메뉴 건너뛰기




Volumn 17, Issue 1, 1998, Pages 269-277

The N-end rule pathway controls the import of peptides through degradation of a transcriptional repressor

Author keywords

CUP9; N end rule; Peptide import; Proteolysis; PTR2; UBR1

Indexed keywords

COPPER; HOMEODOMAIN PROTEIN; PEPTIDE; REPRESSOR PROTEIN;

EID: 0032472322     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.1.269     Document Type: Article
Times cited : (106)

References (45)
  • 1
    • 0028964284 scopus 로고
    • A recognition component of the ubiquitin system is required for peptide transport in Saccharomyces cerevisiae
    • Alagramam, K., Naider, F. and Becker, J.M. (1995) A recognition component of the ubiquitin system is required for peptide transport in Saccharomyces cerevisiae. Mol. Microbiol., 15, 225-234.
    • (1995) Mol. Microbiol. , vol.15 , pp. 225-234
    • Alagramam, K.1    Naider, F.2    Becker, J.M.3
  • 3
    • 0024562943 scopus 로고
    • The degradation signal in a short-lived protein
    • Bachmair, A. and Varshavsky, A. (1989) The degradation signal in a short-lived protein. Cell, 56, 1019-1032.
    • (1989) Cell , vol.56 , pp. 1019-1032
    • Bachmair, A.1    Varshavsky, A.2
  • 4
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair, A., Finley, D. and Varshavsky, A. (1986) In vivo half-life of a protein is a function of its amino-terminal residue. Science, 234, 179-186.
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 5
    • 0001236309 scopus 로고
    • Inhibition of the N-end rule pathway in living cells
    • Baker, R.T. and Varshavsky, A. (1991) Inhibition of the N-end rule pathway in living cells. Proc. Natl Acad. Sci. USA, 87, 2374-2378.
    • (1991) Proc. Natl Acad. Sci. USA , vol.87 , pp. 2374-2378
    • Baker, R.T.1    Varshavsky, A.2
  • 6
    • 0029016564 scopus 로고
    • Yeast N-terminal amidase: A new enzyme and component of the N-end rule pathway
    • Baker, R.T. and Varshavsky, A. (1995) Yeast N-terminal amidase: a new enzyme and component of the N-end rule pathway. J. Biol. Chem., 270, 12065-12074.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12065-12074
    • Baker, R.T.1    Varshavsky, A.2
  • 7
    • 0025272837 scopus 로고
    • Cloning and functional analysis of the arginyl-tRNA-protein transferase gene ATE1 of Saccharomyces cerevisiae
    • Balzi, E., Choder, M., Chen, W.A., Varshavsky, A. and Goffeau, A. (1990) Cloning and functional analysis of the arginyl-tRNA-protein transferase gene ATE1 of Saccharomyces cerevisiae. J. Biol. Chem., 265, 7464-7471.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7464-7471
    • Balzi, E.1    Choder, M.2    Chen, W.A.3    Varshavsky, A.4    Goffeau, A.5
  • 9
    • 0025050840 scopus 로고
    • The recognition component of the N-end rule pathway
    • Bartel, B., Wünning, I. and Varshavsky, A. (1990) The recognition component of the N-end rule pathway. EMBO J., 9, 3179-3189.
    • (1990) EMBO J. , vol.9 , pp. 3179-3189
    • Bartel, B.1    Wünning, I.2    Varshavsky, A.3
  • 10
    • 0028685250 scopus 로고
    • Preparation of extracts from yeast and avoidance of proteolysis
    • Burgers, P.M.J. (1995) Preparation of extracts from yeast and avoidance of proteolysis. Methods Mol. Cell. Biol., 5, 330-335.
    • (1995) Methods Mol. Cell. Biol. , vol.5 , pp. 330-335
    • Burgers, P.M.J.1
  • 11
    • 0024514688 scopus 로고
    • A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
    • Chau, V., Tobias, J.W., Bachmair, A., Marriott, D., Ecker, D.J., Gonda, D.K. and Varshavsky, A. (1989) A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science, 243, 1576-1583.
    • (1989) Science , vol.243 , pp. 1576-1583
    • Chau, V.1    Tobias, J.W.2    Bachmair, A.3    Marriott, D.4    Ecker, D.J.5    Gonda, D.K.6    Varshavsky, A.7
  • 12
    • 0027198563 scopus 로고
    • Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 repressor
    • Chen, P., Johnson, P., Sommer, T., Jentsch, S. and Hochstrasser, M. (1993) Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 repressor. Cell, 74, 357-369.
    • (1993) Cell , vol.74 , pp. 357-369
    • Chen, P.1    Johnson, P.2    Sommer, T.3    Jentsch, S.4    Hochstrasser, M.5
  • 13
    • 0026512939 scopus 로고
    • Multifunctional yeast high-copy-number shuttle vectors
    • Christianson, T.W., Sikorski, R.S., Dante, M. and Hieter, P. (1992) Multifunctional yeast high-copy-number shuttle vectors. Gene, 110, 119-122.
    • (1992) Gene , vol.110 , pp. 119-122
    • Christianson, T.W.1    Sikorski, R.S.2    Dante, M.3    Hieter, P.4
  • 16
    • 0023666139 scopus 로고
    • The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation and other stresses
    • Finley, D., Özkaynak, E. and Varshavsky, A. (1987) The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation and other stresses. Cell, 48, 1035-1046.
    • (1987) Cell , vol.48 , pp. 1035-1046
    • Finley, D.1    Özkaynak, E.2    Varshavsky, A.3
  • 17
    • 0029814693 scopus 로고    scopus 로고
    • Cdc48p interacts with Ufd3p, a WD-repeat protein required for ubiquitin-dependent proteolysis in Saccharomyces cerevisiae
    • Ghislain, M., Dohmen, R.J., Lévy, F. and Varshavsky, A. (1996) Cdc48p interacts with Ufd3p, a WD-repeat protein required for ubiquitin-dependent proteolysis in Saccharomyces cerevisiae. EMBO J., 15, 4884-4899.
    • (1996) EMBO J. , vol.15 , pp. 4884-4899
    • Ghislain, M.1    Dohmen, R.J.2    Lévy, F.3    Varshavsky, A.4
  • 18
    • 0024788838 scopus 로고
    • A regulatory hierarchy for cell specialization in yeast
    • Herskowitz, I. (1989) A regulatory hierarchy for cell specialization in yeast. Nature, 342, 749-757.
    • (1989) Nature , vol.342 , pp. 749-757
    • Herskowitz, I.1
  • 19
    • 0029867623 scopus 로고    scopus 로고
    • Proteasomes: Destruction as a programme
    • Hilt, W. and Wolf, D.H. (1996) Proteasomes: destruction as a programme. Trends Biochem. Sci., 21, 96-102.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 96-102
    • Hilt, W.1    Wolf, D.H.2
  • 20
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser, M. (1996) Ubiquitin-dependent protein degradation. Annu. Rev. Genet., 30, 405-439.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 21
    • 0025331090 scopus 로고
    • In vivo degradation of a transcriptional regulator: The yeast α2 repressor
    • Hochstrasser, M. and Varshavsky, A. (1990) In vivo degradation of a transcriptional regulator: the yeast α2 repressor. Cell, 61, 697-708.
    • (1990) Cell , vol.61 , pp. 697-708
    • Hochstrasser, M.1    Varshavsky, A.2
  • 22
    • 0023260311 scopus 로고
    • Regulation of dipeptide transport in S.cerevisiae by micromolar amino acid concentrations
    • Island, M.D., Naider, F. and Becker, J.M. (1987) Regulation of dipeptide transport in S.cerevisiae by micromolar amino acid concentrations. J. Bacteriol., 169, 2132-2136.
    • (1987) J. Bacteriol. , vol.169 , pp. 2132-2136
    • Island, M.D.1    Naider, F.2    Becker, J.M.3
  • 23
    • 0027053491 scopus 로고
    • The ubiquitin-conjugating system
    • Jentsch, S. (1992) The ubiquitin-conjugating system. Annu. Rev. Genet., 26, 179-207.
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 179-207
    • Jentsch, S.1
  • 24
    • 0029162583 scopus 로고
    • Selective protein degradation: A journey's end within the proteasome
    • Jentsch, S. and Schlenker, S. (1995) Selective protein degradation: a journey's end within the proteasome. Cell, 82, 881-884.
    • (1995) Cell , vol.82 , pp. 881-884
    • Jentsch, S.1    Schlenker, S.2
  • 25
    • 0025345753 scopus 로고
    • Cis-trans recognition and subunit-specific degradation of short-lived proteins
    • Johnson, E.S., Gonda, D.K. and Varshavsky, A. (1990) Cis-trans recognition and subunit-specific degradation of short-lived proteins. Nature, 346, 287-291.
    • (1990) Nature , vol.346 , pp. 287-291
    • Johnson, E.S.1    Gonda, D.K.2    Varshavsky, A.3
  • 27
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson, E.S., Ma, P.C.M., Ota, I.M. and Varshavsky, A. (1995) A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. Chem., 270, 17442-17456.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.M.2    Ota, I.M.3    Varshavsky, A.4
  • 29
    • 0028171037 scopus 로고
    • Identification and analysis of a Saccharomyces cerevisiae copper homeostasis gene encoding a homeodomain protein
    • Knight, S.A.B., Tamai, K.T., Kosman, D.J. and Thiele, D.J. (1994) Identification and analysis of a Saccharomyces cerevisiae copper homeostasis gene encoding a homeodomain protein. Mol. Cell. Biol., 14, 7792-7804.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7792-7804
    • Knight, S.A.B.1    Tamai, K.T.2    Kosman, D.J.3    Thiele, D.J.4
  • 30
    • 0028169361 scopus 로고
    • Degradation of Gα by the N-end rule pathway
    • Madura, K. and Varshavsky, A. (1994) Degradation of Gα by the N-end rule pathway. Science, 265, 1454-1458.
    • (1994) Science , vol.265 , pp. 1454-1458
    • Madura, K.1    Varshavsky, A.2
  • 31
    • 0027316341 scopus 로고
    • N-recognin/Ubc2 interactions in the N-end rule pathway
    • Madura, K., Dohmen, R.J. and Varshavsky, A. (1993) N-recognin/Ubc2 interactions in the N-end rule pathway. J. Biol. Chem., 268, 12046-12054.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12046-12054
    • Madura, K.1    Dohmen, R.J.2    Varshavsky, A.3
  • 32
    • 0028586017 scopus 로고
    • Regulatable promoters of Saccharomyces cerevisiae: Comparison of transcriptional activity and their use for heterologous expression
    • Mumberg, G., Müller, R. and Funk, M. (1994) Regulatable promoters of Saccharomyces cerevisiae: comparison of transcriptional activity and their use for heterologous expression. Nucleic Acids Res., 22, 5767-5768.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5767-5768
    • Mumberg, G.1    Müller, R.2    Funk, M.3
  • 33
    • 0029994433 scopus 로고    scopus 로고
    • Copper-dependent degradation of the Saccharomyces cerevisiae plasma membrane copper transporter Ctr1p in the apparent absence of endocytosis
    • Ooi, C.E., Rabinovich, E., Dancis, A., Bonifacino, J.S. and Klausner, R.D. (1996) Copper-dependent degradation of the Saccharomyces cerevisiae plasma membrane copper transporter Ctr1p in the apparent absence of endocytosis. EMBO J., 15, 3515-3523.
    • (1996) EMBO J. , vol.15 , pp. 3515-3523
    • Ooi, C.E.1    Rabinovich, E.2    Dancis, A.3    Bonifacino, J.S.4    Klausner, R.D.5
  • 34
    • 0025979877 scopus 로고
    • Targeting, disruption, replacement, and allele rescue: Integrative DNA transformation in yeast
    • Rothstein, R. (1991) Targeting, disruption, replacement, and allele rescue: integrative DNA transformation in yeast. Methods Enzymol, 194, 281-301.
    • (1991) Methods Enzymol , vol.194 , pp. 281-301
    • Rothstein, R.1
  • 36
    • 0025362399 scopus 로고
    • A rapid and simple method for preparation of RNA from Saccharomyces cerevisiae
    • Schmitt, M.E., Brown, T.A. and Trumpower, B.L. (1990) A rapid and simple method for preparation of RNA from Saccharomyces cerevisiae. Nucleic Acids Res., 18, 3091-3092.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 3091-3092
    • Schmitt, M.E.1    Brown, T.A.2    Trumpower, B.L.3
  • 37
    • 0028114987 scopus 로고
    • The B-type cyclin kinase inhibitor p40 (Sic1) controls the G1 to S transition in Saccharomvces cerevisiae
    • Schwob, E., Bohm, T., Mendenhall, M.D. and Nasmyth, K. (1994) The B-type cyclin kinase inhibitor p40 (Sic1) controls the G1 to S transition in Saccharomvces cerevisiae. Cell. 79, 233-244.
    • (1994) Cell. , vol.79 , pp. 233-244
    • Schwob, E.1    Bohm, T.2    Mendenhall, M.D.3    Nasmyth, K.4
  • 39
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in S. cerevisiae
    • Sikorski, R.S. and Hieter, P. (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in S. cerevisiae. Genetics, 122, 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 40
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith, D.B. and Johnson, K.S. (1988) Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene, 67, 31-38.
    • (1988) Gene , vol.67 , pp. 31-38
    • Smith, D.B.1    Johnson, K.S.2
  • 41
    • 0028843868 scopus 로고
    • The tetratricopeptide repeats of Ssn6 interact with the homeodomain of α2
    • Smith, R.L., Redd, M.J. and Johnson, A.D. (1995) The tetratricopeptide repeats of Ssn6 interact with the homeodomain of α2. Genes Dev., 9, 2903-2910.
    • (1995) Genes Dev. , vol.9 , pp. 2903-2910
    • Smith, R.L.1    Redd, M.J.2    Johnson, A.D.3
  • 42
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: Functions, mysteries, uses
    • Varshavsky, A. (1996) The N-end rule: functions, mysteries, uses. Proc. Natl Acad. Sci. USA. 93, 12142-12149.
    • (1996) Proc. Natl Acad. Sci. USA. , vol.93 , pp. 12142-12149
    • Varshavsky, A.1
  • 43
    • 0021355340 scopus 로고
    • A method for quantitative recovery of protein in dilute solution in the presence of detergents and lipids
    • Wessel, D. and Flügge, U.I. (1984) A method for quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal. Biochem., 138, 141-143.
    • (1984) Anal. Biochem. , vol.138 , pp. 141-143
    • Wessel, D.1    Flügge, U.I.2
  • 45
    • 0027284578 scopus 로고
    • Copper and gene regulation in yeast
    • Zhou, P. and Thiele, D.J. (1993) Copper and gene regulation in yeast. Biofactors, 4, 105-115.
    • (1993) Biofactors , vol.4 , pp. 105-115
    • Zhou, P.1    Thiele, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.