Chaperones and proteases - Guardians of protein integrity in eukaryotic organelles

Annals of the New York Academy of Sciences

Volumn 1113, Issue , 2007, Pages 72-86

  Leidhold, Claudia ^a   Voos, Wolfgang ^a  

^a UNIVERSITY OF FREIBURG   (Germany)

Author keywords

Chaperone; Chloroplast; Endoplasmic reticulum; Mitochondria; Protease

Indexed keywords

CARBOHYDRATE; CHAPERONE; ENDOPEPTIDASE CLP; MEMBRANE PROTEIN; PROTEINASE;

CELL ORGANELLE; CHLOROPLAST; CONFERENCE PAPER; ENDOPLASMIC RETICULUM; EUKARYOTE; HUMAN; MITOCHONDRION; NONHUMAN; PROTEIN DEGRADATION; PROTEIN QUALITY; QUALITY CONTROL; THYLAKOID MEMBRANE;

EUKARYOTA;

EID: 35548993242     PISSN: 00778923     EISSN: 17496632     Source Type: Book Series    
DOI: 10.1196/annals.1391.011     Document Type: Conference Paper

References (69)

1. PICKART, C.M. & R.E. COHEN. 2004. Proteasomes and their kin: proteases in the machine age. Nat. Rev. Mol. Cell Biol. 5: 177-187.
2. ADAM, Z. & A.K. CLARKE. 2002. Cutting edge of chloroplast proteolysis. Trends Plant Sci. 7: 451-456.
3. LANGER, T. & W. NEUPERT. 1996. Regulated protein degradation in mitochondria. Experientia 52: 1069-1076.
4. MEUSSER, B., C. HIRSCH, E. JAROSCH & T. SOMMER. 2005. ERAD: the long road to destruction. Nat. Cell Biol. 7: 766-772.
5. RÖMISCH, K. 2005. Endoplasmic reticulum-associated degradation. Annu. Rev. Cell Dev. Biol. 21: 435-456.
6. KWONG, J.Q., M.F. BEAL & G. MANFREDI. 2006. The role of mitochondria in inherited neurodegenerative diseases. J. Neurochem. 97: 1659-1675.
7. WIEDEMANN, N., A.E. FRAZIER & N. PFANNER. 2004. The protein import machinery of mitochondria. J. Biol. Chem. 279: 14473-14476.
8. GAKH, O., P. CAVADINI & G. ISAYA. 2002. Mitochondrial processing peptidases. Biochim. Biophys. Acta 1592: 63-77.
9. VOOS, W. & K. RÖTTGERS. 2002. Molecular chaperones as essential mediators of mitochondrial biogenesis. Biochim. Biophys. Acta 1592: 51-62.
10. WAGNER, I., H. ARLT, VAN DYCK, L., et al. 1994. Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J. 13: 5135-5145.
11. MOGK, A., T. TOMOYASU, P. GOLOUBINOFF, et al. 1999. Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. EMBO J. 18: 6934-6949.
12. LEIDHOLD, C., B.V. JANOWSKY, D. BECKER, et al. 2006. Structure and function of Hsp78, the mitochondrial ClpB homolog. J. Struct. Biol. 156: 149-164.
13. SCHMITT, M., W. NEUPERT & T. LANGER. 1996. The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria. J. Cell Biol. 134: 1375-1386.
14. VON JANOWSKY, B., T. MAJOR, K. KNAPP & W. VOOS. 2006. The disaggregation activity of the mitochondrial ClpB homolog Hsp78 maintains Hsp70 function during heat stress. J. Mol. Biol. 357: 793-807.
15. VAN DYCK, L., M. DEMBOWSKI, W. NEUPERT & T. LANGER. 1998. Mcx1p, a ClpX homologue in mitochondria of Saccharomyces cerevisiae. FEBS Lett. 438: 250-254.
16. RÖTTGERS, K., N. ZUFALL, B. GUIARD & W. VOOS. 2002. The ClpB homolog Hsp78 is required for the efficient degradation of proteins in the mitochondrial matrix. J. Biol. Chem. 277: 45829-45837.
17. VAN DYCK, L., D.A. PEARCE & F. SHERMAN. 1994. PIM1 encodes a mitochondrial ATP-dependent protease that is required for mitochondrial function in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 269: 238-242.
18. WANG, N., S. GOTTESMAN, M.C. WILLINGHAM, et al. 1993. A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease. Proc. Natl. Acad. Sci. USA 90: 11247-11251.
19. REP, M., J.M. VAN DIJL, K. SUDA, et al. 1996. Promotion of mitochondrial membrane complex assembly by a proteolytically inactive yeast Lon. Science 274: 103-106.
20. LIU, T., B. LU, I. LEE, et al. 2004. DNA and RNA binding by the mitochondrial Lon protease is regulated by nucleotide and protein substrate. J. Biol. Chem. 279: 13902-13910.
21. BOTA, D.A. & K.J. DAVIES. 2002. Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. Nat. Cell Biol. 4: 674-680.
22. VON JANOWSKY, B., K. KNAPP, T. MAJOR, et al. 2005. Structural properties of substrate proteins determine their proteolysis by the mitochondrial AAA+ protease Pim1. Biol. Chem. 386: 1307-1317.
23. LU, B., T. LIU, J.A. CROSBY, et al. 2003. The ATP-dependent Lon protease of Mus musculus is a DNA-binding protein that is functionally conserved between yeast and mammals. Gene 306: 45-55.
24. BOTA, D.A., J.K. NGO & K.J. DAVIES. 2005. Downregulation of the human Lon protease impairs mitochondrial structure and function and causes cell death. Free Radic. Biol. Med. 38: 665-677.
25. MAJOR, T., B. VON JANOWSKY, T. RUPPERT, et al. 2006. Proteomic analysis of mitochondrial protein turnover: identification of novel substrate proteins of the matrix protease Pim1. Mol. Cell Biol. 26: 762-776.
26. SAUER, R.T., D.N. BOLON, B.M. BURTON, et al. 2004. Sculpting the proteome with AAA(+) proteases and disassembly machines. Cell 119: 9-18.
27. ZHAO, Q., J. WANG, I.V. LEVICHKIN, et al. 2002. A mitochondrial specific stress response in mammalian cells. EMBO J. 21: 4411-4419.
28. LEONHARD, K., J.M. HERRMANN, R.A. STUART, et al. 1996. AAA proteases with catalytic sites on opposite membrane surfaces comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria. EMBO J. 15: 4218-4229.
29. GRAEF, M. & T. LANGER. 2006. Substrate specific consequences of central pore mutations in the i-AAA protease Yme1 on substrate engagement. J. Struct. Biol. 156: 101-108.
30. BIENIOSSEK, C., T. SCHALCH, M. BUMANN, et al. 2006. The molecular architecture of the metalloprotease FtsH. Proc. Natl. Acad. Sci. USA 103: 3066-3071.
31. ITO, K. & Y. AKIYAMA. 2005. Cellular functions, mechanism of action, and regulation of FtsH protease. Annu. Rev. Microbiol. 59: 211-231.
32. NOLDEN, M., S. EHSES, M. KOPPEN, et al. 2005. The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria. Cell 123: 277-289.
33. TATSUTA, T., S. AUGUSTIN, M. NOLDEN, et al. 2007. m-AAA protease-driven membrane dislocation allows intramembrane cleavage by rhomboid in mitochondria. EMBO J. 26: 325-335.
34. JEYARAJU, D.V., L. XU, M.C. LETELLIER, et al. 2006. Phosphorylation and cleavage of presenilin-associated rhomboid-like protein (PARL) promotes changes in mitochondrial morphology. Proc. Natl. Acad. Sci. USA 103: 18562-18567.
35. KÄSER, M., M. KAMBACHELD, B. KISTERS- WOIKE & T. LANGER. 2003. Oma1, a novel membrane-bound metallopeptidase in mitochondria with activities overlapping with the m-AAA protease. J. Biol. Chem. 278: 46414-46423.
36. FALKEVALL, A., N. ALIKHANI, S. BHUSHAN, et al. 2006. Degradation of the amyloid beta-protein by the novel mitochondrial peptidasome, PreP. J. Biol. Chem. 281: 29096-29104.
37. KAMBACHELD, M., S. AUGUSTIN, T. TATSUTA, et al. 2005. Role of the novel metallopeptidase Mop112 and saccharolysin for the complete degradation of proteins residing in different subcompartments of mitochondria. J. Biol. Chem. 280: 20132-20139.
38. IGAKI, T., Y. SUZUKI, N. TOKUSHIGE, et al. 2007. Evolution of mitochondrial cell death pathway: proapoptotic role of HtrA2/Omi in Drosophila. Biochem. Biophys. Res. Commun. 356: 993-997.
39. BOSTON, R.S., P.V. VIITANEN & E. VIERLING. 1996. Molecular chaperones and protein folding in plants. Plant Mol. Biol. 32: 191-222.
40. SOLL, J. & E. SCHLEIFF. 2004. Protein import into chloroplasts. Nat. Rev. Mol. Cell Biol. 5: 198-208.
41. SCHRODA, M., J. KROPAT, U. OSTER, et al. 2001. Possible role for molecular chaperones in assembly and repair of photosystem II. Biochem. Soc. Trans. 29: 413-418.
42. LEE, C., S. PRAKASH & A. MATOUSCHEK. 2002. Concurrent translocation of multiple polypeptide chains through the proteasomal degradation channel. J. Biol. Chem. 277: 34760-34765.
43. ADAM, Z., A. RUDELLA & K.J. VAN WIJK. 2006. Recent advances in the study of Clp, FtsH and other proteases located in chloroplasts. Curr. Opin. Plant Biol. 9: 234-240.
44. ADAM, Z., I. ADAMSKA, K. NAKABAYASHI, et al. 2001. Chloroplast and mitochondrial proteases in Arabidopsis. A proposed nomenclature. Plant Physiol. 125: 1912-1918.
45. YU, F., S. PARK & S.R. RODERMEL. 2004. The Arabidopsis FtsH metalloprotease gene family: interchangeability of subunits in chloroplast oligomeric complexes. Plant J. 37: 864-876.
46. ZALTSMAN, A., N. ORI & Z. ADAM. 2005. Two types of FtsH protease subunits are required for chloroplast biogenesis and Photosystem II repair in Arabidopsis. Plant Cell 17: 2782-2790.
47. CLAUSEN, T., C. SOUTHAN & M. EHRMANN. 2002. The HtrA family of proteases: implications for protein composition and cell fate. Mol. Cell 10: 443-455.
48. LINDAHL, M., C. SPETEA, T. HUNDAL, et al. 2000. The thylakoid FtsH protease plays a role in the light-induced turnover of the photosystem II D1 protein. Plant Cell 12: 419-431.
49. HAUSSUHL, K., B. ANDERSSON & I. ADAMSKA. 2001. A chloroplast DegP2 protease performs the primary cleavage of the photodamaged D1 protein in plant photosystem II. EMBO J. 20: 713-722.
50. CHASSIN, Y., E. KAPRI-PARDES, G. SINVANY, et al. 2002. Expression and characterization of the thylakoid lumen protease DegP1 from Arabidopsis. Plant Physiol. 130: 857-864.
51. ZHENG, B., T. HALPERIN, O. HRUSKOVA- HEIDINGSFELDOVA, et al. 2002. Characterization of chloroplast Clp proteins in Arabidopsis: localization, tissue specificity and stress responses. Physiol. Plant 114: 92-101.
52. PELTIER, J.B., D.R. RIPOLL, G. FRISO, et al. 2004. Clp protease complexes from photosynthetic and non-photosynthetic plastids and mitochondria of plants, their predicted three-dimensional structures, and functional implications. J. Biol. Chem. 279: 4768-4781.
53. ZHENG, B., T.M. MACDONALD, S. SUTINEN, et al. 2006. A nuclear-encoded ClpP subunit of the chloroplast ATP-dependent Clp protease is essential for early development in Arabidopsis thaliana. Planta 224: 1103-1115.
54. SJÖGREN, L.L., T.M. STANNE, B. ZHENG, et al. 2006. Structural and functional insights into the chloroplast ATP-dependent Clp protease in Arabidopsis. Plant Cell 18: 2635-2649.
55. OSBORNE, A.R., T.A. RAPOPORT & B. VAN DEN BERG. 2005. Protein translocation by the Sec61/SecY channel. Annu. Rev. Cell Dev. Biol. 21: 529-550.
56. ZHANG, Y., G. NIJBROEK, M.L. SULLIVAN, et al. 2001. Hsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeast. Mol. Biol. Cell 12: 1303-1314.
57. KLEIZEN, B. & I. BRAAKMAN. 2004. Protein folding and quality control in the endoplasmic reticulum. Curr. Opin. Cell Biol. 16: 343-349.
58. PLEMPER, R.K., S. BÖHMLER, J. BORDALLO, et al. 1997. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 388: 891-895.
59. MOLINARI, M., C. GALLI, O. VANONI, et al. 2005. Persistent glycoprotein misfolding activates the glucosidase II/UGT1-driven calnexin cycle to delay aggregation and loss of folding competence. Mol. Cell 20: 503-512.
60. MOLINARI, M., V. CALANCA, C. GALLI, et al. 2003. Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle. Science 299: 1397-1400.
61. KALIES, K.U., S. ALLAN, T. SERGEYENKO, et al. 2005. The protein translocation channel binds proteasomes to the endoplasmic reticulum membrane. EMBO J. 24: 2284-2293.
62. YE, Y., Y. SHIBATA, C. YUN, et al. 2004. A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature 429: 841-847.
63. YE, Y., H.H. MEYER & T.A. RAPOPORT. 2001. The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 414: 652-656.
64. JAROSCH, E., C. TAXIS, C. VOLKWEIN, et al. 2002. Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nat. Cell Biol. 4: 134-139.
65. NEUBER, O., E. JAROSCH, C. VOLKWEIN, et al. 2005. Ubx2 links the Cdc48 complex to ER-associated protein degradation. Nat. Cell Biol. 7: 993-998.
66. GAUSS, R., T. SOMMER & E. JAROSCH. 2006. The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitment. EMBO J. 25: 1827-1835.
67. CARVALHO, P., V. GODER & T.A. RAPOPORT. 2006. Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins. Cell 126: 3613-3673.
68. DENIC, V., E.M. QUAN & J.S. WEISSMAN. 2006. A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation. Cell 126: 349-359.
69. GAUSS, R., E. JAROSCH, T. SOMMER & C. HIRSCH. 2006. A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery. Nat. Cell Biol. 8: 849-854.