메뉴 건너뛰기




Volumn 265, Issue 2, 1999, Pages 680-687

Structural versatility of bovine ribonuclease A. Distinct conformers of trimeric and tetrameric aggregates of the enzyme

Author keywords

Conformational isomers; Double stranded RNA; Poly(A); RNase A aggregates; RNase A trimer and tetramer conformers

Indexed keywords

AMINO ACID; DOUBLE STRANDED RNA; POLYADENYLIC ACID; POLYCYTIDYLIC ACID; POLYURIDYLIC ACID; RIBONUCLEASE A; RNA;

EID: 0001483424     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00761.x     Document Type: Article
Times cited : (77)

References (34)
  • 1
    • 0001236723 scopus 로고
    • On the aggregation of bovine pancreatic ribonuclease
    • 1. Crestfield, A.M., Stein, W.H. & Moore, S. (1962) On the aggregation of bovine pancreatic ribonuclease. Arch. Biochem. Biophys. 1 (Suppl), 217-222.
    • (1962) Arch. Biochem. Biophys. , vol.1 , Issue.SUPPL. , pp. 217-222
    • Crestfield, A.M.1    Stein, W.H.2    Moore, S.3
  • 2
    • 0032575272 scopus 로고    scopus 로고
    • Two different forms of aggregated dimers of ribonuclease A
    • 2. Gotte, G. & Libonati, M. (1998) Two different forms of aggregated dimers of ribonuclease A. Biochim. Biophys. Acta 1386, 106-112.
    • (1998) Biochim. Biophys. Acta , vol.1386 , pp. 106-112
    • Gotte, G.1    Libonati, M.2
  • 3
    • 0027043131 scopus 로고
    • Revisiting the action of bovine ribonuclease A and pancreatic-type ribonucleases on double-stranded RNA
    • 3. Libonati, M. & Sorrentino, S. (1992) Revisiting the action of bovine ribonuclease A and pancreatic-type ribonucleases on double-stranded RNA. Mol. Cell. Biochem. 117, 139-151.
    • (1992) Mol. Cell. Biochem. , vol.117 , pp. 139-151
    • Libonati, M.1    Sorrentino, S.2
  • 4
    • 0028131158 scopus 로고
    • Human pancreatic-type and nonpancreatic-type ribonucleases: A direct side-by-side comparison of their catalytic properties
    • 4. Sorrentino, S. & Libonati, M. (1994) Human pancreatic-type and nonpancreatic-type ribonucleases: a direct side-by-side comparison of their catalytic properties. Arch. Biochem. Biophys. 312, 340-348.
    • (1994) Arch. Biochem. Biophys. , vol.312 , pp. 340-348
    • Sorrentino, S.1    Libonati, M.2
  • 5
    • 0029681842 scopus 로고    scopus 로고
    • Structure, reactivity, and biology of double-stranded RNA
    • 5. Nicholson, A.W. (1996) Structure, reactivity, and biology of double-stranded RNA. Progr. Nucleic Acids Res. Mol. Biol. 52, 1-65.
    • (1996) Progr. Nucleic Acids Res. Mol. Biol. , vol.52 , pp. 1-65
    • Nicholson, A.W.1
  • 6
    • 0030781085 scopus 로고    scopus 로고
    • Single-strand-preferring RNases degrade double-stranded RNA by destabilizing its secondary structure
    • 6. Yakovlev, G., Moiseyev, G.P., Sorrentino, S., De Prisco, R. & Libonati, M. (1997) Single-strand-preferring RNases degrade double-stranded RNA by destabilizing its secondary structure. J. Biomol. Struct. Dyn. 15, 243-250.
    • (1997) J. Biomol. Struct. Dyn. , vol.15 , pp. 243-250
    • Yakovlev, G.1    Moiseyev, G.P.2    Sorrentino, S.3    De Prisco, R.4    Libonati, M.5
  • 7
    • 0029833445 scopus 로고    scopus 로고
    • The activity on double-stranded RNA of aggregates of ribonuclease A higher than dimers increases as a function of the size of the aggregates
    • 7. Libonati, M., Bertoldi, M. & Sorrentino, S. (1996) The activity on double-stranded RNA of aggregates of ribonuclease A higher than dimers increases as a function of the size of the aggregates. Biochem. J. 318, 287-290.
    • (1996) Biochem. J. , vol.318 , pp. 287-290
    • Libonati, M.1    Bertoldi, M.2    Sorrentino, S.3
  • 8
    • 0032584210 scopus 로고    scopus 로고
    • The crystal structure of a 3D domain-swapped dimer of RNase A at 2.1 Å resolution
    • 8. Liu, Y., Hart, P.J., Schlunegger, M.P. & Eisenberg, D. (1998) The crystal structure of a 3D domain-swapped dimer of RNase A at 2.1 Å resolution. Proc. Natl Acad. Sci. USA 95, 3437-3442.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 3437-3442
    • Liu, Y.1    Hart, P.J.2    Schlunegger, M.P.3    Eisenberg, D.4
  • 9
    • 0017717820 scopus 로고
    • Polyspermine-ribonuclease prepared by cross-linkage with dimethyl suberimidate
    • 9. Wang, D. & Moore, S. (1977) Polyspermine-ribonuclease prepared by cross-linkage with dimethyl suberimidate. Biochemistry 16, 2937-2942.
    • (1977) Biochemistry , vol.16 , pp. 2937-2942
    • Wang, D.1    Moore, S.2
  • 10
    • 0017294923 scopus 로고
    • Preparation of cross-linked dimers of pancreatic ribonuclease
    • 10. Wang, D., Wilson, G. & Moore, S. (1976) Preparation of cross-linked dimers of pancreatic ribonuclease. Biochemistry 15, 660-665.
    • (1976) Biochemistry , vol.15 , pp. 660-665
    • Wang, D.1    Wilson, G.2    Moore, S.3
  • 11
    • 0000925011 scopus 로고
    • Analysis of protein conformation by gel electrophoresis
    • Creighton, T.E., ed., Oxford University Press, IRL Press, Oxford, UK
    • 11. Goldenberg, D.P. (1989) Analysis of protein conformation by gel electrophoresis. In Protein Structure. A Practical Approach (Creighton, T.E., ed.), pp. 225-250, Oxford University Press, IRL Press, Oxford, UK
    • (1989) Protein Structure. A Practical Approach , pp. 225-250
    • Goldenberg, D.P.1
  • 12
    • 0014487393 scopus 로고
    • Breakdown of double-stranded RNA by bull semen ribonuclease
    • 12. Libonati, M. & Floridi, A. (1969) Breakdown of double-stranded RNA by bull semen ribonuclease. Eur. J. Biochem. 8, 81-87.
    • (1969) Eur. J. Biochem. , vol.8 , pp. 81-87
    • Libonati, M.1    Floridi, A.2
  • 13
    • 84872631302 scopus 로고
    • A spectrophotometric method for measurement of ribonuclease activity
    • 13. Kunitz, M. (1946) A spectrophotometric method for measurement of ribonuclease activity. J. Biol. Chem. 164, 563-568.
    • (1946) J. Biol. Chem. , vol.164 , pp. 563-568
    • Kunitz, M.1
  • 14
    • 0021433730 scopus 로고
    • Isolation and characterization of monodeamidated derivatives of bovine pancreatic ribonuclease A
    • 14. Venkatesh, Y.P. & Vithayathil, P.J. (1984) Isolation and characterization of monodeamidated derivatives of bovine pancreatic ribonuclease A. Int. J. Pept. Prot. Res. 23, 494-505.
    • (1984) Int. J. Pept. Prot. Res. , vol.23 , pp. 494-505
    • Venkatesh, Y.P.1    Vithayathil, P.J.2
  • 15
    • 0024565705 scopus 로고
    • Effect of protein conformation on rate of deamidation: Ribonuclease A
    • 15. Wearne, S.J. & Creighton, T.E. (1989) Effect of protein conformation on rate of deamidation: ribonuclease A. Proteins 5, 8-12.
    • (1989) Proteins , vol.5 , pp. 8-12
    • Wearne, S.J.1    Creighton, T.E.2
  • 17
    • 0017125321 scopus 로고
    • DNA 'melting' proteins: I. Effects of bovine pancreatic ribonuclease binding on the conformation and stability of DNA
    • 17. Jensen, D.E. & von Hippel, P.H. (1976) DNA 'melting' proteins: I. Effects of bovine pancreatic ribonuclease binding on the conformation and stability of DNA. J. Biol. Chem. 251, 7198-7214.
    • (1976) J. Biol. Chem. , vol.251 , pp. 7198-7214
    • Jensen, D.E.1    Von Hippel, P.H.2
  • 20
    • 0009726906 scopus 로고
    • Action of dimeric ribonucleases on double-stranded RNA
    • 20. D'Alessio, G., Zofra, S. & Libonati, M. (1972) Action of dimeric ribonucleases on double-stranded RNA. FEBS Lett. 24, 355-358.
    • (1972) FEBS Lett. , vol.24 , pp. 355-358
    • D'Alessio, G.1    Zofra, S.2    Libonati, M.3
  • 21
    • 0016248359 scopus 로고
    • Action of dimeric hybrids of native and selectively alkylated ribonuclease A on double-stranded ribonucleic acid
    • 21. D'Alessio, G., Doskocil, J. & Libonati, M. (1974) Action of dimeric hybrids of native and selectively alkylated ribonuclease A on double-stranded ribonucleic acid. Biochem. J. 141, 317-320.
    • (1974) Biochem. J. , vol.141 , pp. 317-320
    • D'Alessio, G.1    Doskocil, J.2    Libonati, M.3
  • 22
    • 0016844511 scopus 로고
    • Degradation of double-stranded RNA by a monomeric derivative of ribonuclease BS-1
    • 22. Libonati, M., Malorni, M.C., Parente, A. & D'Alessio, G. (1975) Degradation of double-stranded RNA by a monomeric derivative of ribonuclease BS-1. Biochim. Biophys. Acta 402, 83-87.
    • (1975) Biochim. Biophys. Acta , vol.402 , pp. 83-87
    • Libonati, M.1    Malorni, M.C.2    Parente, A.3    D'Alessio, G.4
  • 23
    • 0017786095 scopus 로고
    • Correlazione fra basicità delle molecole di ribonucleasi e degradazione di RNA a doppia elica: Un ulteriore contributo
    • 23. Parente, A., Palmieri, M., De Prisco, R. & Libonati, M. (1977) Correlazione fra basicità delle molecole di ribonucleasi e degradazione di RNA a doppia elica: un ulteriore contributo. Boll. Soc. It. Biol. Sper. 53, 465-470.
    • (1977) Boll. Soc. It. Biol. Sper. , vol.53 , pp. 465-470
    • Parente, A.1    Palmieri, M.2    De Prisco, R.3    Libonati, M.4
  • 24
    • 0001375071 scopus 로고
    • The physical and chemical properties of nucleic acids
    • 24. Felsenfeld, G. & Miles, H.T. (1967) The physical and chemical properties of nucleic acids. Annu. Rev. Biochem. 36, 407-448.
    • (1967) Annu. Rev. Biochem. , vol.36 , pp. 407-448
    • Felsenfeld, G.1    Miles, H.T.2
  • 25
    • 0017139229 scopus 로고
    • Basic charges on mammalian ribonuclease molecules and the ability to attack double-stranded RNA
    • 25. Libonati, M., Furia, A. & Beintema, J.J. (1976) Basic charges on mammalian ribonuclease molecules and the ability to attack double-stranded RNA. Eur. J. Biochem. 69, 445-451.
    • (1976) Eur. J. Biochem. , vol.69 , pp. 445-451
    • Libonati, M.1    Furia, A.2    Beintema, J.J.3
  • 26
  • 27
    • 0021208349 scopus 로고
    • A ribonuclease from human seminal plasma active on double-stranded RNA
    • 27. De Prisco, R., Sorrentino, S., Leone, E. & Libonati, M. (1984) A ribonuclease from human seminal plasma active on double-stranded RNA. Biochim. Biophys. Acta 788, 356-363.
    • (1984) Biochim. Biophys. Acta , vol.788 , pp. 356-363
    • De Prisco, R.1    Sorrentino, S.2    Leone, E.3    Libonati, M.4
  • 28
    • 0031671323 scopus 로고    scopus 로고
    • Human extracellular ribonucleases: Multiplicity, molecular diversity and catalytic properties of the major RNase types
    • 28. Sorrentino, S. (1998) Human extracellular ribonucleases: multiplicity, molecular diversity and catalytic properties of the major RNase types. Cell. Mol. Life Sci. 54, 785-794.
    • (1998) Cell. Mol. Life Sci. , vol.54 , pp. 785-794
    • Sorrentino, S.1
  • 29
    • 0028275049 scopus 로고
    • Structural determinants of enzymatic processivity
    • 29. del Cardayré, S.B. & Raines, R.T. (1994) Structural determinants of enzymatic processivity. Biochemistry 33, 631-637.
    • (1994) Biochemistry , vol.33 , pp. 631-637
    • Del Cardayré, S.B.1    Raines, R.T.2
  • 30
    • 0000989565 scopus 로고
    • Hydrolysis of polyadenylic acid by pancreatic ribonuclease
    • 30. Beers, R.F. Jr (1960) Hydrolysis of polyadenylic acid by pancreatic ribonuclease. J. Biol. Chem. 235, 2393-2398.
    • (1960) J. Biol. Chem. , vol.235 , pp. 2393-2398
    • Beers R.F., Jr.1
  • 32
    • 0001005285 scopus 로고    scopus 로고
    • Ribonuclease A
    • 32. Raines, R.T. (1998) Ribonuclease A. Chem. Rev. 98, 1045-1066.
    • (1998) Chem. Rev. , vol.98 , pp. 1045-1066
    • Raines, R.T.1
  • 33
    • 0029091002 scopus 로고
    • A residue to residue hydrogen bond mediates the nucleotide specificity of ribonuclease A
    • 33. del Cardayré, S.B. & Raines, R.T. (1995) A residue to residue hydrogen bond mediates the nucleotide specificity of ribonuclease A. J. Mol. Biol. 252, 328-336.
    • (1995) J. Mol. Biol. , vol.252 , pp. 328-336
    • Del Cardayré, S.B.1    Raines, R.T.2
  • 34
    • 0033080367 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegenerative diseases: Molecular aspects
    • 34. Perutz, M.F. (1999) Glutamine repeats and neurodegenerative diseases: molecular aspects. Trends Biochem. Sci. 24, 58-63.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 58-63
    • Perutz, M.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.