메뉴 건너뛰기




Volumn 71, Issue 2, 2007, Pages 472-480

Biochemical analysis of the yeast proteinase inhibitor (IC) homolog ICh and its comparison with IC

Author keywords

Carboxypeptidase Y (CPY); Carboxypeptidase Y (CPY) inhibitor; Carboxypeptidase Y (CPY) inhibitor homolog; Functional characterization; Phosphatidylethanolamine binding protein (PEBP)

Indexed keywords

CARBOXYPEPTIDASE Y (CPY); CARBOXYPEPTIDASE Y (CPY) INHIBITOR HOMOLOGS; CARBOXYPEPTIDASE Y (CPY) INHIBITORS; FUNCTIONAL CHARACTERIZATION;

EID: 33847189523     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.60528     Document Type: Article
Times cited : (5)

References (40)
  • 1
    • 0016201526 scopus 로고
    • Compartmentation of inhibitors of proteinases A and B and carboxypeptidase Y in yeast
    • Matern, H., Betz, H., and Holzer, H., Compartmentation of inhibitors of proteinases A and B and carboxypeptidase Y in yeast. Biochem. Biophys. Res. Commun., 60, 1051-1057 (1974).
    • (1974) Biochem. Biophys. Res. Commun , vol.60 , pp. 1051-1057
    • Matern, H.1    Betz, H.2    Holzer, H.3
  • 2
    • 0016375955 scopus 로고
    • Isolation and characterization of the carboxypeptidase Y inhibitor from yeast
    • Matern, H., Hoffmann, M., and Holzer, H., Isolation and characterization of the carboxypeptidase Y inhibitor from yeast. Proc. Natl. Acad. Sci. USA, 71, 4874-4878 (1974).
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4874-4878
    • Matern, H.1    Hoffmann, M.2    Holzer, H.3
  • 4
    • 0032502257 scopus 로고    scopus 로고
    • A high-affinity inhibitor of yeast carboxypeptidase Y is encoded by TFS1 and shows homology to a family of lipid binding proteins
    • Bruun, A. W., Svendsen, I., Sorensen, S. O., Kielland-Brandt, M. C., and Winther, J. R., A high-affinity inhibitor of yeast carboxypeptidase Y is encoded by TFS1 and shows homology to a family of lipid binding proteins. Biochemistry, 37, 3351-3357 (1998).
    • (1998) Biochemistry , vol.37 , pp. 3351-3357
    • Bruun, A.W.1    Svendsen, I.2    Sorensen, S.O.3    Kielland-Brandt, M.C.4    Winther, J.R.5
  • 8
    • 4644250687 scopus 로고    scopus 로고
    • The stress-induced Tfs1p requires NatB-mediated acetylation to inhibit carboxypeptidase Y and to regulate the protein kinase A pathway
    • Caesar, R., and Blomberg, A., The stress-induced Tfs1p requires NatB-mediated acetylation to inhibit carboxypeptidase Y and to regulate the protein kinase A pathway. J. Biol. Chem., 279, 38532-38543 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 38532-38543
    • Caesar, R.1    Blomberg, A.2
  • 11
    • 0029123401 scopus 로고
    • From structure to function: Possible biological roles of a new widespread protein family binding hydrophobic ligands and displaying a nucleotide binding site
    • Schoentgen, F., and Jolles, P., From structure to function: possible biological roles of a new widespread protein family binding hydrophobic ligands and displaying a nucleotide binding site. FEBS Lett., 369, 22-26 (1995).
    • (1995) FEBS Lett , vol.369 , pp. 22-26
    • Schoentgen, F.1    Jolles, P.2
  • 12
    • 0021751250 scopus 로고
    • Purification and characterization of a basic 23 kDa cytosolic protein from bovine brain
    • Bernier, I., and Jolles, P., Purification and characterization of a basic 23 kDa cytosolic protein from bovine brain. Biochem. Biophys. Acta, 790, 174-181 (1984).
    • (1984) Biochem. Biophys. Acta , vol.790 , pp. 174-181
    • Bernier, I.1    Jolles, P.2
  • 13
    • 0022445734 scopus 로고
    • Ligand-binding studies with a 23 kDa protein purified from bovine brain cytosol
    • Bernier, I., Tresca, J. P., and Jolles, P., Ligand-binding studies with a 23 kDa protein purified from bovine brain cytosol. Biochem. Biophys. Acta, 871, 19-23 (1986).
    • (1986) Biochem. Biophys. Acta , vol.871 , pp. 19-23
    • Bernier, I.1    Tresca, J.P.2    Jolles, P.3
  • 14
    • 0026043708 scopus 로고
    • 23 kDa protein from rat sperm plasma membranes shows sequence similarity and phospholipid binding properties to a bovine brain cytosolic protein
    • Jones, R., and Hall, L., A 23 kDa protein from rat sperm plasma membranes shows sequence similarity and phospholipid binding properties to a bovine brain cytosolic protein. Biochem. Biophys. Acta, 1080, 78-82 (1991).
    • (1991) Biochem. Biophys. Acta , vol.1080 , pp. 78-82
    • Jones, R.1    Hall, L.A.2
  • 17
    • 0037631323 scopus 로고    scopus 로고
    • Activation of Raf-1 signaling by protein kinase C through a mechanism involving Raf kinase inhibitory protein
    • Corbit, K. C., Trakul, N., Eves, E. M., Diaz, B., Marshall, M., and Rosner, M. R., Activation of Raf-1 signaling by protein kinase C through a mechanism involving Raf kinase inhibitory protein. J. Biol. Chem., 278, 13061-13068 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 13061-13068
    • Corbit, K.C.1    Trakul, N.2    Eves, E.M.3    Diaz, B.4    Marshall, M.5    Rosner, M.R.6
  • 18
    • 0035808362 scopus 로고    scopus 로고
    • The phosphatidyletanolamine-binding protein is the prototype of a novel family of serine protease inhibitors
    • Hengst, U., Albrecht, H., Hess, D., and Monard, D., The phosphatidyletanolamine-binding protein is the prototype of a novel family of serine protease inhibitors. J. Biol. Chem., 276, 535-540 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 535-540
    • Hengst, U.1    Albrecht, H.2    Hess, D.3    Monard, D.4
  • 19
    • 0346874333 scopus 로고    scopus 로고
    • Protein kinase C switches the Raf kinase inhibitor from Raf-1 to GRK-2
    • Lorenz, K., Lohse, M. J., and Quitterer, U., Protein kinase C switches the Raf kinase inhibitor from Raf-1 to GRK-2. Nature, 426, 574-579 (2003).
    • (2003) Nature , vol.426 , pp. 574-579
    • Lorenz, K.1    Lohse, M.J.2    Quitterer, U.3
  • 20
    • 0029069889 scopus 로고
    • Sequence homology of rat and human HCNP precursor proteins, bovine phosphatidylethanolamine-binding protein and rat 23-kDa protein associated with the opioid-binding protein
    • Tohdoh, N., Tojo, S., Agui, H., and Ojika, K., Sequence homology of rat and human HCNP precursor proteins, bovine phosphatidylethanolamine-binding protein and rat 23-kDa protein associated with the opioid-binding protein. Brain Res. Mol. Brain Res., 30, 381-384 (1995).
    • (1995) Brain Res. Mol. Brain Res , vol.30 , pp. 381-384
    • Tohdoh, N.1    Tojo, S.2    Agui, H.3    Ojika, K.4
  • 22
    • 11144354419 scopus 로고    scopus 로고
    • The hippocampal cholinergic neurostimulating peptide, the N-terminal fragment of the secreted phosphatidylethanolamine-binding protein, possesses a new biological activity on cardiac physiology
    • Goumon, Y., Angelone, T., Schoentgen, F., Chasserot-Golaz, S., Almas, B., Fukami, M. M., Langley, K., Welters, I. D., Tota, B., Aunis, D., and Metz-Boutigue, M.-H., The hippocampal cholinergic neurostimulating peptide, the N-terminal fragment of the secreted phosphatidylethanolamine-binding protein, possesses a new biological activity on cardiac physiology. J. Biol. Chem., 279, 13054-13064 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 13054-13064
    • Goumon, Y.1    Angelone, T.2    Schoentgen, F.3    Chasserot-Golaz, S.4    Almas, B.5    Fukami, M.M.6    Langley, K.7    Welters, I.D.8    Tota, B.9    Aunis, D.10    Metz-Boutigue, M.-H.11
  • 23
    • 0032532743 scopus 로고    scopus 로고
    • Crystal structure of the phosphatidylethanolamine-binding protein from bovine brain: A novel structural class of phospholipid-binding proteins
    • Serre, L., Vallee, B., Bureaud, N., Schoentgen, F., and Zelwer, C., Crystal structure of the phosphatidylethanolamine-binding protein from bovine brain: a novel structural class of phospholipid-binding proteins. Structure, 15, 1255-1265 (1998).
    • (1998) Structure , vol.15 , pp. 1255-1265
    • Serre, L.1    Vallee, B.2    Bureaud, N.3    Schoentgen, F.4    Zelwer, C.5
  • 24
    • 33751092247 scopus 로고    scopus 로고
    • C, a phospahtidylethanolamine-binding protein family member
    • C, a phospahtidylethanolamine-binding protein family member. FEBS J., 273, 5374-5383 (2006).
    • (2006) FEBS J , vol.273 , pp. 5374-5383
    • Mima, J.1    Fukada, H.2    Nagayama, M.3    Ueda, M.4
  • 25
    • 0033520985 scopus 로고    scopus 로고
    • A pair of related genes with antagonistic roles in mediating flowering signals
    • Kobayashi, Y., Kaya, H., Goto, K., Iwabuchi, M., and Araki, T., A pair of related genes with antagonistic roles in mediating flowering signals. Science, 286, 1960-1962 (1999).
    • (1999) Science , vol.286 , pp. 1960-1962
    • Kobayashi, Y.1    Kaya, H.2    Goto, K.3    Iwabuchi, M.4    Araki, T.5
  • 27
    • 23644461931 scopus 로고    scopus 로고
    • Abe, M., Kobayashi, Y., Yamamoto, S., Daimon, Y., Yamaguchi, A., Ikeda, Y., Ichinoki, H., Notaguchi, M., Goto, K., and Araki, T., FD, a bZIP protein mediating signals from the floral pathway integrator FT at the shoot apex. Science, 309, 1052-1056 (2005).
    • Abe, M., Kobayashi, Y., Yamamoto, S., Daimon, Y., Yamaguchi, A., Ikeda, Y., Ichinoki, H., Notaguchi, M., Goto, K., and Araki, T., FD, a bZIP protein mediating signals from the floral pathway integrator FT at the shoot apex. Science, 309, 1052-1056 (2005).
  • 28
    • 23644440652 scopus 로고    scopus 로고
    • Integration of spatial and temporal information during floral induction in Arabidopsis
    • Wigge, P. A., Kim, M. C., Jaeger, K. E., Busch, W., Schmid, M., Lohmann, J. U., and Weigel, D., Integration of spatial and temporal information during floral induction in Arabidopsis. Science, 309, 1056-1059 (2005).
    • (2005) Science , vol.309 , pp. 1056-1059
    • Wigge, P.A.1    Kim, M.C.2    Jaeger, K.E.3    Busch, W.4    Schmid, M.5    Lohmann, J.U.6    Weigel, D.7
  • 29
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield, N., and Fasman, G. D., Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry, 8, 4108-4116 (1969).
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 30
    • 33947453415 scopus 로고
    • Spectrophotometric study of the reaction of protein sulfidryl groups with organic mercurials
    • Boyer, P. D., Spectrophotometric study of the reaction of protein sulfidryl groups with organic mercurials. J. Am. Chem. Soc., 76, 4331-4337 (1954).
    • (1954) J. Am. Chem. Soc , vol.76 , pp. 4331-4337
    • Boyer, P.D.1
  • 31
    • 0001199026 scopus 로고
    • The molecular absorpton coefficient of reduced Ellman's reagent: 3-carboxylato-4-nitrothiophenolate
    • Gething, M. J., and Davidson, B. E., The molecular absorpton coefficient of reduced Ellman's reagent: 3-carboxylato-4-nitrothiophenolate. Eur. J. Biochem., 30, 352-353 (1972).
    • (1972) Eur. J. Biochem , vol.30 , pp. 352-353
    • Gething, M.J.1    Davidson, B.E.2
  • 33
    • 0033601196 scopus 로고    scopus 로고
    • The action of N-terminal acetyltransferases on yeast ribosomal proteins
    • Arnold, R. J., Polevoda, B., Reilly, J. P., and Sherman, F., The action of N-terminal acetyltransferases on yeast ribosomal proteins. J. Biol. Chem., 274, 37035-37040 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 37035-37040
    • Arnold, R.J.1    Polevoda, B.2    Reilly, J.P.3    Sherman, F.4
  • 34
    • 0032532458 scopus 로고    scopus 로고
    • Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction
    • Banfield, M. J., Barker, J. J., Perry, A. C., and Brady, R. L., Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction. Structure, 6, 1245-1254 (1998).
    • (1998) Structure , vol.6 , pp. 1245-1254
    • Banfield, M.J.1    Barker, J.J.2    Perry, A.C.3    Brady, R.L.4
  • 35
    • 0035854480 scopus 로고    scopus 로고
    • Crystal structure of YBHB and YBCL from Escherichia coli, two bacterial homologue to a Raf kinase inhibitor protein
    • Serre, L., Pereira de Jesus, K., Zelwer, C., Bureaud, N., Schoentgen, F., and Benedetti, H., Crystal structure of YBHB and YBCL from Escherichia coli, two bacterial homologue to a Raf kinase inhibitor protein. J. Mol. Biol., 310, 617-634 (2001).
    • (2001) J. Mol. Biol , vol.310 , pp. 617-634
    • Serre, L.1    Pereira de Jesus, K.2    Zelwer, C.3    Bureaud, N.4    Schoentgen, F.5    Benedetti, H.6
  • 36
    • 0036077621 scopus 로고    scopus 로고
    • The crystal structure of PEBP-2, a homologue of the PEBP/RKIP family
    • Simister, P. C., Banfield, M. J., and Brady, R. L., The crystal structure of PEBP-2, a homologue of the PEBP/RKIP family. Acta Crystallogr. D, 58, 1077-1080 (2002).
    • (2002) Acta Crystallogr. D , vol.58 , pp. 1077-1080
    • Simister, P.C.1    Banfield, M.J.2    Brady, R.L.3
  • 37
    • 0031015315 scopus 로고    scopus 로고
    • Inflorescence commitment and architecture in Arabidopsis
    • Bradley, D., Ratcliffe, O., Vincent, C., Carpenter, R., and Coen, E., Inflorescence commitment and architecture in Arabidopsis. Science, 275, 80-83 (1997).
    • (1997) Science , vol.275 , pp. 80-83
    • Bradley, D.1    Ratcliffe, O.2    Vincent, C.3    Carpenter, R.4    Coen, E.5
  • 38
    • 4644271595 scopus 로고    scopus 로고
    • Tfs1p, a member of the PEBP family, inhibits the Ira2p but not the Ira1p Ras GTPase-activating protein in Saccharomyces cerevisiae
    • Chautard, H., Jacquet, M., Schoentgen, F., Bureaud, N., and Benedetti, H., Tfs1p, a member of the PEBP family, inhibits the Ira2p but not the Ira1p Ras GTPase-activating protein in Saccharomyces cerevisiae. Eukaryotic Cell, 3, 459-470 (2004).
    • (2004) Eukaryotic Cell , vol.3 , pp. 459-470
    • Chautard, H.1    Jacquet, M.2    Schoentgen, F.3    Bureaud, N.4    Benedetti, H.5
  • 39
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G., and Gibson, T. J., CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res., 22, 4673-4680 (1994).
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 40
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet, P., Courcelle, E., Stuart, D. I., and Metoz, F., ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics, 15, 305-308 (1999).
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.