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Volumn 10, Issue 1, 2000, Pages 32-38

RecQ family helicases: Roles in cancer and aging

Author keywords

[No Author keywords available]

Indexed keywords

DNA; HELICASE;

EID: 0034001767     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-437X(99)00039-8     Document Type: Review
Times cited : (163)

References (59)
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    • This was the first report showing that a RecQ family helicase (BLM) is able to unwind a variety of G4-DNA structures. Moreover, it was shown that G4 DNA was a preferred substrate for the BLM helicase.
    • Sun H., Karow J.K., Hickson I.D., Maizels N. The Bloom's syndrome helicase unwinds G4 DNA. J Biol Chem. 273:1998;27587-27592. This was the first report showing that a RecQ family helicase (BLM) is able to unwind a variety of G4-DNA structures. Moreover, it was shown that G4 DNA was a preferred substrate for the BLM helicase.
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    • In this paper, WRN was shown to unwind G4-DNA based on the fragile X syndrome repeat sequence. Unlike BLM and Sgs1, WRN was shown to be incapable of unwinding G4-DNA of a telomeric sequence or an IgG switch region sequence.
    • Fry M., Loeb L.A. Human Werner syndrome DNA helicase unwinds tetrahelical structures of the fragile X syndrome repeat sequence d(CGG)n. J Biol Chem. 274:1999;12797-12802. In this paper, WRN was shown to unwind G4-DNA based on the fragile X syndrome repeat sequence. Unlike BLM and Sgs1, WRN was shown to be incapable of unwinding G4-DNA of a telomeric sequence or an IgG switch region sequence.
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    • •]) describing an exonuclease activity which resides in the amino-terminal domain of WRN. These authors find that this exonuclease proceeds in a 3′→5′ direction.
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    • •]. These authors found that the exonuclease activity of WRN proceeds in a 5′→3′ direction, which contradicts the other reports on the WRN exonuclease activity.
    • •]. These authors found that the exonuclease activity of WRN proceeds in a 5′→3′ direction, which contradicts the other reports on the WRN exonuclease activity.
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    • The first structural study of a RecQ family helicase. BLM is shown to have a native molecular mass >700 kDa and to form oligomeric ring structures detectable by electron microscopy. These data suggest that the BLM protein may encode one or two strands of DNA and translocate along the DNA in a processive manner.
    • Karow J.K., Newman R.H., Freemont P.S., Hickson I.D. Oligomeric ring structure of the Bloom's syndrome helicase. Curr Biol. 9:1999;597-600. The first structural study of a RecQ family helicase. BLM is shown to have a native molecular mass >700 kDa and to form oligomeric ring structures detectable by electron microscopy. These data suggest that the BLM protein may encode one or two strands of DNA and translocate along the DNA in a processive manner.
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    • Topoisomerase III is essential for accurate nuclear division in Schizosaccharomyces pombe
    • + gene and show that it is essential for cell viability. Moreover, they show that deletion of rqh1 in fission yeast suppresses the lethality of top3 mutants. This indicates that the genetic interaction between RecQ helicases and topo III is conserved amongst different yeast species.
    • + gene and show that it is essential for cell viability. Moreover, they show that deletion of rqh1 in fission yeast suppresses the lethality of top3 mutants. This indicates that the genetic interaction between RecQ helicases and topo III is conserved amongst different yeast species.
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    • In this report, the gene encoding a second human topo III protein (now known as topo IIIβ) is cloned and the gene product shown to interact physically with budding yeast Sgs1. Expression of the cDNA also partially restores growth in topo III-deficient yeast cells.
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    • RecQ helicase and topoisomerase III comprise a novel DNA strand passage function: A conserved mechanism for control of DNA recombination
    • These authors show that E. coli RecQ can unwind a covalently closed double-stranded DNA substrate, and that this provides a substrate for E. coli topo III to catenate two or more substrate molecules. Budding yeast topo III can substitute for the E. coli enzyme in this reaction. This presents the first evidence for a functional biochemical link between a RecQ helicase and a topoisomerase, confirming the well-established genetic link in yeast.
    • Harmon F.G., DiGate R.J., Kowalczykowski S.C. RecQ helicase and topoisomerase III comprise a novel DNA strand passage function: a conserved mechanism for control of DNA recombination. Mol Cell. 3:1999;611-620. These authors show that E. coli RecQ can unwind a covalently closed double-stranded DNA substrate, and that this provides a substrate for E. coli topo III to catenate two or more substrate molecules. Budding yeast topo III can substitute for the E. coli enzyme in this reaction. This presents the first evidence for a functional biochemical link between a RecQ helicase and a topoisomerase, confirming the well-established genetic link in yeast.
    • (1999) Mol Cell , vol.3 , pp. 611-620
    • Harmon, F.G.1    Digate, R.J.2    Kowalczykowski, S.C.3
  • 48
    • 0040436076 scopus 로고    scopus 로고
    • Functional and physical interaction between WRN helicase and human replication protein A
    • These authors showed that WRN binds to RPA and is able to unwind long duplex substrates in its presence. Hence, RPA influences the processivity of the WRN helicase reaction.
    • Brosh R.M. Jr., Orren D.K., Nehlin J.O., Ravn P.H., Kenny M.K., Machwe A., Bohr V.A. Functional and physical interaction between WRN helicase and human replication protein A. J Biol Chem. 274:1999;18341-18350. These authors showed that WRN binds to RPA and is able to unwind long duplex substrates in its presence. Hence, RPA influences the processivity of the WRN helicase reaction.
    • (1999) J Biol Chem , vol.274 , pp. 18341-18350
    • Brosh R.M., Jr.1    Orren, D.K.2    Nehlin, J.O.3    Ravn, P.H.4    Kenny, M.K.5    Machwe, A.6    Bohr, V.A.7
  • 49
    • 0033545879 scopus 로고    scopus 로고
    • Bloom's syndrome protein, BLM, colocalizes with replication protein A in meiotic prophase nuclei of mammalian spermatocytes
    • The authors of this paper describe a study of the localisation of the BLM protein in mouse spermatocytes. In meiotic prophase, BLM was found along synaptonemal complexes, colocalising with RPA, which is also known to be involved in meiotic synapsis. This report suggests a role for BLM during meiosis.
    • Walpita D., Plug A.W., Neff N.F., German J., Ashley T. Bloom's syndrome protein, BLM, colocalizes with replication protein A in meiotic prophase nuclei of mammalian spermatocytes. Proc Natl Acad Sci USA. 96:1999;5622-5627. The authors of this paper describe a study of the localisation of the BLM protein in mouse spermatocytes. In meiotic prophase, BLM was found along synaptonemal complexes, colocalising with RPA, which is also known to be involved in meiotic synapsis. This report suggests a role for BLM during meiosis.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 5622-5627
    • Walpita, D.1    Plug, A.W.2    Neff, N.F.3    German, J.4    Ashley, T.5
  • 50
    • 0033151615 scopus 로고    scopus 로고
    • P53-mediated apoptosis is attenuated in Werner syndrome cells
    • These authors show that p53 binds to the WRN protein both in vivo and in vitro. Moreover, evidence is presented that the p53-mediated apoptotic reponse is reduced in WS cells but can be restored by ectopic expression of the WRN cDNA. This is the first report that links a RecQ helicase with another protein known to play a role in cancer formation.
    • Spillare E.A., Robles A.I., Wang X.W., Shen J.C., Yu C.E., Schellenberg G.D., Harris C.C. p53-mediated apoptosis is attenuated in Werner syndrome cells. Genes Dev. 13:1999;1355-1360. These authors show that p53 binds to the WRN protein both in vivo and in vitro. Moreover, evidence is presented that the p53-mediated apoptotic reponse is reduced in WS cells but can be restored by ectopic expression of the WRN cDNA. This is the first report that links a RecQ helicase with another protein known to play a role in cancer formation.
    • (1999) Genes Dev , vol.13 , pp. 1355-1360
    • Spillare, E.A.1    Robles, A.I.2    Wang, X.W.3    Shen, J.C.4    Yu, C.E.5    Schellenberg, G.D.6    Harris, C.C.7
  • 51
    • 0032555220 scopus 로고    scopus 로고
    • Bloom's and Werner's syndrome genes suppress hyperrecombination in yeast sgs1 mutant: Implication for genomic instability in human diseases
    • This study makes extensive use of a yeast model to characterise the human BLM and WRN proteins. It is shown that expression of either protein can reduce the increased recombination rate characteristic of an sgs1 mutant. Furthermore, it is shown that BLM, but not WRN, can restore slow growth in a top3 sgs1 mutant and reduce the hydroxyurea sensitivity of an sgs1 mutant.
    • Yamagata K., Kato J., Shimamoto A., Goto M., Furuichi Y., Ikeda H. Bloom's and Werner's syndrome genes suppress hyperrecombination in yeast sgs1 mutant: implication for genomic instability in human diseases. Proc Natl Acad Sci USA. 95:1998;8733-8738. This study makes extensive use of a yeast model to characterise the human BLM and WRN proteins. It is shown that expression of either protein can reduce the increased recombination rate characteristic of an sgs1 mutant. Furthermore, it is shown that BLM, but not WRN, can restore slow growth in a top3 sgs1 mutant and reduce the hydroxyurea sensitivity of an sgs1 mutant.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 8733-8738
    • Yamagata, K.1    Kato, J.2    Shimamoto, A.3    Goto, M.4    Furuichi, Y.5    Ikeda, H.6
  • 52
    • 0033559694 scopus 로고    scopus 로고
    • The essential role of yeast topoisomerase III in meiosis depends on recombination
    • Gangloff S., de Massy B., Arthur L., Rothstein R., Fabre F. The essential role of yeast topoisomerase III in meiosis depends on recombination. EMBO J. 18:1999;1701-1711.
    • (1999) EMBO J , vol.18 , pp. 1701-1711
    • Gangloff, S.1    De Massy, B.2    Arthur, L.3    Rothstein, R.4    Fabre, F.5
  • 53
    • 0031848284 scopus 로고    scopus 로고
    • Replication focus-forming activity 1 and the Werner syndrome gene product
    • These authors identify a homologue of the WRN protein in Xenopus egg extracts. This new protein, termed FFA-1, is found to be a component required for the formation of replication foci. This is the first direct evidence for RecQ helicase involvement in the initiation and/or elongation steps of DNA replication.
    • Yan H., Chen C.Y., Kobayashi R., Newport J. Replication focus-forming activity 1 and the Werner syndrome gene product. Nat Genet. 19:1998;375-378. These authors identify a homologue of the WRN protein in Xenopus egg extracts. This new protein, termed FFA-1, is found to be a component required for the formation of replication foci. This is the first direct evidence for RecQ helicase involvement in the initiation and/or elongation steps of DNA replication.
    • (1998) Nat Genet , vol.19 , pp. 375-378
    • Yan, H.1    Chen, C.Y.2    Kobayashi, R.3    Newport, J.4
  • 54
    • 0033565598 scopus 로고    scopus 로고
    • Genetic recombination: Helicases and topoisomerases link up
    • Wu L., Karow J.K., Hickson I.D. Genetic recombination: helicases and topoisomerases link up. Curr Biol. 9:1999;R518-R520.
    • (1999) Curr Biol , vol.9
    • Wu, L.1    Karow, J.K.2    Hickson, I.D.3
  • 55
    • 0031459980 scopus 로고    scopus 로고
    • Extrachromosomal rDNA circles: A cause of aging in yeast
    • Sinclair D.A., Mills K., Guarente L. Extrachromosomal rDNA circles: a cause of aging in yeast. Cell. 91:1997;1033-1042.
    • (1997) Cell , vol.91 , pp. 1033-1042
    • Sinclair, D.A.1    Mills, K.2    Guarente, L.3
  • 56
    • 0032146147 scopus 로고    scopus 로고
    • Werner helicase is localized to transcriptionally active nucleoli of cycling cells
    • In this report, WRN is found to localise to the nucleoli of replicating cells and to translocate to the nucleoplasm when cells become quiescent or upon addition of the genotoxic agent 4NQO. The authors suggest a role for WRN in rDNA metabolism.
    • Gray M.D., Wang L., Youssoufian H., Martin G.M., Oshima J. Werner helicase is localized to transcriptionally active nucleoli of cycling cells. Exp Cell Res. 242:1998;487-494. In this report, WRN is found to localise to the nucleoli of replicating cells and to translocate to the nucleoplasm when cells become quiescent or upon addition of the genotoxic agent 4NQO. The authors suggest a role for WRN in rDNA metabolism.
    • (1998) Exp Cell Res , vol.242 , pp. 487-494
    • Gray, M.D.1    Wang, L.2    Youssoufian, H.3    Martin, G.M.4    Oshima, J.5
  • 57
    • 0032499703 scopus 로고    scopus 로고
    • Nucleolar localization of the Werner syndrome protein in human cells
    • These authors show that WRN is localised in the nucleolus in a variety of normal and transformed human cell lines. Contrary to this, however, homologous protein in mouse cells is shown to localise diffusely throughout the nucleus. The nucleolar location of WRN is intriguing given that the Sgs1 helicase of S. cerevisiae also localises to the nucleus and plays a key role in stabilising nucleolar structure.
    • Marciniak R.A., Lombard D.B., Johnson F.B., Guarente L. Nucleolar localization of the Werner syndrome protein in human cells. Proc Natl Acad Sci USA. 95:1998;6887-6892. These authors show that WRN is localised in the nucleolus in a variety of normal and transformed human cell lines. Contrary to this, however, homologous protein in mouse cells is shown to localise diffusely throughout the nucleus. The nucleolar location of WRN is intriguing given that the Sgs1 helicase of S. cerevisiae also localises to the nucleus and plays a key role in stabilising nucleolar structure.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6887-6892
    • Marciniak, R.A.1    Lombard, D.B.2    Johnson, F.B.3    Guarente, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.