메뉴 건너뛰기




Volumn 282, Issue 1-2, 1998, Pages 280-283

Mitochondrial leader sequences: Structural similarities and sequence differences

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA;

EID: 3543028004     PISSN: 0022104X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1097-010x(199809/10)282:1/2<280::aid-jez30>3.0.co;2-v     Document Type: Article
Times cited : (19)

References (16)
  • 1
    • 0024518002 scopus 로고
    • Sequence and structural requirements of a mitochondrial protein import signal defined by saturation cassette mutagenesis
    • Bedwell, D.M., S.A. Strobel, K. Yun, G.D. Jongeward, and S.D. Emr (1989) Sequence and structural requirements of a mitochondrial protein import signal defined by saturation cassette mutagenesis. Mol. Cell. Biol., 9:1014-1025.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1014-1025
    • Bedwell, D.M.1    Strobel, S.A.2    Yun, K.3    Jongeward, G.D.4    Emr, S.D.5
  • 2
    • 0026731326 scopus 로고
    • Conformational analysis of a mitochondrial presequence derived from the F1-ATPase -subunit by CD and NMR spectroscopy
    • Bruch, M.D., and D.W. Hoyt (1992) Conformational analysis of a mitochondrial presequence derived from the F1-ATPase -subunit by CD and NMR spectroscopy. Biochim. Biophys. Acta, 1159:81-93.
    • (1992) Biochim. Biophys. Acta , vol.1159 , pp. 81-93
    • Bruch, M.D.1    Hoyt, D.W.2
  • 3
    • 0024723123 scopus 로고
    • N-Terminal half of a mitochondrial presequence peptide takes a helical conformation when bound to dodecylphosphocholine micelles: A nuclear magnetic resonance study
    • Endo, T., I. Shimada, D. Roise, and F. Inagaki (1989) N-Terminal half of a mitochondrial presequence peptide takes a helical conformation when bound to dodecylphosphocholine micelles: a nuclear magnetic resonance study. J. Biochem., 106:396-400.
    • (1989) J. Biochem. , vol.106 , pp. 396-400
    • Endo, T.1    Shimada, I.2    Roise, D.3    Inagaki, F.4
  • 4
    • 0025053384 scopus 로고
    • Cleavage site motifs in mitochondrial targeting peptides
    • Gavel, A., and G. von Heijne (1990) Cleavage site motifs in mitochondrial targeting peptides. Prot. Eng., 4:33-37.
    • (1990) Prot. Eng. , vol.4 , pp. 33-37
    • Gavel, A.1    Von Heijne, G.2
  • 5
    • 0028068519 scopus 로고
    • Structures of the presequences of two mitochondrial matrix proteins that are not processed upon import
    • Hammen, P.K., D.G. Gorenstein, and H. Weiner (1994) Structures of the presequences of two mitochondrial matrix proteins that are not processed upon import. Biochemistry, 33:8610-8617.
    • (1994) Biochemistry , vol.33 , pp. 8610-8617
    • Hammen, P.K.1    Gorenstein, D.G.2    Weiner, H.3
  • 6
    • 0029788381 scopus 로고    scopus 로고
    • The role of positive charges and structural segments in the presequence of rat liver aldehyde dehydrogenase in import into mitochondria
    • Hammen, P.K., M. Waltner, B. Hahnemann, T.S. Heard, and H. Weiner (1996) The role of positive charges and structural segments in the presequence of rat liver aldehyde dehydrogenase in import into mitochondria. J. Biol. Chem., 271:21041-21048.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21041-21048
    • Hammen, P.K.1    Waltner, M.2    Hahnemann, B.3    Heard, T.S.4    Weiner, H.5
  • 8
    • 0028948675 scopus 로고
    • The yeast mitochondrial protein import receptor mas20p binds precursor proteins through electrostatic interaction with the positively charged presequence
    • Haucke, V., T. Lithgow, S. Rospert, K. Hahne, and G. Schatz (1995) The yeast mitochondrial protein import receptor mas20p binds precursor proteins through electrostatic interaction with the positively charged presequence. J. Biol. Chem., 270:5565-5570.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5565-5570
    • Haucke, V.1    Lithgow, T.2    Rospert, S.3    Hahne, K.4    Schatz, G.5
  • 9
    • 0028855710 scopus 로고
    • Solution structure of the acetylated and noncleavable mitochondrial targeting signal of rat chaperonin 10
    • Jarvis, J.A., M.T. Ryan, N.J. Hoogenraad, D.J. Craik, and P.B. Hoj (1995) Solution structure of the acetylated and noncleavable mitochondrial targeting signal of rat chaperonin 10. J. Biol. Chem., 270:1323-1331.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1323-1331
    • Jarvis, J.A.1    Ryan, M.T.2    Hoogenraad, N.J.3    Craik, D.J.4    Hoj, P.B.5
  • 10
    • 0025077695 scopus 로고
    • 2D NMR and structural model for a mitochondrial leader peptide bound to a micelle
    • Karslake, C., M. Piotto, Y.K Pak, H. Weiner, and D.G. Gorenstein (1990) 2D NMR and structural model for a mitochondrial leader peptide bound to a micelle. Biochemistry, 29:9872-9878.
    • (1990) Biochemistry , vol.29 , pp. 9872-9878
    • Karslake, C.1    Piotto, M.2    Pak, Y.K.3    Weiner, H.4    Gorenstein, D.G.5
  • 11
    • 0006078510 scopus 로고
    • Different structures in the amino-terminal domain of the ornithine transcarbamylase leader peptide are involved in mitochondrial import and carboxyl-terminal cleavage
    • Kraus, J.P, J. Novotny, F. Kalousek, M. Swaroop, and L.E. Rosenberg (1988) Different structures in the amino-terminal domain of the ornithine transcarbamylase leader peptide are involved in mitochondrial import and carboxyl-terminal cleavage. Proc. Natl. Acad. Sci. USA, 85:8905-8909.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8905-8909
    • Kraus, J.P.1    Novotny, J.2    Kalousek, F.3    Swaroop, M.4    Rosenberg, L.E.5
  • 13
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz, G., and B. Dobberstein (1996) Common principles of protein translocation across membranes. Science, 271: 1519-1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 14
    • 0027295559 scopus 로고
    • Import, processing and two-dimensional NMR structure of a linker-deleted leader peptide of rat liver mitochondrial aldehyde dehydrogenase
    • Thornton, K., Y. Wang, H. Weiner, and D.G. Gorenstein (1993) Import, processing and two-dimensional NMR structure of a linker-deleted leader peptide of rat liver mitochondrial aldehyde dehydrogenase. J. Biol. Chem., 268:19906-19914.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19906-19914
    • Thornton, K.1    Wang, Y.2    Weiner, H.3    Gorenstein, D.G.4
  • 15
    • 0022731676 scopus 로고
    • Mitochondrial targeting sequences may form amphiphilic helices
    • von Heijne, G. (1986) Mitochondrial targeting sequences may form amphiphilic helices. EMBO J., 5:1335-1342.
    • (1986) EMBO J. , vol.5 , pp. 1335-1342
    • Von Heijne, G.1
  • 16
    • 0027502921 scopus 로고
    • The presequence of rat liver aldehyde dehydrogenase requires the presence of an -helix at its n-terminal region which is stabilized by the helix at its C-termini
    • Wang, Y., and H. Weiner (1993) The presequence of rat liver aldehyde dehydrogenase requires the presence of an -helix at its n-terminal region which is stabilized by the helix at its C-termini. J. Biol. Chem., 268:4759-4765.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4759-4765
    • Wang, Y.1    Weiner, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.