메뉴 건너뛰기




Volumn 26, Issue 9, 2001, Pages 566-572

Dynamic protein interactions in the bacteriophage T4 replisome

Author keywords

[No Author keywords available]

Indexed keywords

CELL DNA; CELL PROTEIN; DNA POLYMERASE; FLUORESCENT DYE; HOLOENZYME;

EID: 0035449555     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(01)01929-6     Document Type: Review
Times cited : (25)

References (57)
  • 1
    • 0026560910 scopus 로고
    • Protein-protein interactions at a DNA replication fork: Bacteriophage T4 as a model
    • (1992) FASEB J. , vol.6 , pp. 871-878
    • Nossal, N.G.1
  • 3
    • 0026464542 scopus 로고
    • Kinetic characterization of the polymerase and exonuclease activities of the gene 43 protein of bacteriophage T4
    • (1992) Biochemistry , vol.31 , pp. 10984-10994
    • Capson, T.L.1
  • 4
    • 0034628915 scopus 로고    scopus 로고
    • Crystal structure of the DNA polymerase processivity factor of T4 bacteriophage
    • (2000) J. Mol. Biol. , vol.296 , pp. 1215-1223
    • Moarefi, I.1
  • 6
    • 0021705138 scopus 로고
    • Characterization of the stimulatory effect of T4 gene 45 protein and the gene 44/62 protein complex on DNA synthesis by T4 DNA polymerase
    • (1984) J. Mol. Biol. , vol.177 , pp. 313-327
    • Mace, D.C.1    Alberts, B.M.2
  • 7
    • 0029890834 scopus 로고    scopus 로고
    • Role of adenosine 5′-triphosphate hydrolysis in the assembly of the bacteriophage T4 DNA replication holoenzyme complex
    • (1996) Biochemistry , vol.35 , pp. 9253-9265
    • Berdis, A.J.1    Benkovic, S.J.2
  • 8
    • 0032568497 scopus 로고    scopus 로고
    • Dissecting the order of bacteriophage T4 DNA polymerase holoenzyme assembly
    • (1998) Biochemistry , vol.37 , pp. 7749-7756
    • Sexton, D.J.1
  • 10
    • 0030064447 scopus 로고    scopus 로고
    • Dual role of the 44/62 protein as a matchmaker protein and DNA polymerase chaperone during assembly of the bacteriophage T4 holoenzyme complex
    • (1996) Biochemistry , vol.35 , pp. 1084-1092
    • Kaboord, B.F.1    Benkovic, S.J.2
  • 11
    • 0025051903 scopus 로고
    • Effects of the bacteriophage T4 gene 41 and gene 32 proteins on RNA primer synthesis: Coupling of leading- and lagging-strand DNA synthesis at a replication fork
    • (1990) Biochemistry , vol.29 , pp. 1791-1798
    • Cha, T.A.1    Alberts, B.M.2
  • 12
    • 0023645225 scopus 로고
    • Bacteriophage T4 DNA primase-helicase. Characterization of oligomer synthesis by T4 61 protein alone and in conjunction with T4 41 protein
    • (1987) J. Biol. Chem. , vol.262 , pp. 10873-10878
    • Hinton, D.M.1    Nossal, N.G.2
  • 13
    • 0020364657 scopus 로고
    • Bacteriophage T4 gene 41 protein, required for the synthesis of RNA primers, is also a DNA helicase
    • (1982) J. Biol. Chem. , vol.257 , pp. 12426-12434
    • Venkatesan, M.1
  • 14
    • 0028586099 scopus 로고
    • Purification and characterization of bacteriophage T4 gene 59 protein. A DNA helicase assembly protein involved in DNA replication
    • (1994) J. Biol. Chem. , vol.269 , pp. 33049-33062
    • Barry, J.1    Alberts, B.2
  • 17
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1
  • 19
    • 0031299174 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer in studies of inter-chromophoric distances in biomolecules
    • (1997) Acta Biochim. Pol. , vol.44 , pp. 477-489
    • Lankiewicz, L.1
  • 24
    • 0034264852 scopus 로고    scopus 로고
    • A FRET-based sensor reveals large ATP hydrolysis-induced conformational changes and three distinct states of the molecular motor myosin
    • (2000) Cell , vol.102 , pp. 683-694
    • Shih, W.M.1
  • 26
    • 0032544186 scopus 로고    scopus 로고
    • Three mechanistic steps detected by FRET after presynaptic filament formation in homologous recombination. ATP hydrolysis required for release of oligonucleotide heteroduplex product from RecA
    • (1998) Biochemistry , vol.37 , pp. 11692-11706
    • Gumbs, O.H.1    Shaner, S.L.2
  • 27
    • 0032478136 scopus 로고    scopus 로고
    • Use of fluorescence resonance energy transfer to investigate the conformation of DNA substrates bound to the Klenow fragment
    • (1998) Biochemistry , vol.37 , pp. 2979-2990
    • Furey, W.S.1
  • 28
    • 0034666136 scopus 로고    scopus 로고
    • Molecular mechanism and energetics of clamp assembly in Escherichia coli. The role of ATP hydrolysis when γ complex loads β on DNA
    • (2000) J. Biol. Chem. , vol.275 , pp. 28413-28420
    • Bertram, J.G.1
  • 29
    • 0030573047 scopus 로고    scopus 로고
    • Fluorescence monitoring of T4 polymerase holoenzyme accessory protein interactions during loading of the sliding clamp onto the template-primer junction
    • (1996) J. Mol. Biol. , vol.264 , pp. 426-439
    • Latham, G.J.1
  • 30
    • 0031438369 scopus 로고    scopus 로고
    • Structural analyses of gp45 sliding clamp interactions during assembly of the bacteriophage T4 DNA polymerase holoenzyme. II. The gp44/62 clamp loader interacts with a single defined face of the sliding clamp ring
    • (1997) J. Biol. Chem. , vol.272 , pp. 31677-31684
    • Latham, G.J.1
  • 31
    • 0031451343 scopus 로고    scopus 로고
    • Structural analyses of gp45 sliding clamp interactions during assembly of the bacteriophage T4 DNA polymerase holoenzyme. III. The gp43 DNA polymerase binds to the same face of the sliding clamp as the clamp loader
    • (1997) J. Biol. Chem. , vol.272 , pp. 31685-31692
    • Latham, G.J.1
  • 32
    • 0033564238 scopus 로고    scopus 로고
    • Sliding clamp of the bacteriophage T4 polymerase has open and closed subunit interfaces in solution
    • (1999) Biochemistry , vol.38 , pp. 7696-7709
    • Alley, S.C.1
  • 33
    • 0034696523 scopus 로고    scopus 로고
    • Tracking sliding clamp opening and closing during bacteriophage T4 DNA polymerase holoenzyme assembly
    • (2000) Biochemistry , vol.39 , pp. 3076-3090
    • Alley, S.C.1
  • 35
    • 0035876386 scopus 로고    scopus 로고
    • Dissection of the ATP-driven reaction cycle of the bacteriophage T4 DNA replication processivity clamp loading system
    • (2001) J. Mol. Biol. , vol.309 , pp. 869-891
    • Pietroni, P.1
  • 36
    • 0032692565 scopus 로고    scopus 로고
    • Building a replisome from interacting pieces: Sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex
    • (1999) Cell , vol.99 , pp. 155-166
    • Shamoo, Y.1    Steitz, T.A.2
  • 37
    • 0035914387 scopus 로고    scopus 로고
    • Building a replisome solution structure by elucidation of protein-protein interactions in the bacteriophage T4 DNA polymerase holoenzyme
    • in press
    • J. Biol. Chem.
    • Alley, S.C.1
  • 38
    • 0034725870 scopus 로고    scopus 로고
    • A structural model of transcription elongation
    • (2000) Science , vol.289 , pp. 619-625
    • Korzheva, N.1
  • 40
    • 0028905501 scopus 로고
    • The phage T4-coded DNA replication helicase (gp41) forms a hexamer upon activation by nucleoside triphosphate
    • (1995) J. Biol. Chem. , vol.270 , pp. 7462-7473
    • Dong, F.1
  • 42
    • 0017079854 scopus 로고
    • Crosslinking with bifunctional reagents as a means for studying the symmetry of oligomeric proteins
    • (1976) Eur. J. Biochem. , vol.68 , pp. 373-383
    • Hajdu, J.1
  • 44
    • 0034705128 scopus 로고    scopus 로고
    • High throughput protein fold identification by using experimental constraints derived from intramolecular cross-links and mass spectrometry
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 5802-5806
    • Young, M.M.1
  • 48
    • 0033648564 scopus 로고    scopus 로고
    • Probing protein surface topology by chemical surface labeling, crosslinking, and mass spectrometry
    • (2000) Methods Mol. Biol. , vol.146 , pp. 113-131
    • Bennett, K.L.1
  • 49
    • 0031435067 scopus 로고    scopus 로고
    • Structural analyses of gp45 sliding clamp interactions during assembly of the bacteriophage T4 DNA polymerase holoenzyme. I. Conformational changes within the gp44/62-gp45-ATP complex during clamp loading
    • (1997) J. Biol. Chem. , vol.272 , pp. 31666-31676
    • Pietroni, P.1
  • 50
    • 0033607159 scopus 로고    scopus 로고
    • Opening of a monomer-monomer interface of the trimeric bacteriophage T4-coded gp45 sliding clamp is required for clamp loading onto DNA
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 12448-12453
    • Latham, G.J.1
  • 51
    • 0033609952 scopus 로고    scopus 로고
    • The carboxyl terminus of the bacteriophage T4 DNA polymerase contacts its sliding clamp at the subunit interface
    • (1999) J. Biol. Chem. , vol.274 , pp. 24485-24489
    • Alley, S.C.1
  • 53
    • 0034725391 scopus 로고    scopus 로고
    • Mapping protein-protein interactions in the bacteriophage T4 DNA polymerase holoenzyme using a novel trifunctional photocrosslinking and affinity reagent
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 6126-6127
    • Alley, S.C.1
  • 54
    • 0039251501 scopus 로고    scopus 로고
    • Simultaneous interactions of bacteriophage T4 DNA replication proteins gp59 and gp32 with single-stranded (ss) DNA. Co-modulation of ssDNA binding activities in a DNA helicase assembly intermediate
    • (1999) J. Biol. Chem. , vol.274 , pp. 22830-22838
    • Lefebvre, S.D.1
  • 55
    • 0035816713 scopus 로고    scopus 로고
    • Identification and mapping of protein-protein interactions between gp32 and gp59 by crosslinking
    • (2001) J. Biol. Chem. , vol.276 , pp. 25236-25242
    • Ishmael, F.T.1
  • 56
    • 0029052511 scopus 로고
    • Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA
    • (1995) Nature , vol.376 , pp. 362-366
    • Shamoo, Y.1
  • 57
    • 0028598643 scopus 로고
    • The gene 59 protein of bacteriophage T4 modulates the intrinsic and single-stranded DNA-stimulated ATPase activities of gene 41 protein, the T4 replicative DNA helicase
    • (1994) J. Biol. Chem. , vol.269 , pp. 33069-33081
    • Morrical, S.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.