메뉴 건너뛰기




Volumn 71, Issue 1, 1997, Pages 444-450

Analysis of cleavage site mutations between the NC and PR Gag domains of rous sarcoma virus

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; GAG PROTEIN; ISOLEUCINE; MUTANT PROTEIN; POLYPEPTIDE; PROLINE; PROTEINASE; SYNTHETIC PEPTIDE;

EID: 0031060496     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.71.1.444-450.1997     Document Type: Article
Times cited : (11)

References (40)
  • 1
    • 0029618847 scopus 로고
    • Avian sarcoma leukemia virus protease linked to the adjacent Gag polyprotein is enzymatically active
    • Arad, G., R. Bar-Meir, N. Almog, M. Chorev, and M. Kotler. 1995. Avian sarcoma leukemia virus protease linked to the adjacent Gag polyprotein is enzymatically active. Virology 214:439-444.
    • (1995) Virology , vol.214 , pp. 439-444
    • Arad, G.1    Bar-Meir, R.2    Almog, N.3    Chorev, M.4    Kotler, M.5
  • 2
    • 0027087479 scopus 로고
    • Synthetic "interface" peptides alter dimeric assembly of the HIV-1 and 2 proteases
    • 1a.Babé, L. M., J. Rosé, and C. S. Craik. 1992. Synthetic "interface" peptides alter dimeric assembly of the HIV-1 and 2 proteases. Protein Sci. 1:1244-1253.
    • (1992) Protein Sci. , vol.1 , pp. 1244-1253
    • Babé, L.M.1    Rosé, J.2    Craik, C.S.3
  • 3
    • 0025985690 scopus 로고
    • Assembly and processing of avian retroviral Gag polyproteins containing linked protease dimers
    • Burstein, H., D. Bizub, and A. M. Skalka. 1991. Assembly and processing of avian retroviral Gag polyproteins containing linked protease dimers. J. Virol. 65:6165-6172.
    • (1991) J. Virol. , vol.65 , pp. 6165-6172
    • Burstein, H.1    Bizub, D.2    Skalka, A.M.3
  • 4
    • 0026587626 scopus 로고
    • Processing of avian retroviral Gag polyprotein precursors is blocked by a mutation in the NC-PR cleavage site
    • Burstein, H., D. Bizub, M. Kotler, G. Schatz, V. M. Vogt, and A. M. Skalka. 1992. Processing of avian retroviral Gag polyprotein precursors is blocked by a mutation in the NC-PR cleavage site. J. Virol. 66:1781-1785.
    • (1992) J. Virol. , vol.66 , pp. 1781-1785
    • Burstein, H.1    Bizub, D.2    Kotler, M.3    Schatz, G.4    Vogt, V.M.5    Skalka, A.M.6
  • 5
    • 0027232325 scopus 로고
    • Comparison of the substrate binding pockets of Rous sarcoma virus and human immunodeficiency virus type 1 proteinases
    • Cameron, C. E., B. Grinde, P. Jacques, J. Jentoft, J. Leis, A. Wlodawer, and I. T. Weber. 1993. Comparison of the substrate binding pockets of Rous sarcoma virus and human immunodeficiency virus type 1 proteinases. J. Biol. Chem. 268:11711-11720.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11711-11720
    • Cameron, C.E.1    Grinde, B.2    Jacques, P.3    Jentoft, J.4    Leis, J.5    Wlodawer, A.6    Weber, I.T.7
  • 6
    • 0028345852 scopus 로고
    • Proteolytic processing mechanisms of a miniprecursor of the aspartic protease of human immunodeficiency virus type 1
    • Co, E., G. Koelsch, Y. Lin, E. Ido, J. A. Hartsuck, and J. Tang. 1994. Proteolytic processing mechanisms of a miniprecursor of the aspartic protease of human immunodeficiency virus type 1. Biochemistry 33:1248-1254.
    • (1994) Biochemistry , vol.33 , pp. 1248-1254
    • Co, E.1    Koelsch, G.2    Lin, Y.3    Ido, E.4    Hartsuck, J.A.5    Tang, J.6
  • 7
    • 0025290527 scopus 로고
    • The structure and function of the aspartic proteinases
    • Davies, D. R. 1990. The structure and function of the aspartic proteinases. Annu. Rev. Biophys. Chem. 19:189-215.
    • (1990) Annu. Rev. Biophys. Chem. , vol.19 , pp. 189-215
    • Davies, D.R.1
  • 8
    • 0026778802 scopus 로고
    • Analysis of substrate interactions of the Rous sarcoma virus wild-type and mutant proteases and human immunodeficiency virus 1 protease using a set of systematically altered peptide substrates
    • Grinde, B., C. E. Cameron, J. Leis, I. T. Weber, A. Wlodawer, H. Burstein, and A. M. Skalka. 1992. Analysis of substrate interactions of the Rous sarcoma virus wild-type and mutant proteases and human immunodeficiency virus 1 protease using a set of systematically altered peptide substrates. J. Biol. Chem. 267:9491-9498.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9491-9498
    • Grinde, B.1    Cameron, C.E.2    Leis, J.3    Weber, I.T.4    Wlodawer, A.5    Burstein, H.6    Skalka, A.M.7
  • 9
    • 10544228656 scopus 로고    scopus 로고
    • Personal communication
    • 7a.Hrusková, O. Personal communication.
    • Hrusková, O.1
  • 10
    • 0025298840 scopus 로고
    • Structure of the aspartic protease from Rous sarcoma retrovirus refined at 1 A resolution
    • Jaskólski, M., M. Miller, J. K. M. Rao, J. Leis, and A. Wlodawer. 1990. Structure of the aspartic protease from Rous sarcoma retrovirus refined at 1 A resolution. Biochemistry 29:5889-5898.
    • (1990) Biochemistry , vol.29 , pp. 5889-5898
    • Jaskólski, M.1    Miller, M.2    Rao, J.K.M.3    Leis, J.4    Wlodawer, A.5
  • 11
    • 0020685965 scopus 로고
    • Cyanogen bromide digestion of the avian myeloblastosis virus pp19 protein: Isolation of an amino-terminal peptide that binds to viral RNA
    • Johnson, S. P., M. Veigl, T. Vanaman, and J. Leis. 1983. Cyanogen bromide digestion of the avian myeloblastosis virus pp19 protein: isolation of an amino-terminal peptide that binds to viral RNA. J. Virol. 45:876-881.
    • (1983) J. Virol. , vol.45 , pp. 876-881
    • Johnson, S.P.1    Veigl, M.2    Vanaman, T.3    Leis, J.4
  • 12
    • 0025922096 scopus 로고
    • Mutating P2 and P1 residues at cleavage junctions in the HIV-1 pol polyprotein
    • Jupp, R. A., L. H. Phylip, J. S. Mills, S. F. J. LeGrice, and J. Kay. 1991. Mutating P2 and P1 residues at cleavage junctions in the HIV-1 pol polyprotein. FEBS Lett. 283:180-184.
    • (1991) FEBS Lett. , vol.283 , pp. 180-184
    • Jupp, R.A.1    Phylip, L.H.2    Mills, J.S.3    LeGrice, S.F.J.4    Kay, J.5
  • 14
    • 0023705654 scopus 로고
    • Activity of avian retroviral protease expressed in Eshcrichia coli
    • Kotler, M., R. A. Katz, and A. M. Skalka. 1988. Activity of avian retroviral protease expressed in Eshcrichia coli. J. Virol. 62:2696-2700.
    • (1988) J. Virol. , vol.62 , pp. 2696-2700
    • Kotler, M.1    Katz, R.A.2    Skalka, A.M.3
  • 16
    • 0024518207 scopus 로고
    • Avian retroviral protease and cellular aspartic proteases are distinguished by activities on peptide substrates
    • Kotler, M., W. Danho, R. A. Katz, J. Leis, and A. M. Skalka. 1989. Avian retroviral protease and cellular aspartic proteases are distinguished by activities on peptide substrates. J. Biol. Chem. 264:3428-3435.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3428-3435
    • Kotler, M.1    Danho, W.2    Katz, R.A.3    Leis, J.4    Skalka, A.M.5
  • 17
    • 0026322839 scopus 로고
    • Human immunodeficiency virus proteinase dimer as a component of the viral polyprotein prevents particle assembly and viral infectivity
    • Kräusslich, H.-G. 1991. Human immunodeficiency virus proteinase dimer as a component of the viral polyprotein prevents particle assembly and viral infectivity. Proc. Natl. Acad. Sci. USA 88:3213-3217.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3213-3217
    • Kräusslich, H.-G.1
  • 18
    • 0027936212 scopus 로고
    • Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyprotein
    • Louis, J. M., N. T. Nashed, K. D. Parris, A. R. Kimmel, and D. M. Jerina. 1994. Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyprotein. Proc. Natl. Acad. Sci. USA 91:7970-7974.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7970-7974
    • Louis, J.M.1    Nashed, N.T.2    Parris, K.D.3    Kimmel, A.R.4    Jerina, D.M.5
  • 19
    • 0025205235 scopus 로고
    • Role of the Gag polyprotein precursor in packaging and maturation of Rous sarcoma virus genomic RNA
    • Oertle, S., and P.-F. Spahr. 1990. Role of the Gag polyprotein precursor in packaging and maturation of Rous sarcoma virus genomic RNA. J. Virol. 64:5757-5763.
    • (1990) J. Virol. , vol.64 , pp. 5757-5763
    • Oertle, S.1    Spahr, P.-F.2
  • 20
    • 0029880870 scopus 로고    scopus 로고
    • Analysis of Rous sarcoma virus Gag proteins by mass spectrometry indicates trimming by host exopeptidase
    • Pepinsky, R. B., I. A. Papayannopoulos, S. Campbell, and V. M. Vogt. 1996. Analysis of Rous sarcoma virus Gag proteins by mass spectrometry indicates trimming by host exopeptidase. J. Virol. 70:3313-3318.
    • (1996) J. Virol. , vol.70 , pp. 3313-3318
    • Pepinsky, R.B.1    Papayannopoulos, I.A.2    Campbell, S.3    Vogt, V.M.4
  • 21
    • 0029166751 scopus 로고
    • Differential proteolytic processing leads to multiple forms of the CA protein in avian sarcoma and leukemia viruses
    • Pepinsky, R. B., I. A. Papayannopoulos, E. P. Chow, N. K. Krishna, R. C. Craven, and V. M. Vogt. 1995. Differential proteolytic processing leads to multiple forms of the CA protein in avian sarcoma and leukemia viruses. J. Virol. 69:6430-6438.
    • (1995) J. Virol. , vol.69 , pp. 6430-6438
    • Pepinsky, R.B.1    Papayannopoulos, I.A.2    Chow, E.P.3    Krishna, N.K.4    Craven, R.C.5    Vogt, V.M.6
  • 22
    • 0026316549 scopus 로고
    • Analysis of retroviral protease cleavage sites reveals two types of cleavage sites and the structural requirements of the P1 amino acid
    • Pettit, S. C., J. Simsic, D. D. Loeb, L. Everitt, C. A. Hutchison III, and R. Swanstrom. 1991. Analysis of retroviral protease cleavage sites reveals two types of cleavage sites and the structural requirements of the P1 amino acid. J. Biol. Chem. 266:14539-14547.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14539-14547
    • Pettit, S.C.1    Simsic, J.2    Loeb, D.D.3    Everitt, L.4    Hutchison III, C.A.5    Swanstrom, R.6
  • 25
    • 0026345896 scopus 로고
    • A cumulative specificity model for proteases from human immunodeficiency virus types 1 and 2, inferred from statistical analysis of an extended substrate data base
    • Poorman, R. A., A. G. Tomasselli, R. L. Heinrikson, and F. J. Kézdy. 1991. A cumulative specificity model for proteases from human immunodeficiency virus types 1 and 2, inferred from statistical analysis of an extended substrate data base. J. Biol. Chem. 266:14554-14561.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14554-14561
    • Poorman, R.A.1    Tomasselli, A.G.2    Heinrikson, R.L.3    Kézdy, F.J.4
  • 28
    • 0029939026 scopus 로고    scopus 로고
    • Human immunodeficiency virus, type I protease substrate specificity is limited by interactions between substrate amino acids bound in adjacent enzyme subsites
    • Ridky, T. W., C. E. Cameron, J. Leis, T. Copeland, A. Wlodawer, I. T. Weber, and R. W. Harrison. 1996. Human immunodeficiency virus, type I protease substrate specificity is limited by interactions between substrate amino acids bound in adjacent enzyme subsites. J. Biol. Chem. 271:4709-4717.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4709-4717
    • Ridky, T.W.1    Cameron, C.E.2    Leis, J.3    Copeland, T.4    Wlodawer, A.5    Weber, I.T.6    Harrison, R.W.7
  • 29
    • 0027263501 scopus 로고
    • Regulation of autoproteolysis of the HIV-1 and HIV-2 proteases with engineered amino acid substitutions
    • Rosé, J. R., R. Salto, and C. S. Craik. 1993. Regulation of autoproteolysis of the HIV-1 and HIV-2 proteases with engineered amino acid substitutions. J. Biol. Chem. 268:11939-11945.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11939-11945
    • Rosé, J.R.1    Salto, R.2    Craik, C.S.3
  • 30
    • 0028060377 scopus 로고
    • Efficiency and selectivity of RNA packaging by Rous sarcoma virus gag deletion mutants
    • Sakalian, M., J. W. Wills, and V. M. Vogt. 1994. Efficiency and selectivity of RNA packaging by Rous sarcoma virus gag deletion mutants. J. Virol. 68:5969-5981.
    • (1994) J. Virol. , vol.68 , pp. 5969-5981
    • Sakalian, M.1    Wills, J.W.2    Vogt, V.M.3
  • 31
    • 0030586028 scopus 로고    scopus 로고
    • Proteolytic activity of the NC-PR fragment of avian sarcoma and leukemia virus Gag protein expressed in E. coli
    • Séllos-Moura, M., and V. M. Vogt. 1996. Proteolytic activity of the NC-PR fragment of avian sarcoma and leukemia virus Gag protein expressed in E. coli. Virology 221:335-345.
    • (1996) Virology , vol.221 , pp. 335-345
    • Séllos-Moura, M.1    Vogt, V.M.2
  • 32
    • 0025000261 scopus 로고
    • Properties of avian retrovirus particles defective in viral protease
    • Stewart, L., G. Schatz, and V. M. Vogt. 1990. Properties of avian retrovirus particles defective in viral protease. J. Virol. 64:5076-5092.
    • (1990) J. Virol. , vol.64 , pp. 5076-5092
    • Stewart, L.1    Schatz, G.2    Vogt, V.M.3
  • 33
    • 0026060425 scopus 로고
    • Trans-acting viral protease is necessary and sufficient for activation of avian leukosis virus reverse transcriptase
    • Stewart, L., and V. M. Vogt. 1991. trans-acting viral protease is necessary and sufficient for activation of avian leukosis virus reverse transcriptase. J. Virol. 65:6218-6231.
    • (1991) J. Virol. , vol.65 , pp. 6218-6231
    • Stewart, L.1    Vogt, V.M.2
  • 34
    • 0027429434 scopus 로고
    • Reverse transcriptase and protease activities of avian leukosis virus Gag-Pol fusion proteins expressed in insect cells
    • Stewart, L., and V. M. Vogt. 1993. Reverse transcriptase and protease activities of avian leukosis virus Gag-Pol fusion proteins expressed in insect cells. J. Virol. 67:7582-7596.
    • (1993) J. Virol. , vol.67 , pp. 7582-7596
    • Stewart, L.1    Vogt, V.M.2
  • 35
    • 0028094459 scopus 로고
    • Proteolytic cleavage at the Gag-Pol junction in avian leukosis viruses: Differences in vitro and in vivo
    • Stewart, L., and V. M. Vogt. 1994. Proteolytic cleavage at the Gag-Pol junction in avian leukosis viruses: differences in vitro and in vivo. Virology 204:45-59.
    • (1994) Virology , vol.204 , pp. 45-59
    • Stewart, L.1    Vogt, V.M.2
  • 36
    • 0016853225 scopus 로고
    • Generation of avian myeloblastosis virus structural proteins by proteolytic cleavage of a precursor polypeptide
    • Vogt, V. M., R. Eisenman, and H. Diggelmann. 1975. Generation of avian myeloblastosis virus structural proteins by proteolytic cleavage of a precursor polypeptide. J. Mol. Biol. 96:471-493.
    • (1975) J. Mol. Biol. , vol.96 , pp. 471-493
    • Vogt, V.M.1    Eisenman, R.2    Diggelmann, H.3
  • 37
    • 0027218692 scopus 로고
    • Structure-based inhibitors of HIV-1 protease
    • Wlodawer, A., and J. W. Erickson. 1993. Structure-based inhibitors of HIV-1 protease. Annu. Rev. Biochem. 62:543-585.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 543-585
    • Wlodawer, A.1    Erickson, J.W.2
  • 38
    • 0025986843 scopus 로고
    • Dissociative inhibition of dimeric enzymes: Kinetic characterization of the inhibition of HIV-1 protease by its carboxyl terminal tetrapeptide
    • Zhang, Z. Y., R. A. Poorman, L. L. Maggiora, R. L. Heinrikson, and F. J. Kezdy. 1991. Dissociative inhibition of dimeric enzymes: kinetic characterization of the inhibition of HIV-1 protease by its carboxyl terminal tetrapeptide. J. Biol. Chem. 266:15591-15594.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15591-15594
    • Zhang, Z.Y.1    Poorman, R.A.2    Maggiora, L.L.3    Heinrikson, R.L.4    Kezdy, F.J.5
  • 39
    • 0027957918 scopus 로고
    • Proteolytic activity of novel human immunodeficiency virus type 1 proteinase proteins from a precursor with a blocking mutation at the N terminus of the PR domain
    • Zybarth, G., H.-G. Kräusslich, K. Partin, and C. Carter. 1994. Proteolytic activity of novel human immunodeficiency virus type 1 proteinase proteins from a precursor with a blocking mutation at the N terminus of the PR domain. J. Virol. 68:240-250.
    • (1994) J. Virol. , vol.68 , pp. 240-250
    • Zybarth, G.1    Kräusslich, H.-G.2    Partin, K.3    Carter, C.4
  • 40
    • 0029013602 scopus 로고
    • Domains upstream of the protease (PR) in human immunodeficiency virus type 1 Gag-Pol influence PR autoprocessing
    • Zybarth, G., and C. Carter. 1995. Domains upstream of the protease (PR) in human immunodeficiency virus type 1 Gag-Pol influence PR autoprocessing. J. Virol. 69:3878-3884.
    • (1995) J. Virol. , vol.69 , pp. 3878-3884
    • Zybarth, G.1    Carter, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.