메뉴 건너뛰기




Volumn 364, Issue 2, 2007, Pages 159-164

A high-throughput assay shows that DNase-I binds actin monomers and polymers with similar affinity

Author keywords

Actin; Actin binding proteins; Critical concentration; Dissociation constant; DNase I; Gelsolin; Phalloidin; Ultrasensitivity

Indexed keywords

DISSOCIATION;

EID: 34147150069     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2007.02.027     Document Type: Article
Times cited : (19)

References (25)
  • 1
    • 76549250377 scopus 로고
    • Crystalline desoxyribonuclease; isolation and general properties; spectrophotometric method for the measurement of desoxyribonuclease activity
    • Kunitz M. Crystalline desoxyribonuclease; isolation and general properties; spectrophotometric method for the measurement of desoxyribonuclease activity. J. Gen. Physiol. 33 (1950) 349-362
    • (1950) J. Gen. Physiol. , vol.33 , pp. 349-362
    • Kunitz, M.1
  • 3
    • 0014045718 scopus 로고
    • Studies on the complex formation between deoxyribonuclease I and spleen inhibitor II
    • Lindberg U. Studies on the complex formation between deoxyribonuclease I and spleen inhibitor II. Biochemistry 6 (1967) 343-347
    • (1967) Biochemistry , vol.6 , pp. 343-347
    • Lindberg, U.1
  • 4
    • 0016361516 scopus 로고
    • Actin is the naturally occurring inhibitor of deoxyribonuclease I
    • Lazarides E., and Lindberg U. Actin is the naturally occurring inhibitor of deoxyribonuclease I. Proc. Natl. Acad. Sci. USA 71 (1974) 4742-4746
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4742-4746
    • Lazarides, E.1    Lindberg, U.2
  • 5
    • 0000186456 scopus 로고    scopus 로고
    • Thermal unfolding of G-actin monitored with the DNase I-inhibition assay stabilities of actin isoforms
    • Schuler H., Lindberg U., Schutt C.E., and Karlsson R. Thermal unfolding of G-actin monitored with the DNase I-inhibition assay stabilities of actin isoforms. Eur. J. Biochem. 267 (2000) 476-486
    • (2000) Eur. J. Biochem. , vol.267 , pp. 476-486
    • Schuler, H.1    Lindberg, U.2    Schutt, C.E.3    Karlsson, R.4
  • 6
    • 0034570849 scopus 로고    scopus 로고
    • Monitoring actin folding. Purification protocols for labeled proteins and binding to DNase I-sepharose beads
    • Thulasiraman V., Ferreyra R.G., and Frydman J. Monitoring actin folding. Purification protocols for labeled proteins and binding to DNase I-sepharose beads. Methods Mol. Biol. 140 (2000) 161-167
    • (2000) Methods Mol. Biol. , vol.140 , pp. 161-167
    • Thulasiraman, V.1    Ferreyra, R.G.2    Frydman, J.3
  • 7
    • 0026794025 scopus 로고
    • Removal of the amino-terminal acidic residues of yeast actin. Studies in vitro and in vivo
    • Cook R.K., Blake W.T., and Rubenstein P.A. Removal of the amino-terminal acidic residues of yeast actin. Studies in vitro and in vivo. J. Biol. Chem. 267 (1992) 9430-9436
    • (1992) J. Biol. Chem. , vol.267 , pp. 9430-9436
    • Cook, R.K.1    Blake, W.T.2    Rubenstein, P.A.3
  • 9
    • 0018827176 scopus 로고
    • The interaction of bovine pancreatic deoxyribonuclease I and skeletal muscle actin
    • Mannherz H.G., Goody R.S., Konrad M., and Nowak E. The interaction of bovine pancreatic deoxyribonuclease I and skeletal muscle actin. Eur. J. Biochem. 104 (1980) 367-379
    • (1980) Eur. J. Biochem. , vol.104 , pp. 367-379
    • Mannherz, H.G.1    Goody, R.S.2    Konrad, M.3    Nowak, E.4
  • 10
    • 0023857288 scopus 로고
    • Association of deoxyribonuclease I with the pointed ends of actin filaments in human red blood cell membrane skeletons
    • Podolski J.L., and Steck T.L. Association of deoxyribonuclease I with the pointed ends of actin filaments in human red blood cell membrane skeletons. J. Biol. Chem. 263 (1988) 638-645
    • (1988) J. Biol. Chem. , vol.263 , pp. 638-645
    • Podolski, J.L.1    Steck, T.L.2
  • 11
    • 0037428457 scopus 로고    scopus 로고
    • Structure of an F-actin trimer disrupted by gelsolin and implications for the mechanism of severing
    • Dawson J.F., Sablin E.P., Spudich J.A., and Fletterick R.J. Structure of an F-actin trimer disrupted by gelsolin and implications for the mechanism of severing. J. Biol. Chem. 278 (2003) 1229-1238
    • (2003) J. Biol. Chem. , vol.278 , pp. 1229-1238
    • Dawson, J.F.1    Sablin, E.P.2    Spudich, J.A.3    Fletterick, R.J.4
  • 13
    • 0018038933 scopus 로고
    • Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease I
    • Blikstad I., Markey F., Carlsson L., Persson T., and Lindberg U. Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease I. Cell 15 (1978) 935-943
    • (1978) Cell , vol.15 , pp. 935-943
    • Blikstad, I.1    Markey, F.2    Carlsson, L.3    Persson, T.4    Lindberg, U.5
  • 14
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich J.A., and Watt S. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246 (1971) 4866-4871
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 15
    • 0027418763 scopus 로고
    • Nucleotide binding to actin. Cation dependence of nucleotide dissociation and exchange rates
    • Kinosian H.J., Selden L.A., Estes J.E., and Gershman L.C. Nucleotide binding to actin. Cation dependence of nucleotide dissociation and exchange rates. J. Biol. Chem. 268 (1993) 8683-8691
    • (1993) J. Biol. Chem. , vol.268 , pp. 8683-8691
    • Kinosian, H.J.1    Selden, L.A.2    Estes, J.E.3    Gershman, L.C.4
  • 17
    • 0035213599 scopus 로고    scopus 로고
    • Ultrasensitivity in (supra)molecularly organized and crowded environments
    • Aon M.A., Gomez-Casati D.F., Iglesias A.A., and Cortassa S. Ultrasensitivity in (supra)molecularly organized and crowded environments. Cell Biol. Int. 25 (2001) 1091-1099
    • (2001) Cell Biol. Int. , vol.25 , pp. 1091-1099
    • Aon, M.A.1    Gomez-Casati, D.F.2    Iglesias, A.A.3    Cortassa, S.4
  • 18
    • 0034616882 scopus 로고    scopus 로고
    • Covalent binding of ATPgammaS to the nucleotide-binding site in S14C-actin
    • Schuler H., Schutt C.E., Lindberg U., and Karlsson R. Covalent binding of ATPgammaS to the nucleotide-binding site in S14C-actin. FEBS Lett. 476 (2000) 155-159
    • (2000) FEBS Lett. , vol.476 , pp. 155-159
    • Schuler, H.1    Schutt, C.E.2    Lindberg, U.3    Karlsson, R.4
  • 19
    • 0141707869 scopus 로고    scopus 로고
    • Solution properties of tetramethylrhodamine-modified G-actin
    • Kudryashov D.S., and Reisler E. Solution properties of tetramethylrhodamine-modified G-actin. Biophys. J. 85 (2003) 2466-2475
    • (2003) Biophys. J. , vol.85 , pp. 2466-2475
    • Kudryashov, D.S.1    Reisler, E.2
  • 20
    • 0028363603 scopus 로고
    • DNase I increases the rate constant of depolymerization at the pointed (-) end of actin filaments
    • Weber A., Pennise C.R., and Pring M. DNase I increases the rate constant of depolymerization at the pointed (-) end of actin filaments. Biochemistry 33 (1994) 4780-4786
    • (1994) Biochemistry , vol.33 , pp. 4780-4786
    • Weber, A.1    Pennise, C.R.2    Pring, M.3
  • 22
    • 0033662118 scopus 로고    scopus 로고
    • The role of ATP, ADP and divalent cations in the formation of binary and ternary complexes of actin, cofilin and DNase I
    • Chhabra D., Nosworthy N.J., and dos Remedios C.G. The role of ATP, ADP and divalent cations in the formation of binary and ternary complexes of actin, cofilin and DNase I. Electrophoresis 21 (2000) 3863-3869
    • (2000) Electrophoresis , vol.21 , pp. 3863-3869
    • Chhabra, D.1    Nosworthy, N.J.2    dos Remedios, C.G.3
  • 23
    • 0001424903 scopus 로고
    • An amplified sensitivity arising from covalent modification in biological systems
    • Goldbeter A., and Koshland Jr. D.E. An amplified sensitivity arising from covalent modification in biological systems. Proc. Natl. Acad. Sci. USA 78 (1981) 6840-6844
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 6840-6844
    • Goldbeter, A.1    Koshland Jr., D.E.2
  • 24
    • 2642661483 scopus 로고    scopus 로고
    • The era of pathway quantification
    • Koshland Jr. D.E. The era of pathway quantification. Science 280 (1998) 852-853
    • (1998) Science , vol.280 , pp. 852-853
    • Koshland Jr., D.E.1
  • 25
    • 0021272952 scopus 로고
    • Phalloidin enhances actin assembly by preventing monomer dissociation
    • Coluccio L.M., and Tilney L.G. Phalloidin enhances actin assembly by preventing monomer dissociation. J. Cell Biol. 99 (1984) 529-535
    • (1984) J. Cell Biol. , vol.99 , pp. 529-535
    • Coluccio, L.M.1    Tilney, L.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.