The precursor of the F1β subunit of the ATP synthase is covalently modified upon binding to plant mitochondria

Plant Molecular Biology

Volumn 41, Issue 4, 1999, Pages 505-515

  Von Stedingk, Erik ^a   Pavlov, Pavel F ^a   Grinkevich, Vladimir A ^a,b   Glaser, Elzbieta ^a  

^a STOCKHOLM UNIVERSITY   (Sweden)

^b MOSCOW STATE UNIVERSITY   (Russian Federation)

Author keywords

ATP synthase; Modification; PF1 ; Plant mitochondria; Precursor; Protein import

Indexed keywords

ACYLATION; ADENOSINE TRIPHOSPHATE SYNTHASE; AMINO TERMINAL SEQUENCE; CATALYSIS; EDETIC ACID; ENZYME ACTIVITY; ENZYME INHIBITOR; ENZYME MODIFICATION; ENZYME PRECURSOR; ENZYME SUBUNIT; METHYLATION; MITOCHONDRION; PHOSPHATASE; POTASSIUM CHLORIDE; PROTEIN KINASE; PROTEIN TARGETING; UREA;

EMBRYOPHYTA; NICOTIANA PLUMBAGINIFOLIA;

ADENOSINE TRIPHOSPHATE; CALCIUM; ENZYME PRECURSOR; METALLOPROTEINASE; MITOCHONDRIAL PROCESSING PEPTIDASE; PEPTIDE FRAGMENT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

ARTICLE; BINDING COMPETITION; BIOTINYLATION; CHEMISTRY; DRUG EFFECT; INTRACELLULAR MEMBRANE; METABOLISM; MITOCHONDRION; MOLECULAR WEIGHT; PLANT; POTATO; PROTEIN BINDING; PROTEIN PROCESSING; TOBACCO;

ADENOSINE TRIPHOSPHATE; BINDING, COMPETITIVE; BIOTINYLATION; CALCIUM; ENZYME PRECURSORS; INTRACELLULAR MEMBRANES; METALLOENDOPEPTIDASES; MITOCHONDRIA; MOLECULAR WEIGHT; PEPTIDE FRAGMENTS; PLANTS, TOXIC; PROTEIN BINDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTON-TRANSLOCATING ATPASES; SOLANUM TUBEROSUM; TOBACCO;

EID: 0032585896     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006375123496     Document Type: Article

References (46)

1. Bairoch, A., Bucher, P. and Hofmann, K. 1997. The PROSITE database, its status in 1997. Nucl. Acids Res. 25: 217-221.
2. Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
3. Braun, H.P. and Schmitz, U.K. 1995. The bifunctional cytochrome c reductase/processing peptidase complex from plant mitochondria. J. Bioenerg. Biomembr. 27: 423-436.
4. Brix, J., Dietmeier, K. and Pfanner, N. 1997. Differential recognition of preproteins by the purified cytosolic domains of the mitochondrial import receptors Tom20, Tom22, and Tom70. J. Biol. Chem. 272: 20730-20735.
5. Caplan, A.J. Cyr, D.M. and Douglas, M.G. 1992. YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell 71: 1143-1155.
6. Cyr, D.M. and Douglas, M.G. 1991. Early events in the transport of proteins into mitochondria. Import competition by a mitochondrial presequence. J. Biol. Chem. 266: 21700-21708.
7. Dietmeier, K., Honlinger, A., Bomer, U., Dekker, P.J., Eckerskorn, C., Lottspeich, F., Kubrich, M. and Pfanner, N. 1997. Tom5 functionally links mitochondrial preprotein receptors to the general import pore. Nature 388: 195-200.
8. 1 complex of the respiratory chain. In: A. Brennicke and U. Kuch (Eds.), Plant Mitochondria, VCH Verlagsgesellschaft, Germany, pp. 233-241.
9. Glaser, S.M. and Cumsky, M.G. 1990a. A synthetic presequence reversibly inhibits protein import into yeast mitochondria. J. Biol. Chem. 265: 8808-8816.
10. Glaser, S.M. and Cumsky, M.G. 1990b. Localization of a synthetic presequence that blocks protein import into mitochondria. J. Biol. Chem. 265: 8817-8822.
11. Glaser, E., Sjoling, S., Tanudji, M. and Whelan, J. 1998. Mitochondrial protein import in plants. Signals, sorting, targeting, processing and regulation. Plant Mol. Biol. 38: 311-338.
12. Hachiya. N., Komiya, T., Alam, R., Iwahashi, J., Sakaguchi, M., Omura, T. and Mihara, K. 1994. MSF, a novel cytoplasmic chaperone which functions in precursor targeting to mitochondria. EMBO J. 13: 5146-5154.
13. Hachiya, N., Mihara, K., Suda, K., Horst, M., Schatz, G. and Lithgow, T. 1995. Reconstruction of the initial steps of mitochondrial protein import. Nature 376: 705-709.
14. 1-ATPase β subunit precursor. Import requires external ATP. J. Biol. Chem. 269: 7192-7200.
15. 2+/calmodulin-dependent protein kinase II blocks its nuclear targeting. J. Biol. Chem. 273: 19763-19771.
16. Hines, V., Brandt, A., Griffiths, G., Horstmann, H., Brutsch, H. and Schatz, G. 1990. Protein import into yeast mitochondria is accelerated by the outer membrane protein MAS70. EMBO J. 9: 3191-3200.
17. Honlinger, A., Bomer, U., Alconada, A., Eckerskorn, C. Lottspeich, F., Dietmeier, K. and Pfanner, N. 1996. Tom7 modulates the dynamics of the mitochondrial outer membrane translocase and plays a pathway-related role in protein import. EMBO J. 15: 2125-2137.
18. Jänsch, L., Kruft, V., Schmitz, U.K. and Braun, H.P. 1998. Unique composition of the preprotein translocase of the outer mitochondrial membrane from plants. J. Biol. Chem. 273: 17251-17257.
19. Kiebler, M., Pfaller, R., Sollner, T., Griffiths, G., Horstmann, H., Pfanner, N. and Neupert, W. 1990. Identification of a mitochondrial receptor complex required for recognition and membrane insertion of precursor proteins. Nature 348: 610-616.
20. 2 for import into mitochondria and for proteolytic processing. Eur. J. Biochem. 236: 856-861.
21. Knorpp, C., Hugosson, M. and Glaser, E. 1992. Temperature dependence and kinetics of plant mitochondrial protein import. In: H. Lambers and L. van der Plas (Eds.), Molecular, Biochemical and Physiological Aspects of Plant Respiration, SPB Academic Publishing, The Hague, Netherlands, pp. 361-365.
22. Komiya, T., Hachiya, N., Sakaguchi, M., Omura, T. and Mihara, K. 1994. Recognition of mitochondria-targeting signals by a cytosolic import stimulation factor, MSF. J. Biol. Chem. 269: 30893-30897.
23. Komiya, T., Rospert, S., Koehler, C., Looser, R., Schatz, G. and Mihara, K. 1998. Interaction of mitochondrial targeting signals with acidic receptor domains along the protein import pathway: evidence for the 'acid chain' hypothesis. EMBO J. 17: 3886-3898.
24. Kunkele, K.P., Heins, S., Dembowski, M., Nargang, F.E., Benz, R., Thieffry, M., Walz, J., Lill, R., Nussberger, S. and Neupert, W. 1998. The preprotein translocation channel of the outer membrane of mitochondria. Cell 93: 1009-1019.
25. Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
26. Lain, B., Yanez, A., Iriarte, A. and Martinez-Carrion, M. 1998. Aminotransferase variants as the role of the N-terminal region of a mature protein in mitochondrial precursor import and processing. J. Biol. Chem. 273: 4406-4415.
27. Luciano, P. and Geli, V. 1996. The mitochondrial processing peptidase: function and specificity. Experientia 52: 1077-1082.
28. Moczko, M., Bomer, U., Kubrich, M., Zufall, N., Honlinger, A. and Pfanner, N. 1997. The intermembrane space domain of mitochondrial Tom22 functions as a trans binding site for preproteins with N-terminal targeting sequences. Mol. Cell Biol. 17: 6574-6584.
29. Murakami, K., Tanase, S., Morino, Y. and Mori, M. 1992. Presequence binding factor-dependent and -independent import of proteins into mitochondria. J. Biol. Chem. 267: 13119-13122.
30. Neupert, W. 1997. Protein import into mitochondria. Annu. Rev. Biochem. 66: 863-917.
31. Pfanner, N., Craig, E.A. and Honlinger, A. 1997. Mitochondrial preprotein translocase. Annu. Rev. Cell Dev. Biol. 13: 25-51.
32. Pical, C., Fredlund, K.M., Petit, P.X., Sommarin, M. and Møller, I.M. 1993. The outer membrane of plant mitochondria contains a calcium-dependent protein kinase and multiple phosphoproteins. FEBS Lett. 336: 347-351.
33. Rapaport, D., Neupert, W. and Lill, R. 1997. Mitochondrial protein import. Tom40 plays a major role in targeting and translocation of preproteins by forming a specific binding site for the presequence. J. Biol. Chem. 272: 18725-18731.
34. Schägger, H., and von Jagow, G. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166: 368-379.
35. Schneider, G., Sjöling, S., Wallin, E., Wrede, P., Glaser, E. and von Heijne, G. 1998. Feature-extraction from endopeptidase cleavage sites in mitochondrial targeting peptides. Proteins 30: 49-60.
36. Sjöling, S. and Glaser, E. 1998. Mitochondrial targeting peptides in plants. Trends Plant Sci. 3: 136-140.
37. 1β presequence is important for recognition by the mitochondrial processing peptidase. J. Biol. Chem. 269: 32059-32062.
38. Smagula, C. and Douglas, M.G. 1988. Mitochondrial import of the ADP/ATP carrier protein in Saccharomyces cerevisiae. Sequences required for receptor binding and membrane translocation. J. Biol. Chem. 263: 6783-6790.
39. Szigyarto, C., Dessi, P., Smith, M.K., Knorpp, C., Harmey, M.A., Day, D.A., Glaser, E. and Whelan, J. 1998. A matrix-located processing peptidase of plant mitochondria. Plant Mol. Biol. 36: 171-181.
40. Terada, K., Kanazawa, M., Bukau, B. and Mori, M. 1997. The human DnaJ homologue dj2 facilitates mitochondrial protein import and luciferase refolding. J. Cell Biol. 139: 1089-1095.
41. von Heijne, G., Steppuhn, J. and Herrmann, R.G. 1989. Domain structure of mitochondrial and chloroplast targeting peptides. Eur. J. Biochem. 180: 535-545.
42. von Stedingk, E.M., Pavlov, P.F., Grinkevich, V.A. and Glaser, E. 1997. Mitochondrial protein import: modification of sulfhydryl groups of the inner mitochondrial membrane import machinery in Solanum tuberosum inhibits protein import. Plant Mol. Biol. 35: 809-820.
43. Wachter, C., Schatz, G. and Glick, B.S. 1994. Protein import into mitochondria: the requirement for external ATP is precursor-specific whereas intramitochondrial ATP is universally needed for translocation into the matrix. Mol. Biol. Cell 5: 465-474.
44. Waegemann, X. and Soll, J. 1996. Phosphorylation of the transit sequence of chloroplast precursor proteins. J. Biol. Chem. 271: 6545-6554.
45. Wang, X., Dumont, M.E. and Sherman, F. 1996. Sequence requirements for mitochondrial import of yeast cytochrome c. J. Biol. Chem. 271: 6594-6604.
46. Whelan, J., O'Mahony, P. and Harmey, M.A. 1990. Processing of precursor proteins by plant mitochondria. Arch. Biochem. Biophys. 279: 281-285.