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Volumn 10, Issue 11, 2000, Pages

Protein sorting: Recognizing mitochondrial presequences

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA;

EID: 0034214123     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(00)00507-8     Document Type: Review
Times cited : (94)

References (33)
  • 1
    • 0018987976 scopus 로고
    • Intracellular protein topogenesis
    • Blobel G. Intracellular protein topogenesis. Proc Natl Acad Sci USA. 77:1980;1496-1500.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 1496-1500
    • Blobel, G.1
  • 2
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz G., Dobberstein B. Common principles of protein translocation across membranes. Science. 271:1996;1519-1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 3
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert W. Protein import into mitochondria. Annu Rev Biochem. 66:1997;863-917.
    • (1997) Annu Rev Biochem , vol.66 , pp. 863-917
    • Neupert, W.1
  • 5
    • 0034598904 scopus 로고    scopus 로고
    • Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20
    • Abe Y., Shodai T., Muto T., Mihara K., Torii H., Nishikawa S.-i., Endo T., Kohda D. Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20. Cell. 100:2000;551-560.
    • (2000) Cell , vol.100 , pp. 551-560
    • Abe, Y.1    Shodai, T.2    Muto, T.3    Mihara, K.4    Torii, H.5    Nishikawa, S.-i.6    Endo, T.7    Kohda, D.8
  • 6
    • 0023920458 scopus 로고
    • Mitochondrial presequences
    • Roise D., Schatz G. Mitochondrial presequences. J Biol Chem. 263:1988;4509-4511.
    • (1988) J Biol Chem , vol.263 , pp. 4509-4511
    • Roise, D.1    Schatz, G.2
  • 7
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • von Heijne G., Steppuhn J., Herrmann R.G. Domain structure of mitochondrial and chloroplast targeting peptides. Eur J Biochem. 180:1989;535-545.
    • (1989) Eur J Biochem , vol.180 , pp. 535-545
    • Von Heijne, G.1    Steppuhn, J.2    Herrmann, R.G.3
  • 8
    • 0024801086 scopus 로고
    • MOM19, an import receptor for mitochondrial precursor proteins
    • Söllner T., Griffiths G., Pfaller R., Pfanner N., Neupert W. MOM19, an import receptor for mitochondrial precursor proteins. Cell. 59:1989;1061-1070.
    • (1989) Cell , vol.59 , pp. 1061-1070
    • Söllner, T.1    Griffiths, G.2    Pfaller, R.3    Pfanner, N.4    Neupert, W.5
  • 9
    • 0027434076 scopus 로고
    • Functional cooperation of mitochondrial protein import receptors in yeast
    • Ramage L., Junne T., Hahne K., Lithgow T., Schatz G. Functional cooperation of mitochondrial protein import receptors in yeast. EMBO J. 12:1993;4115-4123.
    • (1993) EMBO J , vol.12 , pp. 4115-4123
    • Ramage, L.1    Junne, T.2    Hahne, K.3    Lithgow, T.4    Schatz, G.5
  • 10
    • 0028264383 scopus 로고
    • Deletion of the receptor MOM19 strongly impairs import of cleavable preproteins into Saccharomyces cerevisiae mitochondria
    • Moczko M., Ehmann B., Gärtner F., Hönlinger A., Schäfer E., Pfanner N. Deletion of the receptor MOM19 strongly impairs import of cleavable preproteins into Saccharomyces cerevisiae mitochondria. J Biol Chem. 269:1994;9045-9051.
    • (1994) J Biol Chem , vol.269 , pp. 9045-9051
    • Moczko, M.1    Ehmann, B.2    Gärtner, F.3    Hönlinger, A.4    Schäfer, E.5    Pfanner, N.6
  • 12
    • 0031741738 scopus 로고    scopus 로고
    • Preprotein translocase of the outer mitochondrial membrane: Molecular dissection and assembly of the general import pore complex
    • Dekker P.J.T., Ryan M.T., Brix J., Müller H., H.önlinger A., Pfanner N. Preprotein translocase of the outer mitochondrial membrane: molecular dissection and assembly of the general import pore complex. Mol Cell Biol. 18:1998;6515-6524.
    • (1998) Mol Cell Biol , vol.18 , pp. 6515-6524
    • Dekker, P.J.T.1    Ryan, M.T.2    Brix, J.3    Müller, H.4    H.önlinger, A.5    Pfanner, N.6
  • 14
    • 0032188847 scopus 로고    scopus 로고
    • Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins
    • Hill K., Model K., Ryan M.T., Dietmeier K., Martin F., Wagner R., Pfanner N. Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins. Nature. 395:1998;516-521.
    • (1998) Nature , vol.395 , pp. 516-521
    • Hill, K.1    Model, K.2    Ryan, M.T.3    Dietmeier, K.4    Martin, F.5    Wagner, R.6    Pfanner, N.7
  • 15
    • 1842368473 scopus 로고    scopus 로고
    • Just follow the acid chain
    • Schatz G. Just follow the acid chain. Nature. 388:1997;121-122.
    • (1997) Nature , vol.388 , pp. 121-122
    • Schatz, G.1
  • 16
    • 0033592642 scopus 로고    scopus 로고
    • Protein translocation: Is Hsp70 pulling my chain?
    • Jensen R.E., Johnson A.E. Protein translocation: is Hsp70 pulling my chain? Curr Biol. 9:1999;R779-R782.
    • (1999) Curr Biol , vol.9
    • Jensen, R.E.1    Johnson, A.E.2
  • 18
    • 0032527780 scopus 로고    scopus 로고
    • Interaction of mitochondrial targeting signals with acidic receptor domains along the protein import pathway: Evidence for the 'acid chain' hypothesis
    • Komiya T., Rospert S., Koehler C., Looser R., Schatz G., Mihara K. Interaction of mitochondrial targeting signals with acidic receptor domains along the protein import pathway: evidence for the 'acid chain' hypothesis. EMBO J. 17:1998;3886-3898.
    • (1998) EMBO J , vol.17 , pp. 3886-3898
    • Komiya, T.1    Rospert, S.2    Koehler, C.3    Looser, R.4    Schatz, G.5    Mihara, K.6
  • 19
    • 0030769419 scopus 로고    scopus 로고
    • Differential recognition of preproteins by the purified cytosolic domains of the mitochondrial import receptors Tom20, Tom22 and Tom70
    • Brix J., Dietmeier K., Pfanner N. Differential recognition of preproteins by the purified cytosolic domains of the mitochondrial import receptors Tom20, Tom22 and Tom70. J Biol Chem. 272:1997;20730-20735.
    • (1997) J Biol Chem , vol.272 , pp. 20730-20735
    • Brix, J.1    Dietmeier, K.2    Pfanner, N.3
  • 20
    • 0030791131 scopus 로고    scopus 로고
    • Interactions of the human mitochondrial protein import receptor, hTom20, with precursor proteins in vitro reveal pleiotropic specificities and different receptor domain requirements
    • Schleiff E., Shore G.C., Goping I.S. Interactions of the human mitochondrial protein import receptor, hTom20, with precursor proteins in vitro reveal pleiotropic specificities and different receptor domain requirements. J Biol Chem. 272:1997;17784-17789.
    • (1997) J Biol Chem , vol.272 , pp. 17784-17789
    • Schleiff, E.1    Shore, G.C.2    Goping, I.S.3
  • 21
    • 0032558380 scopus 로고    scopus 로고
    • Functional and structural properties of the mitochondrial outer membrane receptor Tom20
    • Schleiff E., Turnbull J.L. Functional and structural properties of the mitochondrial outer membrane receptor Tom20. Biochemistry. 37:1998;13043-13051.
    • (1998) Biochemistry , vol.37 , pp. 13043-13051
    • Schleiff, E.1    Turnbull, J.L.2
  • 22
    • 0032558427 scopus 로고    scopus 로고
    • Characterization of the N-terminal targeting signal binding domain of the mitochondrial outer membrane receptor, Tom20
    • Schleiff E., Turnbull J.L. Characterization of the N-terminal targeting signal binding domain of the mitochondrial outer membrane receptor, Tom20. Biochemistry. 37:1998;13052-13058.
    • (1998) Biochemistry , vol.37 , pp. 13052-13058
    • Schleiff, E.1    Turnbull, J.L.2
  • 23
    • 0040610676 scopus 로고    scopus 로고
    • The mitochondrial import receptors Tom20, Tom22 and Tom70: Distribution of binding sequences in a presequence-carrying preprotein and a non-cleavable preprotein
    • Brix J., R.üdiger S., Bukau B., Schneider-Mergener J., Pfanner N. The mitochondrial import receptors Tom20, Tom22 and Tom70: distribution of binding sequences in a presequence-carrying preprotein and a non-cleavable preprotein. J Biol Chem. 274:1999;16522-16530.
    • (1999) J Biol Chem , vol.274 , pp. 16522-16530
    • Brix, J.1    R.üdiger, S.2    Bukau, B.3    Schneider-Mergener, J.4    Pfanner, N.5
  • 24
    • 0032704556 scopus 로고    scopus 로고
    • Positively charged residues, the helical conformation and the structural flexibility of the leader sequence of pALDH are important for recognition by hTom20
    • Schleiff E., Heard T.S., Weiner H. Positively charged residues, the helical conformation and the structural flexibility of the leader sequence of pALDH are important for recognition by hTom20. FEBS Lett. 461:1999;9-12.
    • (1999) FEBS Lett , vol.461 , pp. 9-12
    • Schleiff, E.1    Heard, T.S.2    Weiner, H.3
  • 25
    • 0028948675 scopus 로고
    • The yeast mitochondrial protein import receptor Mas20p binds precursor proteins through electrostatic interaction with the positively charged presequence
    • Haucke V., Lithgow T., Rospert S., Hahne K., Schatz G. The yeast mitochondrial protein import receptor Mas20p binds precursor proteins through electrostatic interaction with the positively charged presequence. J Biol Chem. 270:1995;5565-5570.
    • (1995) J Biol Chem , vol.270 , pp. 5565-5570
    • Haucke, V.1    Lithgow, T.2    Rospert, S.3    Hahne, K.4    Schatz, G.5
  • 26
    • 0032500553 scopus 로고    scopus 로고
    • Functional analysis of human mitochondrial receptor Tom20 for protein import into mitochondria
    • Yano M., Kanazawa M., Terada K., Takeya M., Hoogenraad N., Mori M. Functional analysis of human mitochondrial receptor Tom20 for protein import into mitochondria. J Biol Chem. 273:1998;26844-26851.
    • (1998) J Biol Chem , vol.273 , pp. 26844-26851
    • Yano, M.1    Kanazawa, M.2    Terada, K.3    Takeya, M.4    Hoogenraad, N.5    Mori, M.6
  • 28
    • 0027295559 scopus 로고
    • Import, processing and two-dimensional NMR structure of a linker-deleted signal peptide of rat liver mitochondrial aldehyde dehydrogenase
    • Thornton K., Wang Y., Weiner H., Gorenstein D.G. 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.
    • (1993) J Biol Chem , vol.268 , pp. 19906-19914
    • Thornton, K.1    Wang, Y.2    Weiner, H.3    Gorenstein, D.G.4
  • 29
    • 0029963554 scopus 로고    scopus 로고
    • The Mas20p and Mas70p subunits of the protein import receptor of yeast mitochondria interact via the tetratricopeptide repeat motif in Mas20p: Evidence for a single hetero-oligomeric receptor
    • Haucke V., Horst M., Schatz G., Lithgow T. The Mas20p and Mas70p subunits of the protein import receptor of yeast mitochondria interact via the tetratricopeptide repeat motif in Mas20p: evidence for a single hetero-oligomeric receptor. EMBO J. 15:1996;1231-1237.
    • (1996) EMBO J , vol.15 , pp. 1231-1237
    • Haucke, V.1    Horst, M.2    Schatz, G.3    Lithgow, T.4
  • 31
    • 0032563163 scopus 로고    scopus 로고
    • Crystal structure of the signal sequence binding subunit of the signal recognition particle
    • Keenan R.J., Freymann D.M., Walter P., Stroud R.M. Crystal structure of the signal sequence binding subunit of the signal recognition particle. Cell. 94:1998;181-191.
    • (1998) Cell , vol.94 , pp. 181-191
    • Keenan, R.J.1    Freymann, D.M.2    Walter, P.3    Stroud, R.M.4
  • 32
    • 0034681490 scopus 로고    scopus 로고
    • Crystal structure of the ribonucleoprotein core of the signal recognition particle
    • Batey R.T., Rambo R.P., Lucast L., Rha B., Doudna J.A. Crystal structure of the ribonucleoprotein core of the signal recognition particle. Science. 287:2000;1232-1239.
    • (2000) Science , vol.287 , pp. 1232-1239
    • Batey, R.T.1    Rambo, R.P.2    Lucast, L.3    Rha, B.4    Doudna, J.A.5
  • 33
    • 0033982735 scopus 로고    scopus 로고
    • Structure of the cytosolic domain of TOM5, a mitochondrial import protein
    • Hammen P.K., Weiner H. Structure of the cytosolic domain of TOM5, a mitochondrial import protein. FEBS Lett. 468:2000;101-104.
    • (2000) FEBS Lett , vol.468 , pp. 101-104
    • Hammen, P.K.1    Weiner, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.