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2018 | 87 | 1 |

Tytuł artykułu

The contribution of individual domains of chloroplast protein AtDeg2 to its chaperone and proteolytic activities

Treść / Zawartość

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
The thylakoid protease AtDeg2 is a non-ATP hydrolyzing chloroplast protease/ chaperone peripherally connected with stromal side of thylakoid membrane. Its linear structure consists of protease domain and two PDZ domains. To unveil the significance of individual domains, chaperone and proteolytic activities of AtDeg2, its mutated recombinant versions have been developed and their ability to suppress protein aggregation and resolubilization of protein aggregates as well as the ability to degrade substrate protein was examined in vitro. Our work reveals for the first time that AtDeg2 is able not only to suppress aggregation of denatured proteins, but to resolubilize existing protein aggregates as well. We show that PDZ2 domain contributes significantly to both chaperone and protease activities of AtDeg2, whereas PDZ1 is required for chaperone but superfluous for proteolytic activity. Protease domain – but not S-268 in its catalytic site – contributes to chaperone activities of AtDeg2. These results show an entirely new function of AtDeg2 chaperone/protease (i.e., disaggregation of protein aggregates) and allow to identify structural motifs required for “old” and new functions of AtDeg2.

Słowa kluczowe

Wydawca

-

Rocznik

Tom

87

Numer

1

Opis fizyczny

Article 3570 [9p.],fig.,ref.

Twórcy

autor
  • Department of Plant Physiology, Institute of Experimental Biology, Faculty of Biology, Adam Mickiewicz University in Poznan, Umultowska 89, 61-614 Poznan, Poland
autor
  • Department of Plant Physiology, Institute of Experimental Biology, Faculty of Biology, Adam Mickiewicz University in Poznan, Umultowska 89, 61-614 Poznan, Poland
autor
  • Department of Plant Physiology, Institute of Experimental Biology, Faculty of Biology, Adam Mickiewicz University in Poznan, Umultowska 89, 61-614 Poznan, Poland
autor
  • Department of Plant Physiology, Institute of Experimental Biology, Faculty of Biology, Adam Mickiewicz University in Poznan, Umultowska 89, 61-614 Poznan, Poland

Bibliografia

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  • 4. Schuhmann H, Huesgen P, Adamska I. The family of Deg/Htr proteases in plants. BMC Plant Biol. 2012;12:52. https://doi.org/10.1186/1471-2229-12-52
  • 5. Haussühl K, Andersson B, Adamska I. A chloroplast DegP2 protease performs the primary cleavage of the photodamaged D1 protein in plant photosystem II. EMBO J. 2001;20(4):713–722. https://doi.org/10.1093/emboj/20.4.713
  • 6. Chassin Y, Kapri-Pardes E, Sinvany G, Arad T, Adam Z. Expression and characterization of the thylakoid lumen protease DegP1 from Arabidopsis. Plant Physiol. 2002;130(2):857–864. https://doi.org/10.1104/pp.007922
  • 7. Schubert M, Petersson UA, Haas BJ, Funk C, Schröder WP, Kieselbach T. Proteome map of the chloroplast lumen of Arabidopsis thaliana. J Biol Chem. 2002;277(10):8354–8365. https://doi.org/10.1074/jbc.M108575200
  • 8. Tanz SK, Castleden I, Hooper CM, Small I, Millar AH. Using the SUBcellular database for Arabidopsis proteins to localize the Deg protease family. Front Plant Sci. 2014;5:396. https://doi.org/10.3389/fpls.2014.00396
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  • 11. Sun R, Fan H, Gao F, Lin Y, Zhang L, Gong W, et al. Crystal structure of Arabidopsis Deg2 protein reveals an internal PDZ ligand locking the hexameric resting state. J Biol Chem. 2012;287(44):37564–37569. https://doi.org/10.1074/jbc.M112.394585
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  • 13. Kapri-Pardes E, Naveh L, Adam Z. The thylakoid lumen protease Deg1 is involved in the repair of photosystem II from photoinhibition in Arabidopsis. Plant Cell. 2007;19(3):1039–1047. https://doi.org/10.1105/tpc.106.046573
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  • 17. Luciński R, Misztal L, Samardakiewicz S, Jackowski G. Involvement of Deg5 proteasae in wounding-related disposal of PsbF apoprotein. Plant Physiol Biochem. 2011;4(3):311– 320. https://doi.org/10.1016/j/plaphy.2011.01.001
  • 18. Baranek M, Wyka T, Jackowski G. Downregulation of chloroplast protease AtDeg5 leads to changes in chronological progression of ontogenetic stages, leaf morphology and chloroplast ultrastructure in Arabidopsis. Acta Soc Bot Pol. 2015;84(1):59–70. https://doi.org/10.5586/asbp.2015.001
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  • 21. Sun X, Ouyang M, Guo J, Ma J, Lu C, Adam Z, et al. The thylakoid protease Deg1 is involved in photosystem-II assembly in Arabidopsis thaliana. Plant J. 2010;62(2):240– 249. https://doi.org/10.1111/j.1365-313X.2010.04140.x
  • 22. Moore M, Goforth RL, Mori H, Henry R. Functional interaction of chloroplast SRP/ FtsY with the ALB3 translocase in thylakoids: substrate not required. J Cell Biol. 2003;162(7):1245–1254. https://doi.org/10.1083/jcb.200307067
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  • 24. Jaru-Ampornpan P, Shen K, Lam VQ, Ali M, Doniach S, Jia TZ, et al. ATP-independent reversal of a membrane protein aggregate by a chloroplast SRP subunit. Nat Struct Mol Biol. 2010;17(6):696–702. https://doi.org/10.1038/nsmb.1836
  • 25. Nguyen TX, Jaru-Ampornpan P, Lam VQ, Cao P, Piszkiewicz S, Hess S, et al. Mechanism of an ATP-independent protein disaggregase: I. Structure of a membrane protein aggregate reveals a mechanism of recognition by its chaperone. J Biol Chem. 2013;288(19):13420–13430. https://doi.org/10.1074/jbc.M113.462812
  • 26. Spiess C, Beil A, Ehrmann M. A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell. 2004;97(3):339–347. https://doi.org/10.1016/S0092-8674(00)80743-6
  • 27. Jiang J, Zhang X, Chen Y, Wu Y, Zhou ZH, Chang Z, et al. Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins. Proc Natl Acad Sci USA. 2008;105(33):11939–11944. https://doi.org/10.1073/pnas.0805464105

Typ dokumentu

Bibliografia

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