Processing of the dual targeted precursor protein of glutathione reductase in mitochondria and chloroplasts

Journal of Molecular Biology

Volumn 343, Issue 3, 2004, Pages 639-647

  Rudhe, Charlotta ^a   Clifton, Rachel ^b   Chew, Orinda ^b   Zemam, Kenza ^a   Richter, Stefan ^c   Lamppa, Gayle ^c   Whelan, James ^b   Glaser, Elzbieta ^a  

^a STOCKHOLM UNIVERSITY   (Sweden)

^b UNIVERSITY OF WESTERN AUSTRALIA   (Australia)

^c UNIVERSITY OF CHICAGO   (United States)

Author keywords

dual targeting; mitochondrial processing peptidase; processing; stromal processing peptidase; targeting signal

Indexed keywords

AMINO ACID; GLUTATHIONE REDUCTASE; MITOCHONDRIAL PROCESSING PEPTIDASE; PEPTIDASE; PROTEIN PRECURSOR; STROMAL PROCESSING PEPTIDASE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CHLOROPLAST; ENZYME ACTIVATION; ENZYME INHIBITION; EXAMINATION; GENE CONSTRUCT; GENE DELETION; GENE MUTATION; GENE SEQUENCE; INFORMATION; MITOCHONDRION; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN TARGETING; SENSITIVITY ANALYSIS; SIGNAL TRANSDUCTION;

PISUM SATIVUM;

EID: 4744359136     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.08.053     Document Type: Article

References (47)

1. W. Neupert Protein import into mitochondria Annu. Rev. Biochem. 66 1997 863 917
2. G. Schatz, and B. Dobberstein Common principles of protein translocation across membranes Science 271 1996 1519 1526
3. K. Keegstra, and K. Cline Protein import and routing systems of chloroplasts Plant Cell 11 1999 557 570
4. J. Soll, and R. Tien Protein translocation into and acorss the chloroplastic envelope membranes Plant Mol. Biol. 38 1998 191 207
5. H.P. Braun, M. Emmermann, V. Kruft, and U.K. Schmitz The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain EMBO J. 11 1992 3219 3227
6. A.C. Eriksson, and E. Glaser Mitochondrial processing proteinase: a general processing proteinase of spinach leaf mitochondria is a membrane-bound enzyme Biochim. Biophys. Acta 1140 1992 208 214
7. M. Arretz, H. Schneider, B. Guiard, M. Brunner, and W. Neupert Characterization of the mitochondrial processing peptidase of Neurospora crassa J. Biol. Chem. 269 1994 4959 4967
8. G. Hawlitschek, H. Schneider, B. Schmidt, M. Tropschug, F.U. Hartl, and W. Neupert Mitochondrial protein import: identification of processing peptidase and of PEP, a processing enhancing protein Cell 53 1988 795 806
9. S. Richter, and G. Lamppa A chloroplast processing enzyme functions as the general stromal processing peptidase Proc. Natl Acad. Sci. USA 95 1998 7463 7468
10. X.P. Zhang, S. Sjoling, M. Tanudji, L. Somogyi, D. Andreu, and L.E. Eriksson Mutagenesis and computer modelling approach to study determinants for recognition of signal peptides by the mitochondrial processing peptidase Plant J. 27 2001 427 438
11. M. Tanudji, S. Sjoling, E. Glaser, and J. Whelan Signals required for the import and processing of the alternative oxidase into mitochondria J. Biol. Chem. 274 1999 1286 1293
12. G. Duby, H. Degand, and M. Boutry Structure requirement and identification of a cryptic cleavage site in the mitochondrial processing of a plant F1-ATPase beta-subunit presequence FEBS Letters 505 2001 409 413
13. P. Moberg, S. Nilsson, A. Stahl, A.C. Eriksson, E. Glaser, and L. Maler NMR solution structure of the mitochondrial F1beta presequence from Nicotiana plumbaginifolia J. Mol. Biol. 336 2004 1129 1140
14. G. von Heijne Mitochondrial targeting sequences may form amphiphilic helices EMBO J. 5 1986 1335 1342
15. Y. Abe, T. Shodai, T. Muto, K. Mihara, H. Torii, and S. Nishikawa Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20 Cell 100 2000 551 560
16. P.K. Hammen, D.G. Gorenstein, and H. Weiner Structure of the signal sequences for two mitochondrial matrix proteins that are not proteolytically processed upon import Biochemistry 33 1994 8610 8617
17. P.K. Hammen, M. Waltner, B. Hahnemann, T.S. Heard, and H. Weiner The role of positive charges and structural segments in the presequence of rat liver aldehyde dehydrogenase in import into mitochondria J. Biol. Chem. 271 1996 21041 21048
18. C. Karslake, M.E. Piotto, Y.K. Pak, H. Weiner, and D.G. Gorenstein 2D NMR and structural model for a mitochondrial signal peptide bound to a micelle Biochemistry 29 1990 9872 9878
19. K. Thornton, Y. Wang, H. Weiner, and D.G. Gorenstein Import, processing, and two-dimensional NMR structure of a linker-deleted signal peptide of rat liver mitochondrial aldehyde dehydrogenase J. Biol. Chem. 268 1993 19906 19914
20. Y. Wang, and H. Weiner The presequence of rat liver aldehyde dehydrogenase requires the presence of an alpha-helix at its N-terminal region which is stabilized by the helix at its C termini J. Biol. Chem. 268 1993 4759 4765
21. S. Sjoling, A.C. Eriksson, and E. Glaser A helical element in the C-terminal domain of the N. plumbaginifolia F1 beta presequence is important for recognition by the mitochondrial processing peptidase J. Biol. Chem. 269 1994 32059 32062
22. A.B. Taylor, B.S. Smith, S. Kitada, K. Kojima, H. Miyaura, and Z. Otwinowski Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences Structure (Camb) 9 2001 615 625
23. G. von Heijne, J. Steppuhn, and R.G. Herrmann Domain structure of mitochondrial and chloroplast tareting peptides Eur. J. Biochem. 180 1989 535 545
24. G.W. Schmidt, and M.L. Mishkind The transport of proteins into chloroplasts Annu. Rev. Biochem. 55 1986 879 912
25. G.A. Karlin-Neumann, and E.M. Tobin Transit peptides of nuclear-encoded chloroplast proteins share a common amino acid framework EMBO J. 5 1986 9 13
26. M.G. Claros, and P. Vincens Computational method to predict mitochondrially imported proteins and their targeting sequences Eur. J. Biochem. 241 1996 779 786
27. S.M. Theg, and F.J. Geske Biophysical characterization of a transit peptide directing chloroplast protein import Biochemistry 31 1992 5053 5060
28. M. Pilon, A.G. Rietveld, P.J. Weisbeek, and B. de Kruijff Secondary structure and folding of a functional chloroplast precursor protein J. Biol. Chem. 267 1992 19907 19913
29. D.B. Bruce Chloroplast transit peptides: structure, function and evolution Trends Cell Biol. 10 2000 440 446
30. H.L. Wienk, M. Czisch, and B. de Kruijff The structural flexibility of the preferredoxin transit peptide FEBS Letters 453 1999 318 326
31. Y. Gavel, and G. von Heijne A conserved cleavage-site motif in chloroplast transit peptides FEBS Letters 261 1990 455 458
32. X.P. Zhang, and E. Glaser Interaction of plant mitochondrial and chloroplast signal peptides with the Hsp70 molecular chaperone Trends Plant Sci. 7 2002 14 21
33. O. Emanuelsson, H. Nielsen, and G. von Heijne ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites Protein Sci. 8 1999 978 984
34. S.E. Clark, and G.K. Lamppa Determinants for cleavage of the chlorophyll a/b binding protein precursor: a requirement for a basic residue that is not universal for chloroplast imported proteins J. Cell Biol. 114 1991 681 688
35. G. Creissen, H. Reynolds, Y. Xue, and P. Mullineaux Simultaneous targeting of pea glutathione reductase and of a bacterial fusion protein to chloroplasts and mitochondria in transgenic tobacco Plant J. 8 1995 167 175
36. C. Rudhe, O. Chew, J. Whelan, and E. Glaser A novel in vitro system for simultaneous import of precursor proteins into mitochondria and chloroplasts Plant J. 30 2002 213 220
37. S. Richter, and G.K. Lamppa Determinants for removal and degradation of transit peptides of chloroplast precursor proteins J. Biol. Chem. 277 2002 43888 43894
38. C. Rudhe, R. Clifton, J. Whelan, and E. Glaser N-terminal domain of the dual-targeted pea glutathione reductase signal peptide controls organellar targeting efficiency J. Mol. Biol. 324 2002 577 585
39. S. Sjoling, and E. Glaser Mitochondrial targeting peptides in plants Trends Plant Sci. 3 1998 136 140
40. C. Klaus, B. Guiard, W. Neupert, and M. Brunner Determinants in the presequence of cytochrome b2 for import into mitochondria and for proteolytic processing Eur. J. Biochem. 236 1996 856 861
41. E. Glaser, and P. Dessi Integration of the mitochondrial-processing peptidase into the cytochrome bc1 complex in plants J. Bioenerg. Biomembr. 31 1999 259 274
42. S. Iwata, J.W. Lee, K. Okada, J.K. Lee, M. Iwata, and B. Rasmussen Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex Science 281 1998 64 71
43. E. Glaser, and P. Dessi Intergration of the mitochondrial-processing peptidase into the cytochrome bc1 complex in plants J. Bioenerg. Biomembr. 31 1999 259 274
44. G. Creissen, E.A. Edwards, C. Enard, A. Wellburn, and P. Mullineaux Molecular characterization of glutathione reductase cDNAs from pea (Pisum sativum L.) Plant J. 2 1992 129 131
45. P.F. Pavlov, P. Moberg, X.P. Zhang, and E. Glaser Chemical cleavage of the overexpressed mitochondrial F1beta precursor with CNBr: a new strategy to construct an import-competent preprotein Biochem. J. 341 1999 95 103
46. A.C. Eriksson, S. Sjoling, and E. Glaser The ubiquinol cytochrome c oxidoreductase complex of spinach leaf mitochondria is involved in both respiration and protein processing Biochim. Biophys. Acta 1186 1994 221 231
47. K.S.J. Waegemann Characterization and isolation of the chloroplast import machinery Methods Cell Biol. 50 1995 255 267