메뉴 건너뛰기




Volumn 242, Issue 1, 1996, Pages 29-35

Exchange of regions of the carboxypeptidase Y propeptide. Sequence specificity and function in folding in vivo

Author keywords

Candida albicans; Propeptide; Protein folding; Protein transport; Saccharomyces cerevisiae

Indexed keywords

HYBRID PROTEIN; SERINE CARBOXYPEPTIDASE;

EID: 0029854775     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0029r.x     Document Type: Article
Times cited : (6)

References (29)
  • 1
    • 0027485469 scopus 로고
    • The role of pro regions in protein folding
    • Baker, D., Shiau, K. S. & Agard, D. A. (1993) The role of pro regions in protein folding, Curr. Biol. 5, 966-970.
    • (1993) Curr. Biol. , vol.5 , pp. 966-970
    • Baker, D.1    Shiau, K.S.2    Agard, D.A.3
  • 2
    • 0025370505 scopus 로고
    • Yeast carboxy-peptidase Y vacuolar targeting signal is defined by four propeptide amino acids
    • Valls, L. A., Winther, J. R. & Stevens, T. H. (1990) Yeast carboxy-peptidase Y vacuolar targeting signal is defined by four propeptide amino acids. J. Cell Biol. 111, 361-368.
    • (1990) J. Cell Biol. , vol.111 , pp. 361-368
    • Valls, L.A.1    Winther, J.R.2    Stevens, T.H.3
  • 3
    • 0024006019 scopus 로고
    • Intracellular sorting and processing of a yeast vacuolar hydrolase: Proteinase A propeptide contains vacuolar targeting information
    • Klionsky, D. J., Banta, L. M. & Emr, S. D. (1988) Intracellular sorting and processing of a yeast vacuolar hydrolase: proteinase A propeptide contains vacuolar targeting information, Mol. Cell. Biol. 8, 2105-2116.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2105-2116
    • Klionsky, D.J.1    Banta, L.M.2    Emr, S.D.3
  • 4
  • 5
    • 0028332917 scopus 로고
    • The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS10 gene
    • Marcusson, E. G., Horazdovsky, B. F., Cereghino, J. L., Gharakhanian, E. & Emr, S. D. (1994) The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS10 gene, Cell 77, 579-586.
    • (1994) Cell , vol.77 , pp. 579-586
    • Marcusson, E.G.1    Horazdovsky, B.F.2    Cereghino, J.L.3    Gharakhanian, E.4    Emr, S.D.5
  • 6
    • 0020181690 scopus 로고
    • Early stages in the yeast secretory pathway are required for transport of carboxypeptidase Y to the vacuole
    • Stevens, T. H., Esmon, B. & Schekman, R. (1982) Early stages in the yeast secretory pathway are required for transport of carboxypeptidase Y to the vacuole, Cell 30, 439-448.
    • (1982) Cell , vol.30 , pp. 439-448
    • Stevens, T.H.1    Esmon, B.2    Schekman, R.3
  • 7
    • 0017842062 scopus 로고
    • Biosynthesis of the vacuolar yeast glycoprotein carboxypeptidase Y. Conversion of precursor into the enzyme
    • Hasilik, A. & Tanner, W. (1978) Biosynthesis of the vacuolar yeast glycoprotein carboxypeptidase Y. Conversion of precursor into the enzyme, Eur. J. Biochem. 85, 599-608.
    • (1978) Eur. J. Biochem. , vol.85 , pp. 599-608
    • Hasilik, A.1    Tanner, W.2
  • 8
    • 0026004831 scopus 로고
    • Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity
    • Winther, J. R. & Sørensen, P. (1991) Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity. Proc Natl Acad. Sci. USA 88, 9330-9334.
    • (1991) Proc Natl Acad. Sci. USA , vol.88 , pp. 9330-9334
    • Winther, J.R.1    Sørensen, P.2
  • 9
    • 0028068376 scopus 로고
    • Refolding of a carboxypeptidase Y folding intermediate in vitro by low-affinity binding of the proregion
    • Winther, J. R., Sørensen, P. & Kielland-Brandt, M. C. (1994) Refolding of a carboxypeptidase Y folding intermediate in vitro by low-affinity binding of the proregion, J. Biol. Chem. 269, 22007-22013.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22007-22013
    • Winther, J.R.1    Sørensen, P.2    Kielland-Brandt, M.C.3
  • 10
    • 0028335179 scopus 로고
    • Requirement of the propeptide for in vivo formation of active yeast carboxypeptidase Y
    • Ramos, C., Winther, J. R. & Kielland-Brandt, M. C. (1994) Requirement of the propeptide for in vivo formation of active yeast carboxypeptidase Y. J. Biol. Chem. 269, 7006-7012.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7006-7012
    • Ramos, C.1    Winther, J.R.2    Kielland-Brandt, M.C.3
  • 11
    • 0026448544 scopus 로고
    • The carboxypeptidase Y-encoding gene from Candida albicans and its transcription during yeast-to-hyphae conversion
    • Mukhtar, M., Logan, D. A. & Käufer, N. F. (1992) The carboxypeptidase Y-encoding gene from Candida albicans and its transcription during yeast-to-hyphae conversion, Gene (Amst.) 121, 173-177.
    • (1992) Gene (Amst.) , vol.121 , pp. 173-177
    • Mukhtar, M.1    Logan, D.A.2    Käufer, N.F.3
  • 12
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman, F. (1991) Getting started with yeast. Methods. Enzymol. 194, 3-21.
    • (1991) Methods. Enzymol. , vol.194 , pp. 3-21
    • Sherman, F.1
  • 13
    • 0022493616 scopus 로고
    • Gene dosage-dependent secretion of yeast vacuolar carboxypeptidase Y
    • Stevens, T. H., Rothman, J. H., Payne, G. S. & Schekman, R. (1986) Gene dosage-dependent secretion of yeast vacuolar carboxypeptidase Y, J. Cell Biol. 102, 1551-1557.
    • (1986) J. Cell Biol. , vol.102 , pp. 1551-1557
    • Stevens, T.H.1    Rothman, J.H.2    Payne, G.S.3    Schekman, R.4
  • 15
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Fukuda, Y., Murata, K. & Kimura, A. (1983) Transformation of intact yeast cells treated with alkali cations, J. Bacteriol. 153, 163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 16
    • 0023652379 scopus 로고
    • Protein sorting in yeast: The localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide
    • Valls, L. A., Hunter, C. P., Rothman, J. H. & Stevens, T. H. (1987) Protein sorting in yeast: The localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide, Cell 48, 887-897.
    • (1987) Cell , vol.48 , pp. 887-897
    • Valls, L.A.1    Hunter, C.P.2    Rothman, J.H.3    Stevens, T.H.4
  • 17
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S. & Hieter, P. (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 18
    • 0027737983 scopus 로고
    • Folding and secretion of Saccharomyces cerevisiae carboxypeptidase Y are influenced by fusion with short heterologous peptides
    • Piskur, J. & Kielland-Brandt, M. C. (1993) Folding and secretion of Saccharomyces cerevisiae carboxypeptidase Y are influenced by fusion with short heterologous peptides, Biotechnol. Appl. Biochem. 18, 239-257.
    • (1993) Biotechnol. Appl. Biochem. , vol.18 , pp. 239-257
    • Piskur, J.1    Kielland-Brandt, M.C.2
  • 19
    • 0025782243 scopus 로고
    • Yeast carboxypeptidase Y requires glycosylation for efficient intracellular transport, but not for vacuolar sorting, in vivo stability, or activity
    • Winther, J. R., Stevens, T. H. & Kielland-Brandt, M. C. (1991) Yeast carboxypeptidase Y requires glycosylation for efficient intracellular transport, but not for vacuolar sorting, in vivo stability, or activity, Eur. J. Biochem. 197, 681-689.
    • (1991) Eur. J. Biochem. , vol.197 , pp. 681-689
    • Winther, J.R.1    Stevens, T.H.2    Kielland-Brandt, M.C.3
  • 20
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. & Doolittle, R. F. (1982) A simple method for displaying the hydropathic character of a protein, J. Mol. Biol. 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 21
    • 0018110116 scopus 로고
    • Prediction of secondary structure of proteins from their amino acid sequence
    • Chou, P. & Fasman, G. D. (1978) Prediction of secondary structure of proteins from their amino acid sequence. Adv. Enzymol. Relat. Areas Mol. Biol. 47, 45-148.
    • (1978) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.47 , pp. 45-148
    • Chou, P.1    Fasman, G.D.2
  • 22
    • 0030066318 scopus 로고    scopus 로고
    • Mutational analysis of the vacuolar sorting signal of procarboxypeptidase Y in yeast shows a low requirement for sequence conservation
    • van Voorst, F., Kielland-Brandt, M. C. & Winther, J. R. (1996) Mutational analysis of the vacuolar sorting signal of procarboxypeptidase Y in yeast shows a low requirement for sequence conservation, J. Biol. Chem. 271, 841-846.
    • (1996) J. Biol. Chem. , vol.271 , pp. 841-846
    • Van Voorst, F.1    Kielland-Brandt, M.C.2    Winther, J.R.3
  • 23
    • 0028284571 scopus 로고
    • Assisting spontaneity: The role of Hsp90 and small Hsps as molecular chaperones
    • Jakob, U. & Buchner, J. (1994) Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones, Trends Biochem. Sci. 19, 205-211.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 205-211
    • Jakob, U.1    Buchner, J.2
  • 25
    • 0029953675 scopus 로고    scopus 로고
    • Competition between folding and glycosylation in the endoplasmic reticulum
    • Holst, B., Bruun, A. W., Kielland-Brandt, M. C. & Winther, J. R. (1996) Competition between folding and glycosylation in the endoplasmic reticulum, EMBO J. 15, 3538-3546.
    • (1996) EMBO J. , vol.15 , pp. 3538-3546
    • Holst, B.1    Bruun, A.W.2    Kielland-Brandt, M.C.3    Winther, J.R.4
  • 26
    • 0026605509 scopus 로고
    • A protein-folding reaction under kinetic control
    • Baker, D., Sohl, J. L. & Agard, D. A. (1992) A protein-folding reaction under kinetic control, Nature 356, 263-265.
    • (1992) Nature , vol.356 , pp. 263-265
    • Baker, D.1    Sohl, J.L.2    Agard, D.A.3
  • 27
    • 0027244542 scopus 로고
    • Catalysis of a protein folding reaction: Thermodynamic and kinetic analysis of subtilisin BPN' interactions with its propeptide fragment
    • Strausberg, S., Alexander, P., Wang, L., Schwarz, F. & Bryan, P. (1993) Catalysis of a protein folding reaction: thermodynamic and kinetic analysis of subtilisin BPN' interactions with its propeptide fragment, Biochemistry 32, 8112-8119.
    • (1993) Biochemistry , vol.32 , pp. 8112-8119
    • Strausberg, S.1    Alexander, P.2    Wang, L.3    Schwarz, F.4    Bryan, P.5
  • 28
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M-J. & Sambrook, J. (1992) Protein folding in the cell. Nature 355, 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.-J.1    Sambrook, J.2
  • 29
    • 0022753540 scopus 로고
    • PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors
    • Ammerer, G., Hunter, C. P., Rothman, J. H., Saari, G. C., Valls, L. A. & Stevens, T. H. (1986) PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors. Mol. Cell. Biol. 6, 2490-2499.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 2490-2499
    • Ammerer, G.1    Hunter, C.P.2    Rothman, J.H.3    Saari, G.C.4    Valls, L.A.5    Stevens, T.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.