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Volumn 21, Issue 10, 2005, Pages 568-572

The promiscuous primase

Author keywords

[No Author keywords available]

Indexed keywords

DNA DIRECTED DNA POLYMERASE; DNA POLYMERASE; DNA PRIMASE; LIGASE;

EID: 24644454684     PISSN: 01689525     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tig.2005.07.010     Document Type: Review
Times cited : (42)

References (31)
  • 2
    • 0035976978 scopus 로고    scopus 로고
    • The archaeal DNA primase - Biochemical characterization of the p41-p46 complex from Pyrococcus furiosus
    • L.D. Liu The archaeal DNA primase - biochemical characterization of the p41-p46 complex from Pyrococcus furiosus J. Biol. Chem. 276 2001 45484 45490
    • (2001) J. Biol. Chem. , vol.276 , pp. 45484-45490
    • Liu, L.D.1
  • 3
    • 0035916786 scopus 로고    scopus 로고
    • Archaeal primase: Bridging the gap between RNA and DNA polymerases
    • A.A. Bocquier Archaeal primase: bridging the gap between RNA and DNA polymerases Curr. Biol. 11 2001 452 456
    • (2001) Curr. Biol. , vol.11 , pp. 452-456
    • Bocquier, A.A.1
  • 4
    • 9244224132 scopus 로고    scopus 로고
    • The heterodimeric primase of the hyperthermophilic archaeon Sulfolobus solfataricus possesses DNA and RNA primase, polymerase and 3′-terminal nucleotidyl transferase activities
    • S.H. Lao-Sirieix, and S.D. Bell The heterodimeric primase of the hyperthermophilic archaeon Sulfolobus solfataricus possesses DNA and RNA primase, polymerase and 3′-terminal nucleotidyl transferase activities J. Mol. Biol. 344 2004 1251 1263
    • (2004) J. Mol. Biol. , vol.344 , pp. 1251-1263
    • Lao-Sirieix, S.H.1    Bell, S.D.2
  • 5
    • 0037295722 scopus 로고    scopus 로고
    • Identification of short 'eukaryotic' Okazaki fragments synthesized from a prokaryotic replication origin
    • F. Matsunaga Identification of short 'eukaryotic' Okazaki fragments synthesized from a prokaryotic replication origin EMBO Rep. 4 2003 154 158
    • (2003) EMBO Rep. , vol.4 , pp. 154-158
    • Matsunaga, F.1
  • 6
    • 4944238318 scopus 로고    scopus 로고
    • The DNA primase of Sulfolobus solfataricus is activated by substrates containing a thymine-rich bubble and has a 3′-terminal nucleotidyl-transferase activity
    • M. De Falco The DNA primase of Sulfolobus solfataricus is activated by substrates containing a thymine-rich bubble and has a 3′-terminal nucleotidyl-transferase activity Nucleic Acids Res. 32 2004 5223 5230
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5223-5230
    • De Falco, M.1
  • 7
    • 0035169689 scopus 로고    scopus 로고
    • Crystal structure of a DNA-dependent RNA polymerase (DNA primase)
    • M.A. Augustin Crystal structure of a DNA-dependent RNA polymerase (DNA primase) Nat. Struct. Biol. 8 2001 57 61
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 57-61
    • Augustin, M.A.1
  • 8
    • 0346025633 scopus 로고    scopus 로고
    • Crystal structure of the Pyrococcus horikoshii DNA primase-UTP complex: Implications for the mechanism of primer synthesis
    • N. Ito Crystal structure of the Pyrococcus horikoshii DNA primase-UTP complex: implications for the mechanism of primer synthesis Genes Cells 8 2003 913 923
    • (2003) Genes Cells , vol.8 , pp. 913-923
    • Ito, N.1
  • 9
    • 0034653865 scopus 로고    scopus 로고
    • Structure of the zinc-binding domain of Bacillus stearothermophilus DNA primase
    • H. Pan, and D.B. Wigley Structure of the zinc-binding domain of Bacillus stearothermophilus DNA primase Structure 8 2000 231 239
    • (2000) Structure , vol.8 , pp. 231-239
    • Pan, H.1    Wigley, D.B.2
  • 10
    • 0028606031 scopus 로고
    • A unified polymerase mechanism for nonhomologous DNA and RNA polymerases
    • T.A. Steitz A unified polymerase mechanism for nonhomologous DNA and RNA polymerases Science 266 1994 2022 2025
    • (1994) Science , vol.266 , pp. 2022-2025
    • Steitz, T.A.1
  • 11
    • 0028136070 scopus 로고
    • Crystal-structure of rat DNA-polymerase-beta - Evidence for a common polymerase mechanism
    • M.R. Sawaya Crystal-structure of rat DNA-polymerase-beta - evidence for a common polymerase mechanism Science 264 1994 1930 1935
    • (1994) Science , vol.264 , pp. 1930-1935
    • Sawaya, M.R.1
  • 12
    • 0038577149 scopus 로고    scopus 로고
    • A novel type of replicative enzyme harbouring ATPase, primase and DNA polymerase activity
    • G. Lipps A novel type of replicative enzyme harbouring ATPase, primase and DNA polymerase activity EMBO J. 22 2003 2516 2525
    • (2003) EMBO J. , vol.22 , pp. 2516-2525
    • Lipps, G.1
  • 13
    • 0742305294 scopus 로고    scopus 로고
    • Structure of a bifunctional DNA primase-polymerase
    • G. Lipps Structure of a bifunctional DNA primase-polymerase Nat. Struct. Mol. Biol. 11 2004 157 162
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 157-162
    • Lipps, G.1
  • 14
    • 12944319325 scopus 로고    scopus 로고
    • Eukaryotic/archaeal primase and MCM proteins encoded in a bacteriophage genome
    • A.T. McGeoch, and S.D. Bell Eukaryotic/archaeal primase and MCM proteins encoded in a bacteriophage genome Cell 120 2005 167 168
    • (2005) Cell , vol.120 , pp. 167-168
    • McGeoch, A.T.1    Bell, S.D.2
  • 15
    • 0033564245 scopus 로고    scopus 로고
    • Arg304 of human DNA primase is a key contributor to catalysis and NTP binding: Primase and the family X polymerases share significant sequence homology
    • B.W. Kirk, and R.D. Kuchta Arg304 of human DNA primase is a key contributor to catalysis and NTP binding: primase and the family X polymerases share significant sequence homology Biochemistry 38 1999 7727 7736
    • (1999) Biochemistry , vol.38 , pp. 7727-7736
    • Kirk, B.W.1    Kuchta, R.D.2
  • 16
    • 0035997349 scopus 로고    scopus 로고
    • Eukaryotic DNA polymerases
    • U. Hubscher Eukaryotic DNA polymerases Annu. Rev. Biochem. 71 2002 133 163
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 133-163
    • Hubscher, U.1
  • 17
    • 2342568939 scopus 로고    scopus 로고
    • De novo DNA synthesis by human DNA polymerase lambda, DNA polymerase mu and terminal deoxyribonucleotidyl transferase
    • K. Ramadan De novo DNA synthesis by human DNA polymerase lambda, DNA polymerase mu and terminal deoxyribonucleotidyl transferase J. Mol. Biol. 339 2004 395 404
    • (2004) J. Mol. Biol. , vol.339 , pp. 395-404
    • Ramadan, K.1
  • 18
    • 0033598831 scopus 로고    scopus 로고
    • Association of terminal deoxynucleotidyl transferase with Ku
    • K.N. Mahajan Association of terminal deoxynucleotidyl transferase with Ku Proc. Natl. Acad. Sci. U. S. A. 96 1999 13926 13931
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 13926-13931
    • Mahajan, K.N.1
  • 19
    • 0037066719 scopus 로고    scopus 로고
    • DNA polymerase lambda, a novel DNA repair enzyme in human cells
    • M. Garcia-Diaz DNA polymerase lambda, a novel DNA repair enzyme in human cells J. Biol. Chem. 277 2002 13184 13191
    • (2002) J. Biol. Chem. , vol.277 , pp. 13184-13191
    • Garcia-Diaz, M.1
  • 20
    • 0034714096 scopus 로고    scopus 로고
    • DNA polymerase lambda (Pol lambda), a novel eukaryotic DNA polymerase with a potential role in meiosis
    • M. Garcia-Diaz DNA polymerase lambda (Pol lambda), a novel eukaryotic DNA polymerase with a potential role in meiosis J. Mol. Biol. 301 2000 851 867
    • (2000) J. Mol. Biol. , vol.301 , pp. 851-867
    • Garcia-Diaz, M.1
  • 21
    • 0242634246 scopus 로고    scopus 로고
    • DNA polymerase mu (Pol mu), homologous to TdT, could act as a DNA mutator in eukaryotic cells
    • O. Dominguez DNA polymerase mu (Pol mu), homologous to TdT, could act as a DNA mutator in eukaryotic cells EMBO J. 19 2000 1731 1742
    • (2000) EMBO J. , vol.19 , pp. 1731-1742
    • Dominguez, O.1
  • 22
    • 0042662911 scopus 로고    scopus 로고
    • Lack of sugar discrimination by human Pol mu requires a single glycine residue
    • J.F. Ruiz Lack of sugar discrimination by human Pol mu requires a single glycine residue Nucleic Acids Res. 31 2003 4441 4449
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4441-4449
    • Ruiz, J.F.1
  • 23
    • 0345316715 scopus 로고    scopus 로고
    • Human DNA polymerase lambda possesses terminal deoxyribonucleotidyl transferase activity and can elongate RNA primers: Implications for novel functions
    • K. Ramadan Human DNA polymerase lambda possesses terminal deoxyribonucleotidyl transferase activity and can elongate RNA primers: implications for novel functions J. Mol. Biol. 328 2003 63 72
    • (2003) J. Mol. Biol. , vol.328 , pp. 63-72
    • Ramadan, K.1
  • 24
    • 0141483284 scopus 로고    scopus 로고
    • The frameshift infidelity of human DNA polymerase lambda. Implications for function
    • K. Bebenek The frameshift infidelity of human DNA polymerase lambda. Implications for function J. Biol. Chem. 278 2003 34685 34690
    • (2003) J. Biol. Chem. , vol.278 , pp. 34685-34690
    • Bebenek, K.1
  • 25
    • 0035860767 scopus 로고    scopus 로고
    • Identification of an intrinsic 5′-deoxyribose-5-phosphate lyase activity in human DNA polymerase lambda: A possible role in base excision repair
    • M. Garcia-Diaz Identification of an intrinsic 5′-deoxyribose-5- phosphate lyase activity in human DNA polymerase lambda: a possible role in base excision repair J. Biol. Chem. 276 2001 34659 34663
    • (2001) J. Biol. Chem. , vol.276 , pp. 34659-34663
    • Garcia-Diaz, M.1
  • 26
    • 0034889360 scopus 로고    scopus 로고
    • Prokaryotic homologs of the eukaryotic DNA-end-binding protein Ku, novel domains in the Ku protein and prediction of a prokaryotic double-strand break repair system
    • L. Aravind, and E.V. Koonin Prokaryotic homologs of the eukaryotic DNA-end-binding protein Ku, novel domains in the Ku protein and prediction of a prokaryotic double-strand break repair system Genome Res. 11 2001 1365 1374
    • (2001) Genome Res. , vol.11 , pp. 1365-1374
    • Aravind, L.1    Koonin, E.V.2
  • 27
    • 0035816444 scopus 로고    scopus 로고
    • Identification of bacterial homologues of the Ku DNA repair proteins
    • A.J. Doherty Identification of bacterial homologues of the Ku DNA repair proteins FEBS Lett. 500 2001 186 188
    • (2001) FEBS Lett. , vol.500 , pp. 186-188
    • Doherty, A.J.1
  • 28
    • 7444269607 scopus 로고    scopus 로고
    • Mycobacterial Ku and ligase proteins constitute a two-component NHEJ repair machine
    • M. Della Mycobacterial Ku and ligase proteins constitute a two-component NHEJ repair machine Science 306 2004 683 685
    • (2004) Science , vol.306 , pp. 683-685
    • Della, M.1
  • 29
    • 0037031655 scopus 로고    scopus 로고
    • Identification of a DNA nonhomologous end-joining complex in bacteria
    • G.R. Weller Identification of a DNA nonhomologous end-joining complex in bacteria Science 297 2002 1686 1689
    • (2002) Science , vol.297 , pp. 1686-1689
    • Weller, G.R.1
  • 30
    • 12844250647 scopus 로고    scopus 로고
    • A primer-dependent polymerase function of Pseudomonas aeruginosa ATP-dependent DNA ligase (LigD)
    • H. Zhu, and S. Shuman A primer-dependent polymerase function of Pseudomonas aeruginosa ATP-dependent DNA ligase (LigD) J. Biol. Chem. 280 2005 418 427
    • (2005) J. Biol. Chem. , vol.280 , pp. 418-427
    • Zhu, H.1    Shuman, S.2
  • 31
    • 18744380665 scopus 로고    scopus 로고
    • Mechanism of nonhomologous end-joining in mycobacteria: A low-fidelity repair system driven by Ku, ligase D and ligase C
    • C. Gong Mechanism of nonhomologous end-joining in mycobacteria: a low-fidelity repair system driven by Ku, ligase D and ligase C Nat. Struct. Mol. Biol. 12 2005 304 312
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 304-312
    • Gong, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.