메뉴 건너뛰기




Volumn 275, Issue 5, 1996, Pages 346-354

Carboxy-Terminal CVLS-sequence-specific protein farnesyltransferase from the eyes of the shrimp Penaeus japonicus: Purification and characterization

Author keywords

[No Author keywords available]

Indexed keywords

OLIGOPEPTIDE; P21(RAS) FARNESYL PROTEIN TRANSFERASE; P21(RAS) FARNESYL-PROTEIN TRANSFERASE; TRANSFERASE;

EID: 0030219937     PISSN: 0022104X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-010X(19960801)275:5<346::AID-JEZ3>3.0.CO;2-P     Document Type: Article
Times cited : (3)

References (32)
  • 1
    • 0027298707 scopus 로고
    • c-DNA cloning and expression of the α and β subunits of rat rab geranylgeranyl transferase
    • Armstrong, S.A., M.C. Seabra, T.C. Sudhof, J.L. Goldstein, and M.S. Brown (1993) c-DNA cloning and expression of the α and β subunits of rat rab geranylgeranyl transferase. J. Biol. Chem., 268:12221-12229.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12221-12229
    • Armstrong, S.A.1    Seabra, M.C.2    Sudhof, T.C.3    Goldstein, J.L.4    Brown, M.S.5
  • 2
    • 0026667497 scopus 로고
    • Tetrapeptide inhibitors of protein farnesyltransferase: Amino-terminal substitution in phenylalanine-containing tetrapeptides restores farnesylation
    • Brown, M.S., J.L. Goldstein, K.J. Paris, J.P. Burnier, and J. Masters, Jr. (1992) Tetrapeptide inhibitors of protein farnesyltransferase: Amino-terminal substitution in phenylalanine-containing tetrapeptides restores farnesylation. Proc. Natl. Acad. Sci. U.S.A., 89:313-316.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 313-316
    • Brown, M.S.1    Goldstein, J.L.2    Paris, K.J.3    Burnier, J.P.4    Masters Jr., J.5
  • 3
    • 0025026515 scopus 로고
    • Purification and some properties of alkaline phosphatase from the hepatopancreas of the shrimp Penaeus japonicus (Crustacea: Decapoda)
    • Chuang, N.-N., and S.-L. Shih (1990) Purification and some properties of alkaline phosphatase from the hepatopancreas of the shrimp Penaeus japonicus (Crustacea: Decapoda). J. Exp. Zool., 256:1-7.
    • (1990) J. Exp. Zool. , vol.256 , pp. 1-7
    • Chuang, N.-N.1    Shih, S.-L.2
  • 4
    • 0026735063 scopus 로고
    • Protein isoprenylation and methylation at carboxy-terminal cysteine residues
    • Clarke, S. (1992) Protein isoprenylation and methylation at carboxy-terminal cysteine residues. Annu. Rev. Biochem., 61:355-386.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 355-386
    • Clarke, S.1
  • 5
    • 0027332733 scopus 로고
    • Ha gene in murine keratinocytes induces tyrosine phosphorylation and reduces activity of protein kinase. C δ
    • Ha gene in murine keratinocytes induces tyrosine phosphorylation and reduces activity of protein kinase. C δ. J. Biol. Chem., 268:26079-26081.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26079-26081
    • Denning, M.F.1    Dlugosz, A.A.2    Howett, M.K.3    Yuspa, S.H.4
  • 6
    • 0029007293 scopus 로고
    • A mechanism for post-translational modifications of proteins by yeast protein farnesyltransferase
    • Dolence, J.M., and C.D. Poulter (1995) A mechanism for post-translational modifications of proteins by yeast protein farnesyltransferase. Proc. Natl. Acad. Sci. U.S.A., 92:5008-5011.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 5008-5011
    • Dolence, J.M.1    Poulter, C.D.2
  • 7
    • 0025877861 scopus 로고
    • Ras C-terminal processing enzymes - New drug targets?
    • Gibbs, J.B. (1991) Ras C-terminal processing enzymes - new drug targets? Cell, 65:1-4.
    • (1991) Cell , vol.65 , pp. 1-4
    • Gibbs, J.B.1
  • 8
    • 0025277259 scopus 로고
    • Prenyl proteins in eukaryotic cells: A new type of membrane anchor
    • Glomset, J.A., M.H. Gelb, and C.C. Farnsworth (1990) Prenyl proteins in eukaryotic cells: A new type of membrane anchor. Trends Biochem. Sci., 15:139-142.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 139-142
    • Glomset, J.A.1    Gelb, M.H.2    Farnsworth, C.C.3
  • 10
    • 0024406286 scopus 로고
    • All Ras proteins are polyisoprenylated but only some are palmitoylated
    • Hancock, J.F., A.I. Magee, J.E. Childs, and C.J. Marshall (1989) All Ras proteins are polyisoprenylated but only some are palmitoylated. Cell, 57:1167-1177.
    • (1989) Cell , vol.57 , pp. 1167-1177
    • Hancock, J.F.1    Magee, A.I.2    Childs, J.E.3    Marshall, C.J.4
  • 11
    • 0028898579 scopus 로고
    • Ras farnesyltransferase inhibitors suppress the phenotype resulting from an activated ras mutation in Caenorhabditis elegans
    • Hara, M., and M. Han (1995) Ras farnesyltransferase inhibitors suppress the phenotype resulting from an activated ras mutation in Caenorhabditis elegans. Proc. Natl. Acad. Sci. U.S.A., 92:3333-3337.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 3333-3337
    • Hara, M.1    Han, M.2
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0018180634 scopus 로고
    • A simple method for stabilizing protein-sulfhydryl groups during SDS-gel electrophoresis
    • Lane, L.C. (1978) A simple method for stabilizing protein-sulfhydryl groups during SDS-gel electrophoresis. Anal. Biochem., 86:655-664.
    • (1978) Anal. Biochem. , vol.86 , pp. 655-664
    • Lane, L.C.1
  • 14
    • 0027215056 scopus 로고
    • Anionic glutathione S-transferases in shrimp eyes
    • Lin, K.-S., and N.-N. Chuang (1993) Anionic glutathione S-transferases in shrimp eyes. Comp. Biochem. Physiol. [B], 105:151-156.
    • (1993) Comp. Biochem. Physiol. [B] , vol.105 , pp. 151-156
    • Lin, K.-S.1    Chuang, N.-N.2
  • 17
    • 0029058605 scopus 로고
    • The myristoyl-electrostatic switch: A modulator of reversible protein-membrane interactions
    • McLaughlin, S., and A. Aderem (1995) The myristoyl-electrostatic switch: A modulator of reversible protein-membrane interactions. Trends Biochem. Sci., 20:272-276.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 272-276
    • McLaughlin, S.1    Aderem, A.2
  • 18
    • 0022699646 scopus 로고
    • Solid phase synthesis
    • Merrifield, K.R.B. (1986) Solid phase synthesis. Science, 232:341-347.
    • (1986) Science , vol.232 , pp. 341-347
    • Merrifield, K.R.B.1
  • 19
    • 0019492995 scopus 로고
    • Ultrasensitive stain for proteins in polyacrylamide gels shows regional variation in cerebrospinal fluid proteins
    • Merril, G.R., D. Goldman, S.A. Sedman, and M.H. Ebert (1981) Ultrasensitive stain for proteins in polyacrylamide gels shows regional variation in cerebrospinal fluid proteins. Science, 211:1437-1438.
    • (1981) Science , vol.211 , pp. 1437-1438
    • Merril, G.R.1    Goldman, D.2    Sedman, S.A.3    Ebert, M.H.4
  • 20
    • 0028923318 scopus 로고
    • Mutant farnesyltransferase β subunit of Saccharomyces cerevisiae that can substitute for geranylgeranyltransferase type I β subunit
    • Mitsuzawa, H., K. Esson, and F. Tamanoi (1995) Mutant farnesyltransferase β subunit of Saccharomyces cerevisiae that can substitute for geranylgeranyltransferase type I β subunit. Proc. Natl. Acad. Sci. U.S.A., 92:1704-1708.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 1704-1708
    • Mitsuzawa, H.1    Esson, K.2    Tamanoi, F.3
  • 22
    • 0027665766 scopus 로고
    • Negative growth selection against rodent fibroblasts targeted for genetic inhibition of farnesyl transferase
    • Prendergast, G.G., J.P. Davide, A. Kral, R. Diehl, J.B. Gibbs, C.A. Omer, and N.E. Kohl (1993) Negative growth selection against rodent fibroblasts targeted for genetic inhibition of farnesyl transferase. Cell Growth Differ., 4:707-713.
    • (1993) Cell Growth Differ. , vol.4 , pp. 707-713
    • Prendergast, G.G.1    Davide, J.P.2    Kral, A.3    Diehl, R.4    Gibbs, J.B.5    Omer, C.A.6    Kohl, N.E.7
  • 23
    • 0025194466 scopus 로고
    • Inhibition of purified p21 Ras farnesyl: Protein transferase by Cys-AAX tetrapeptides
    • Reiss, Y., J.L. Goldstein, M.C. Seabra, P.J. Casey, and M.S. Brown (1990) Inhibition of purified p21 Ras farnesyl: protein transferase by Cys-AAX tetrapeptides. Cell, 62:81-88.
    • (1990) Cell , vol.62 , pp. 81-88
    • Reiss, Y.1    Goldstein, J.L.2    Seabra, M.C.3    Casey, P.J.4    Brown, M.S.5
  • 25
    • 0026657881 scopus 로고
    • Divalent cation and prenyl pyrophosphate specificities of the protein farnesyltransferase from rat brain, a zinc metalloenzyme
    • Reiss, Y., M.S. Brown, and J.L. Goldstein (1992) Divalent cation and prenyl pyrophosphate specificities of the protein farnesyltransferase from rat brain, a zinc metalloenzyme. J. Biol. Chem., 267:6403-6408.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6403-6408
    • Reiss, Y.1    Brown, M.S.2    Goldstein, J.L.3
  • 26
    • 0028117574 scopus 로고
    • Farnesyl-protein transferase and geranylgeranyl-protein transferase assays using phosphocellulose paper absorption
    • Roskoski, R., Jr., P. Ritchie, and L.G. Gahn (1994) Farnesyl-protein transferase and geranylgeranyl-protein transferase assays using phosphocellulose paper absorption. Anal. Biochem., 222:275-280.
    • (1994) Anal. Biochem. , vol.222 , pp. 275-280
    • Roskoski Jr., R.1    Ritchie, P.2    Gahn, L.G.3
  • 28
    • 0025819073 scopus 로고
    • Protein farnesyltransferase and geranyl-geranyltransferase share a common α subunit
    • Seabra, M.C., Y. Reiss, P.J. Casey, M.S. Brown, and J.L. Goldstein (1991) Protein farnesyltransferase and geranyl-geranyltransferase share a common α subunit. Cell, 65:429-434.
    • (1991) Cell , vol.65 , pp. 429-434
    • Seabra, M.C.1    Reiss, Y.2    Casey, P.J.3    Brown, M.S.4    Goldstein, J.L.5
  • 29
    • 0028217907 scopus 로고
    • The binding of corticosterone to the class-theta glutathione S-trans ferase from the eyes of the shrimp Penaeus japonicus (Crustacea: Decapoda)
    • Tseng, S.-F., and N.-N. Chuang (1994) The binding of corticosterone to the class-theta glutathione S-trans ferase from the eyes of the shrimp Penaeus japonicus (Crustacea: Decapoda). Comp. Biochem. Physiol., 108B(2):215-219.
    • (1994) Comp. Biochem. Physiol. , vol.108 B , Issue.2 , pp. 215-219
    • Tseng, S.-F.1    Chuang, N.-N.2
  • 30
    • 0021528719 scopus 로고
    • Harvey murine sarcoma virus p21 ras protein: Biological and biochemical significance of the cysteine nearest the carboxy terminus
    • Willumensen, B.M., K. Norris, A.G. Papageorge, N.L. Hubbert, and D.R. Lowy (1984) Harvey murine sarcoma virus p21 ras protein: Biological and biochemical significance of the cysteine nearest the carboxy terminus. EMBO J., 3:2581-2585.
    • (1984) EMBO J. , vol.3 , pp. 2581-2585
    • Willumensen, B.M.1    Norris, K.2    Papageorge, A.G.3    Hubbert, N.L.4    Lowy, D.R.5
  • 31
    • 0026652846 scopus 로고
    • Ubiquitin-ras peptide extensions as substrates for farnesyl-protein transferase and carboxymethyltransferase
    • Yoo, Y., S. Watts, and M. Rechsteiner (1992) Ubiquitin-ras peptide extensions as substrates for farnesyl-protein transferase and carboxymethyltransferase. Biochem. J., 285:55-60.
    • (1992) Biochem. J. , vol.285 , pp. 55-60
    • Yoo, Y.1    Watts, S.2    Rechsteiner, M.3
  • 32
    • 0028582233 scopus 로고
    • Farnesylation of p21 Ras proteins in Xenopus oocytes
    • Zhao, J., H.-F. Kung, and V. Manne (1994) Farnesylation of p21 Ras proteins in Xenopus oocytes. Cell. Mol. Biol. Res., 40:313-321.
    • (1994) Cell. Mol. Biol. Res. , vol.40 , pp. 313-321
    • Zhao, J.1    Kung, H.-F.2    Manne, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.