메뉴 건너뛰기




Volumn 284, Issue 4, 1998, Pages 1075-1081

Cryo-EM imaging of the catalytic subunit of the DNA-dependent protein kinase

Author keywords

Cryo electron microscopy; DNA dependent protein kinase; DNA PK; Double strand break repair; Image reconstruction

Indexed keywords

DNA; PROTEIN KINASE;

EID: 0032509097     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2212     Document Type: Article
Times cited : (75)

References (35)
  • 4
    • 0030045003 scopus 로고    scopus 로고
    • Structure and mechanism of DNA topoisomerase II
    • Berger J. M., Gamblin S. J., Harrison S. C., Wang J. C. Structure and mechanism of DNA topoisomerase II. Nature. 379:1996;225-232.
    • (1996) Nature , vol.379 , pp. 225-232
    • Berger, J.M.1    Gamblin, S.J.2    Harrison, S.C.3    Wang, J.C.4
  • 5
    • 0026071588 scopus 로고
    • Scid mutation in mice confers hypersensitivity to ionizing radiation and a deficiency in DNA double-strand break repair
    • Biedermann K. A., Sun J. R., Giaccia A. J., Tosto L. M., Brown J. M. scid mutation in mice confers hypersensitivity to ionizing radiation and a deficiency in DNA double-strand break repair. Proc. Natl Acad. Sci. USA. 88:1991;1394-1397.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 1394-1397
    • Biedermann, K.A.1    Sun, J.R.2    Giaccia, A.J.3    Tosto, L.M.4    Brown, J.M.5
  • 6
    • 0029788520 scopus 로고    scopus 로고
    • Identification of a nonsense mutation in the carboxyl-terminal region of DNA-dependent protein kinase catalytic subunit in the scid mouse
    • Blunt T., Gell D., Fox M., Taccioli G. E., Lehmann A. R., Jackson S. P., Jeggo P. A. Identification of a nonsense mutation in the carboxyl-terminal region of DNA-dependent protein kinase catalytic subunit in the scid mouse. Proc. Natl Acad. Sci. USA. 93:1996;10285-10290.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 10285-10290
    • Blunt, T.1    Gell, D.2    Fox, M.3    Taccioli, G.E.4    Lehmann, A.R.5    Jackson, S.P.6    Jeggo, P.A.7
  • 7
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • Böttcher B., Wynne S. A., Crowther R. A. Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature. 385:1997;88-91.
    • (1997) Nature , vol.385 , pp. 88-91
    • Böttcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 9
    • 0030367822 scopus 로고    scopus 로고
    • Purification and characterization of the double-stranded DNA-activated protein kinase, DNA-PK, from human placenta
    • Chan D. W., Mody C. H., Ting N. S., Lees-Miller S. P. Purification and characterization of the double-stranded DNA-activated protein kinase, DNA-PK, from human placenta. Biochem. Cell Biol. 74:1996;67-73.
    • (1996) Biochem. Cell Biol. , vol.74 , pp. 67-73
    • Chan, D.W.1    Mody, C.H.2    Ting, N.S.3    Lees-Miller, S.P.4
  • 10
    • 0030937751 scopus 로고    scopus 로고
    • Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy
    • Conway J. F., Cheng N., Zlotnick A., Wingfield P. T., Stahl S. J., Steven A. C. Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy. Nature. 385:1997;91-94.
    • (1997) Nature , vol.385 , pp. 91-94
    • Conway, J.F.1    Cheng, N.2    Zlotnick, A.3    Wingfield, P.T.4    Stahl, S.J.5    Steven, A.C.6
  • 11
    • 0029791450 scopus 로고    scopus 로고
    • Biochemical and genetic defects in the DNA-dependent protein kinase in murine scid lymphocytes
    • Danska J. S., Holland D. P., Mariathasan S., Williams K. M., Guidos C. J. Biochemical and genetic defects in the DNA-dependent protein kinase in murine scid lymphocytes. Mol. Cell. Biol. 16:1996;5507-5517.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5507-5517
    • Danska, J.S.1    Holland, D.P.2    Mariathasan, S.3    Williams, K.M.4    Guidos, C.J.5
  • 12
    • 0032486089 scopus 로고    scopus 로고
    • Correlation of the expansion segments in mammalian rRNA with the fine structure of the 80 S ribosome; A cryoelectron microscopic reconstruction of the rabbit reticulocyte ribosome at 21 Å resolution
    • Dube P., Bacher G., Stark H., Mueller F., Zemlin F., van Heel M., Brimacombe R. Correlation of the expansion segments in mammalian rRNA with the fine structure of the 80 S ribosome; a cryoelectron microscopic reconstruction of the rabbit reticulocyte ribosome at 21 Å resolution. J. Mol. Biol. 279:1998;403-421.
    • (1998) J. Mol. Biol. , vol.279 , pp. 403-421
    • Dube, P.1    Bacher, G.2    Stark, H.3    Mueller, F.4    Zemlin, F.5    Van Heel, M.6    Brimacombe, R.7
  • 13
    • 0027048773 scopus 로고
    • Ku autoantigen is the regulatory component of a template-associated protein kinase that phosphorylates RNA polymerase II
    • Dvir A., Peterson S. R., Knuth M. W., Lu H., Dynan W. S. Ku autoantigen is the regulatory component of a template-associated protein kinase that phosphorylates RNA polymerase II. Proc. Natl Acad. Sci. USA. 89:1992;11920-11924.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 11920-11924
    • Dvir, A.1    Peterson, S.R.2    Knuth, M.W.3    Lu, H.4    Dynan, W.S.5
  • 14
    • 0027246193 scopus 로고
    • Purification and characterization of a template-associated protein kinase that phosphorylates RNA polymerase II
    • Dvir A., Stein L. Y., Calore B. L., Dynan W. S. Purification and characterization of a template-associated protein kinase that phosphorylates RNA polymerase II. J. Biol. Chem. 268:1993;10440-10447.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10440-10447
    • Dvir, A.1    Stein, L.Y.2    Calore, B.L.3    Dynan, W.S.4
  • 16
    • 0027397867 scopus 로고
    • The DNA-dependent protein kinase: Requirement for DNA ends and association with Ku antigen
    • Gottlieb T. M., Jackson S. P. The DNA-dependent protein kinase: requirement for DNA ends and association with Ku antigen. Cell. 72:1993;131-142.
    • (1993) Cell , vol.72 , pp. 131-142
    • Gottlieb, T.M.1    Jackson, S.P.2
  • 17
    • 0032549677 scopus 로고    scopus 로고
    • The small heat-shock protein, alpha B-crystalline, has a variable quaternary structure
    • Haley D. A., Horwitz J., Stewart P. L. The small heat-shock protein, alpha B-crystalline, has a variable quaternary structure. J. Mol. Biol. 277:1998;27-35.
    • (1998) J. Mol. Biol. , vol.277 , pp. 27-35
    • Haley, D.A.1    Horwitz, J.2    Stewart, P.L.3
  • 18
    • 0031930488 scopus 로고    scopus 로고
    • DNA-dependent protein kinase: DNA binding and activation in the absence of Ku
    • Hammarsten O., Chu G. DNA-dependent protein kinase: DNA binding and activation in the absence of Ku. Proc. Natl Acad. Sci. USA. 95:1998;525-530.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 525-530
    • Hammarsten, O.1    Chu, G.2
  • 21
    • 0029395076 scopus 로고
    • Menage a trois: Double strand break repair, V(D)J recombination and DNA-PK
    • Jeggo P. A., Taccioli G. E., Jackson S. P. Menage a trois: double strand break repair, V(D)J recombination and DNA-PK. Bioessays. 17:1995;949-957.
    • (1995) Bioessays , vol.17 , pp. 949-957
    • Jeggo, P.A.1    Taccioli, G.E.2    Jackson, S.P.3
  • 22
    • 0030771841 scopus 로고    scopus 로고
    • Binding of Ku and c-Abl at the kinase homology region of DNA-dependent protein kinase catalytic subunit
    • Jin S., Kharbanda S., Haver B., Kuge D., Weaver D. T. Binding of Ku and c-Abl at the kinase homology region of DNA-dependent protein kinase catalytic subunit. J. Biol. Chem. 272:1997;24763-24766.
    • (1997) J. Biol. Chem , vol.272 , pp. 24763-24766
    • Jin, S.1    Kharbanda, S.2    Haver, B.3    Kuge, D.4    Weaver, D.T.5
  • 23
    • 0031045565 scopus 로고    scopus 로고
    • PCNA: Structure, functions and interactions
    • Kelman Z. PCNA: structure, functions and interactions. Oncogene. 14:1997;629-640.
    • (1997) Oncogene , vol.14 , pp. 629-640
    • Kelman, Z.1
  • 24
    • 0026717535 scopus 로고
    • Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: A sliding DNA clamp
    • Kong X. P., Onrust R., O'Donnell M., Kuriyan J. Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp. Cell. 69:1992;425-437.
    • (1992) Cell , vol.69 , pp. 425-437
    • Kong, X.P.1    Onrust, R.2    O'Donnell, M.3    Kuriyan, J.4
  • 25
    • 0028618183 scopus 로고
    • Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
    • Krishna T. S., Kong X. P., Gary S., Burgers P. M., Kuriyan J. Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA. Cell. 79:1994;1233-1243.
    • (1994) Cell , vol.79 , pp. 1233-1243
    • Krishna, T.S.1    Kong, X.P.2    Gary, S.3    Burgers, P.M.4    Kuriyan, J.5
  • 27
    • 0028902932 scopus 로고
    • Loss of the catalytic subunit of the DNA-dependent protein kinase in DNA double-strand-break-repair mutant mammalian cells
    • Peterson S. R., Kurimasa A., Oshimura M., Dynan W. S., Bradbury E. M., Chen D. J. Loss of the catalytic subunit of the DNA-dependent protein kinase in DNA double-strand-break-repair mutant mammalian cells. Proc. Natl Acad. Sci. USA. 92:1995;3171-3174.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3171-3174
    • Peterson, S.R.1    Kurimasa, A.2    Oshimura, M.3    Dynan, W.S.4    Bradbury, E.M.5    Chen, D.J.6
  • 28
    • 0032518680 scopus 로고    scopus 로고
    • Ku protein stimulates DNA end joining by mammalian DNA ligases: A direct role for Ku in repair of DNA double-strand breaks
    • Ramsden D. A., Gellert M. Ku protein stimulates DNA end joining by mammalian DNA ligases: a direct role for Ku in repair of DNA double-strand breaks. EMBO J. 17:1998;609-614.
    • (1998) EMBO J. , vol.17 , pp. 609-614
    • Ramsden, D.A.1    Gellert, M.2
  • 29
    • 0032489634 scopus 로고    scopus 로고
    • Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA
    • Redinbo M. R., Stewart L., Kuhn P., Champoux J. J., Hol W. G. Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA. Science. 279:1998;1504-1513.
    • (1998) Science , vol.279 , pp. 1504-1513
    • Redinbo, M.R.1    Stewart, L.2    Kuhn, P.3    Champoux, J.J.4    Hol, W.G.5
  • 30
    • 0030592538 scopus 로고    scopus 로고
    • The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
    • Roseman A. M., Chen S., White H., Braig K., Saibil H. R. The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Cell. 87:1996;241-251.
    • (1996) Cell , vol.87 , pp. 241-251
    • Roseman, A.M.1    Chen, S.2    White, H.3    Braig, K.4    Saibil, H.R.5
  • 31
    • 0032170734 scopus 로고    scopus 로고
    • QVIEW: Software for rapid selection of particles from digital electron micrographs
    • Shah A. K., Stewart P. L. QVIEW: Software for rapid selection of particles from digital electron micrographs. J. Struct. Biol. 123:1998;17-21.
    • (1998) J. Struct. Biol. , vol.123 , pp. 17-21
    • Shah, A.K.1    Stewart, P.L.2
  • 33
    • 0027184774 scopus 로고
    • Difference imaging of adenovirus: Bridging the resolution gap between X-ray crystallography and electron microscopy
    • Stewart P. L., Fuller S. D., Burnett R. M. Difference imaging of adenovirus: bridging the resolution gap between X-ray crystallography and electron microscopy. EMBO J. 12:1993;2589-2599.
    • (1993) EMBO J. , vol.12 , pp. 2589-2599
    • Stewart, P.L.1    Fuller, S.D.2    Burnett, R.M.3
  • 35
    • 0030746109 scopus 로고    scopus 로고
    • Interaction of DNA-dependent protein kinase with DNA and with Ku: Biochemical and atomic-force microscopy studies
    • Yaneva M., Kowalewski T., Lieber M. R. Interaction of DNA-dependent protein kinase with DNA and with Ku: biochemical and atomic-force microscopy studies. EMBO J. 16:1997;5098-5112.
    • (1997) EMBO J. , vol.16 , pp. 5098-5112
    • Yaneva, M.1    Kowalewski, T.2    Lieber, M.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.