메뉴 건너뛰기




Volumn 13, Issue 5, 2004, Pages 1391-1401

Distinct conformational stability and functional activity of four highly homologous endonuclease colicins

Author keywords

Colicins; Conformational stability; Endonucleases; ESI MS; Protein folding

Indexed keywords

APOENZYME; COLICIN; ENDONUCLEASE; TRYPTOPHAN;

EID: 11144356279     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03508204     Document Type: Article
Times cited : (14)

References (44)
  • 1
    • 0015188985 scopus 로고
    • Specific inactivation of ribosomes by colicin E3 in vitro and mechanism of immunity in colicinogenic cells
    • Bowman, C.M., Sidikaro, J., and Nomura, M. 1971. Specific inactivation of ribosomes by colicin E3 in vitro and mechanism of immunity in colicinogenic cells. Nat. New Biol. 234: 133-137.
    • (1971) Nat. New Biol. , vol.234 , pp. 133-137
    • Bowman, C.M.1    Sidikaro, J.2    Nomura, M.3
  • 2
    • 0034235367 scopus 로고    scopus 로고
    • Relating electrospray ionization response to nonpolar character of small peptides
    • Cech, N.B. and Enke, C.G. 2000. Relating electrospray ionization response to nonpolar character of small peptides. Anal. Chem. 72: 2717-2723.
    • (2000) Anal. Chem. , vol.72 , pp. 2717-2723
    • Cech, N.B.1    Enke, C.G.2
  • 3
    • 0035477456 scopus 로고    scopus 로고
    • Effect of affinity for droplet surfaces on the fraction of analyte molecules charged during electrospray droplet fission
    • -. 2001. Effect of affinity for droplet surfaces on the fraction of analyte molecules charged during electrospray droplet fission. Anal. Chem. 73: 4632-4639.
    • (2001) Anal. Chem. , vol.73 , pp. 4632-4639
  • 4
    • 0036440979 scopus 로고    scopus 로고
    • The crystal structure of the nuclease domain of colicin E7 suggests a mechanism for binding to double-stranded DNA by the H-N-H endonucleases
    • Cheng, Y.S., Hsia, K.C., Doudeva, L.G., Chak, K.F., and Yuan, H.S. 2002. The crystal structure of the nuclease domain of colicin E7 suggests a mechanism for binding to double-stranded DNA by the H-N-H endonucleases. J. Mol. Biol. 324: 227-236.
    • (2002) J. Mol. Biol. , vol.324 , pp. 227-236
    • Cheng, Y.S.1    Hsia, K.C.2    Doudeva, L.G.3    Chak, K.F.4    Yuan, H.S.5
  • 5
    • 0025674590 scopus 로고
    • Probing conformational changes in proteins by mass spectrometry
    • Chowdhury, S.K., Katta, V., and Chait, B.T. 1990. Probing conformational changes in proteins by mass spectrometry. J. Am. Chem. Soc. 112: 9012-9013.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 9012-9013
    • Chowdhury, S.K.1    Katta, V.2    Chait, B.T.3
  • 6
    • 0026042814 scopus 로고
    • Investigation of the specificity of the interaction between colicin E9 and its immunity protein by site-directed mutagenesis
    • Curtis, M.D. and James, R. 1991. Investigation of the specificity of the interaction between colicin E9 and its immunity protein by site-directed mutagenesis. Mol. Microbiol. 5: 2727-2733.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2727-2733
    • Curtis, M.D.1    James, R.2
  • 7
    • 0032823422 scopus 로고    scopus 로고
    • Thermal stability of a flavoprotein assessed from associative analysis of polarized time-resolved fluorescence spectroscopy
    • Digris, A.V., Skakun, V.V., Novikov, E.G., van Hoek, A., Claiborne, A., and Visser, A.J.W.G. 1999. Thermal stability of a flavoprotein assessed from associative analysis of polarized time-resolved fluorescence spectroscopy. Eur. Biophys. J. 28: 526-531.
    • (1999) Eur. Biophys. J. , vol.28 , pp. 526-531
    • Digris, A.V.1    Skakun, V.V.2    Novikov, E.G.3    Van Hoek, A.4    Claiborne, A.5    Visser, A.J.W.G.6
  • 8
    • 0035886952 scopus 로고    scopus 로고
    • Detection of multiple protein conformational ensembles in solution via deconvolution of charge-state distributions in ESI MS
    • Dobo, A. and Kaltashov, I.A. 2001. Detection of multiple protein conformational ensembles in solution via deconvolution of charge-state distributions in ESI MS. Anal. Chem. 73: 4763-4773.
    • (2001) Anal. Chem. , vol.73 , pp. 4763-4773
    • Dobo, A.1    Kaltashov, I.A.2
  • 9
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn, J.B., Mann, M., Meng, C.K., Wong, S.F., and Whitehouse, C.M. 1989. Electrospray ionization for mass spectrometry of large biomolecules. Science 246: 64-71.
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 10
    • 0037180394 scopus 로고    scopus 로고
    • Catalytic mechanisms of restriction and homing endonucleases
    • Galburt, E.A. and Stoddard, B.L. 2002. Catalytic mechanisms of restriction and homing endonucleases. Biochemistry 41: 13851-13860.
    • (2002) Biochemistry , vol.41 , pp. 13851-13860
    • Galburt, E.A.1    Stoddard, B.L.2
  • 12
    • 4444243006 scopus 로고    scopus 로고
    • Investigation of intact protein complexes by mass spectrometry
    • in press
    • Heck, A.J.R. and Van den Heuvel, R.H.H. Investigation of intact protein complexes by mass spectrometry. Mass Spectrom. Rev. (in press).
    • Mass Spectrom. Rev.
    • Heck, A.J.R.1    Van Den Heuvel, R.H.H.2
  • 13
    • 0035861570 scopus 로고    scopus 로고
    • Dynamic protein complexes: Insights from mass spectrometry
    • Hernandez, H. and Robinson, C.V. 2001. Dynamic protein complexes: Insights from mass spectrometry. J. Biol. Chem. 276: 46685-46688.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46685-46688
    • Hernandez, H.1    Robinson, C.V.2
  • 14
    • 0029949518 scopus 로고    scopus 로고
    • The biology of E colicins: Paradigms and paradoxes
    • James, R., Kleanthous, C., and Moore, G.R. 1996. The biology of E colicins: Paradigms and paradoxes. Microbiology 142: 1569-1580.
    • (1996) Microbiology , vol.142 , pp. 1569-1580
    • James, R.1    Kleanthous, C.2    Moore, G.R.3
  • 15
    • 0036589253 scopus 로고    scopus 로고
    • Killing of E. coli cells by E group nuclease colicins
    • James, R., Penfold, C.N., Moore, G.R., and Kleanthous, C. 2002. Killing of E. coli cells by E group nuclease colicins. Biochimie 84: 381-389.
    • (2002) Biochimie , vol.84 , pp. 381-389
    • James, R.1    Penfold, C.N.2    Moore, G.R.3    Kleanthous, C.4
  • 16
    • 0035984339 scopus 로고    scopus 로고
    • Studies of biomolecular conformations and conformational dynamics by mass spectrometry
    • Kaltashov, I.A. and Eyles, S.J. 2002. Studies of biomolecular conformations and conformational dynamics by mass spectrometry. Mass Spectrom. Rev. 21: 37-71.
    • (2002) Mass Spectrom. Rev. , vol.21 , pp. 37-71
    • Kaltashov, I.A.1    Eyles, S.J.2
  • 17
    • 0037072261 scopus 로고    scopus 로고
    • Multistep binding of transition metals to the H-N-H endonuclease toxin colicin E9
    • Keeble, A.H., Hemmings, A.M., James, R., Moore, G.R., and Kleanthous, C. 2002. Multistep binding of transition metals to the H-N-H endonuclease toxin colicin E9. Biochemistry 41: 10234-10244.
    • (2002) Biochemistry , vol.41 , pp. 10234-10244
    • Keeble, A.H.1    Hemmings, A.M.2    James, R.3    Moore, G.R.4    Kleanthous, C.5
  • 19
    • 0002347541 scopus 로고    scopus 로고
    • The crystal structure of the DNase domain of colicin E7 in complex with its inhibitor Im7 protein
    • Ko, T.P., Liao, C.C., Ku, W.Y., Chak, K.F., and Yuan, H.S. 1999. The crystal structure of the DNase domain of colicin E7 in complex with its inhibitor Im7 protein. Structure Fold. Des. 7: 91-102.
    • (1999) Structure Fold. Des. , vol.7 , pp. 91-102
    • Ko, T.P.1    Liao, C.C.2    Ku, W.Y.3    Chak, K.F.4    Yuan, H.S.5
  • 21
    • 0038271924 scopus 로고    scopus 로고
    • Protein-folding kinetics and mechanisms studied by pulse-labeling and mass spectrometry
    • Konermann, L. and Simmons, D.A. 2003. Protein-folding kinetics and mechanisms studied by pulse-labeling and mass spectrometry. Mass Spectrom. Rev. 22: 1-26.
    • (2003) Mass Spectrom. Rev. , vol.22 , pp. 1-26
    • Konermann, L.1    Simmons, D.A.2
  • 22
    • 0033459467 scopus 로고    scopus 로고
    • Structural parsimony in endonuclease active sites: Should the number of homing endonuclease families be redefined?
    • Kuhlmann, U.C., Moore, G.R., James, R., Kleanthous, C., and Hemmings, A.M. 1999. Structural parsimony in endonuclease active sites: Should the number of homing endonuclease families be redefined? FEBS Lett. 463: 1-2.
    • (1999) FEBS Lett. , vol.463 , pp. 1-2
    • Kuhlmann, U.C.1    Moore, G.R.2    James, R.3    Kleanthous, C.4    Hemmings, A.M.5
  • 23
    • 0034283147 scopus 로고    scopus 로고
    • Specificity in protein-protein interactions: The structural basis for dual recognition in endonuclease colicin-immunity protein complexes
    • Kuhlmann, U.C., Pommer, A.J., Moore, G.R., James, R., and Kleanthous, C. 2000. Specificity in protein-protein interactions: The structural basis for dual recognition in endonuclease colicin-immunity protein complexes. J. Mol. Biol. 301: 1163-1178.
    • (2000) J. Mol. Biol. , vol.301 , pp. 1163-1178
    • Kuhlmann, U.C.1    Pommer, A.J.2    Moore, G.R.3    James, R.4    Kleanthous, C.5
  • 25
    • 0030621966 scopus 로고    scopus 로고
    • Studying noncovalent protein complexes by electrospray ionization mass spectrometry
    • Loo, J.A. 1997. Studying noncovalent protein complexes by electrospray ionization mass spectrometry. Mass Spectrom. Rev. 16: 1-23.
    • (1997) Mass Spectrom. Rev. , vol.16 , pp. 1-23
    • Loo, J.A.1
  • 26
    • 0035814768 scopus 로고    scopus 로고
    • Probing protein-metal ion interactions by electrospray ionization mass spectrometry: Enolase and nucleocapsid protein
    • -. 2001. Probing protein-metal ion interactions by electrospray ionization mass spectrometry: Enolase and nucleocapsid protein. Int. J. Mass Spectrom. 204: 113-123.
    • (2001) Int. J. Mass Spectrom. , vol.204 , pp. 113-123
  • 27
    • 0027344496 scopus 로고
    • Heat-induced conformational changes in proteins studied by electrospray ionization mass spectrometry
    • Mirza, U.A., Cohen, S.L., and Chait, B.T. 1993. Heat-induced conformational changes in proteins studied by electrospray ionization mass spectrometry. Anal. Chem. 65: 1-6.
    • (1993) Anal. Chem. , vol.65 , pp. 1-6
    • Mirza, U.A.1    Cohen, S.L.2    Chait, B.T.3
  • 30
    • 0033605708 scopus 로고    scopus 로고
    • A cytotoxic ribonuclease targeting specific transfer RNA anticodons
    • Ogawa, T., Tomita, K., Ueda, T., Watanabe, K., Uozumi, T., and Masaki, H. 1999. A cytotoxic ribonuclease targeting specific transfer RNA anticodons. Science 283: 2097-2100.
    • (1999) Science , vol.283 , pp. 2097-2100
    • Ogawa, T.1    Tomita, K.2    Ueda, T.3    Watanabe, K.4    Uozumi, T.5    Masaki, H.6
  • 31
    • 0032169937 scopus 로고    scopus 로고
    • Enzymological characterization of the nuclease domain from the bacterial toxin colicin E9 from Escherichia coli
    • Pommer, A.J., Wallis, R., Moore, G.R., James, R., and Kleanthous, C. 1998. Enzymological characterization of the nuclease domain from the bacterial toxin colicin E9 from Escherichia coli. Biochem. J. 334: 387-392.
    • (1998) Biochem. J. , vol.334 , pp. 387-392
    • Pommer, A.J.1    Wallis, R.2    Moore, G.R.3    James, R.4    Kleanthous, C.5
  • 34
    • 33748233229 scopus 로고    scopus 로고
    • Electrospray mass spectrometry of biomolecular complexes with noncovalent interactions - New analytical perspectives for supramolecular chemistry and molecular recognition processes
    • Przybylski, M. and Glocker, M.O. 1996. Electrospray mass spectrometry of biomolecular complexes with noncovalent interactions-New analytical perspectives for supramolecular chemistry and molecular recognition processes. Angew. Chem. Int. Ed. Engl. 35: 806-826.
    • (1996) Angew. Chem. Int. Ed. Engl. , vol.35 , pp. 806-826
    • Przybylski, M.1    Glocker, M.O.2
  • 35
    • 0042573738 scopus 로고    scopus 로고
    • Experimental evidence for a ββα-Me-finger nuclease motif to represent the active site of the caspase-activated DNase
    • Scholz, S.R., Korn, C., Bujnicki, J.M., Gimadutdinow, O., Pingoud, A., and Meiss, G. 2003. Experimental evidence for a ββα-Me-finger nuclease motif to represent the active site of the caspase-activated DNase. Biochemistry 42: 9288-9294.
    • (2003) Biochemistry , vol.42 , pp. 9288-9294
    • Scholz, S.R.1    Korn, C.2    Bujnicki, J.M.3    Gimadutdinow, O.4    Pingoud, A.5    Meiss, G.6
  • 36
    • 0034282637 scopus 로고    scopus 로고
    • The stabilities of mammalian apomyoglobins vary over a 600-fold range and can be enhanced by comparative mutagenesis
    • Scott, E.E., Paster, E.V., and Olson, J.S. 2000. The stabilities of mammalian apomyoglobins vary over a 600-fold range and can be enhanced by comparative mutagenesis. J. Biol. Chem. 275: 27129-27136.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27129-27136
    • Scott, E.E.1    Paster, E.V.2    Olson, J.S.3
  • 37
    • 0025424768 scopus 로고
    • New developments in biochemical mass spectrometry: Electrospray ionization
    • Smith, R.D., Loo, J.A., Edmonds, C.G., Barinaga, C.J., and Udseth, H.R. 1990. New developments in biochemical mass spectrometry: Electrospray ionization. Anal. Chem. 62: 882-899.
    • (1990) Anal. Chem. , vol.62 , pp. 882-899
    • Smith, R.D.1    Loo, J.A.2    Edmonds, C.G.3    Barinaga, C.J.4    Udseth, H.R.5
  • 38
    • 0036084606 scopus 로고    scopus 로고
    • Probing metal ion binding and conformational properties of the colicin E9 endonuclease by electrospray ionization time-of-flight mass spectrometry
    • van den Bremer, E.T.J., Jiskoot, W., James, R., Moore, G.R., Kleanthous, C., Heck, A.J.R., and Maier, C.S. 2002. Probing metal ion binding and conformational properties of the colicin E9 endonuclease by electrospray ionization time-of-flight mass spectrometry. Protein Sci. 11: 1738-1752.
    • (2002) Protein Sci. , vol.11 , pp. 1738-1752
    • Van Den Bremer, E.T.J.1    Jiskoot, W.2    James, R.3    Moore, G.R.4    Kleanthous, C.5    Heck, A.J.R.6    Maier, C.S.7
  • 39
    • 0033532556 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry in the study of biomolecular non-covalent interactions
    • Veenstra, T.D. 1999. Electrospray ionization mass spectrometry in the study of biomolecular non-covalent interactions. Biophys. Chem. 79: 63-79.
    • (1999) Biophys. Chem. , vol.79 , pp. 63-79
    • Veenstra, T.D.1
  • 41
    • 0037100603 scopus 로고    scopus 로고
    • Mutagenic scan of the H-N-H motif of colicin E9: Implications for the mechanistic enzymology of colicins, homing enzymes and apoptotic endonucleases
    • Walker, D.C., Georgiou, T., Pommer, A.J., Walker, D., Moore, G.R., Kleanthous, C., and James, R. 2002. Mutagenic scan of the H-N-H motif of colicin E9: Implications for the mechanistic enzymology of colicins, homing enzymes and apoptotic endonucleases. Nucleic Acids Res. 30: 3225-3234.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3225-3234
    • Walker, D.C.1    Georgiou, T.2    Pommer, A.J.3    Walker, D.4    Moore, G.R.5    Kleanthous, C.6    James, R.7
  • 42
    • 0345701261 scopus 로고    scopus 로고
    • The Thermodynamic consequences of bipartite immunity protein binding to the ribosomal ribonuclease colicin E3
    • Walker, D., Moore, G.R., James, R., and Kleanthous, C. 2003. The Thermodynamic consequences of bipartite immunity protein binding to the ribosomal ribonuclease colicin E3. Biochemistry 42: 4161-4171.
    • (2003) Biochemistry , vol.42 , pp. 4161-4171
    • Walker, D.1    Moore, G.R.2    James, R.3    Kleanthous, C.4
  • 43
    • 0028866770 scopus 로고
    • Protein-protein interactions in colicin E9 DNase-immunity protein complexes. 1. Diffusion-controlled association and femtomolar binding for the cognate complex
    • Wallis, R., Moore, G.R., James, R., and Kleanthous, C. 1995a. Protein-protein interactions in colicin E9 DNase-immunity protein complexes. 1. Diffusion-controlled association and femtomolar binding for the cognate complex. Biochemistry 34: 13743-13750.
    • (1995) Biochemistry , vol.34 , pp. 13743-13750
    • Wallis, R.1    Moore, G.R.2    James, R.3    Kleanthous, C.4
  • 44
    • 0028886403 scopus 로고
    • Protein-protein interactions in colicin E9 DNase-immunity protein complexes. 2. Cognate and noncognate interactions that span the millimolar to femtomolar affinity range
    • Wallis, R., Leung, K.Y., Pommer, A.J., Videler, H., Moore, G.R., James, R., and Kleanthous, C. 1995b. Protein-protein interactions in colicin E9 DNase-immunity protein complexes. 2. Cognate and noncognate interactions that span the millimolar to femtomolar affinity range. Biochemistry 34: 13751-13759.
    • (1995) Biochemistry , vol.34 , pp. 13751-13759
    • Wallis, R.1    Leung, K.Y.2    Pommer, A.J.3    Videler, H.4    Moore, G.R.5    James, R.6    Kleanthous, C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.