cpSRP43 to serve as an autonomous chaperone for thermoprotection of TBS proteins.

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Section: Cpsrp43 Protects Mature Tbs Proteins From Heat-induced Aggre...mentioning

confidence: 92%

Section: Cpsrp43 Protects Mature Tbs Proteins From Heat-induced Aggre...mentioning

confidence: 99%

Section: Cpsrp54 Inhibits the Chaperone Activity Of Cpsrp43 Towards T...mentioning

confidence: 99%

Section: Cpsrp54 Inhibits the Chaperone Activity Of Cpsrp43 Towards T...mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Chloroplast SRP43 autonomously protects chlorophyll biosynthesis proteins against heat shock

Siegel

Shan

et al. 2021

Nat. Plants

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Intrinsic disorder and allosteric regulation

Huang

Chen

Lai

et al. 2023

Structure and Intrinsic Disorder in Enzymology

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Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems

et al. 2021

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Solution-phase hydrogen/deuterium exchange (HDX) coupled to mass spectrometry (MS) is a widespread tool for structural analysis across academia and the biopharmaceutical industry. By monitoring the exchangeability of backbone amide protons, HDX-MS can reveal information about higher-order structure and dynamics throughout a protein, can track protein folding pathways, map interaction sites, and assess conformational states of protein samples. The combination of the versatility of the hydrogen/deuterium exchange reaction with the sensitivity of mass spectrometry has enabled the study of extremely challenging protein systems, some of which cannot be suitably studied using other techniques. Improvements over the past three decades have continually increased throughput, robustness, and expanded the limits of what is feasible for HDX-MS investigations. To provide an overview for researchers seeking to utilize and derive the most from HDX-MS for protein structural analysis, we summarize the fundamental principles, basic methodology, strengths and weaknesses, and the established applications of HDX-MS while highlighting new developments and applications.

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A Disorder-to-Order Transition Activates an ATP-Independent Membrane Protein Chaperone

Cited by 9 publications

References 76 publications

Chloroplast SRP43 autonomously protects chlorophyll biosynthesis proteins against heat shock

Chloroplast SRP43 autonomously protects chlorophyll biosynthesis proteins against heat shock

Intrinsic disorder and allosteric regulation

Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems

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