E. Coli Recq DNA Helicase

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For research use only. Not for clinical diagnosis. Catalog No. BAM-01-003-EX E. coli RecQ DNA Helicase BACKGROUND E. coli RecQ helicase contributes to the genomic stability as the prototype of RecQ family DNA helicases, mutations of which genes are associated with premature aging and cancer susceptibility, known as Bloom’s and Werner’s syndromes (1). RecQ helicase functions in both early and late stages of homologous recombination and unwinds DNAs with particular structures, such as the fork structure for replication, the Holliday junction which is an intermediate of recombination, telomere, quadruplex G4-DNA, etc. In replication fork, it forms a complex with topoisomerase III and regulates DNA topology (1, 2). The product is over-produced as a recombinant protein and highly purified by several steps of chromatography. A single band is observed by SDS-PAGE at 64 kD (Fig 1). Applications: 1) Studies on mechanisms of DNA recombination, replication and repair. 2) Application for genetic engineering. For dissociation of special structure DNA. Size: 20 g Form: 50% glycerol, 20 mM Tris-HCl (pH 7.5), 1 mM EDTA, 50 mM KCl, 1 mM DTT Protein concentration: 0.5 mg/ml as measured by BCA method Purity: Over 90% by SDS-PAGE (CBB staining) Biochemical Unwinding duplex DNA, dependent on ATP. DNA-dependent ATPase (Ref.2). Activities: Data Link: UniProtKB/Swiss-Prot P15043 (RECQ_ECOLI) Storage: Store at -70°C References: 1) Hickson I "RecQ helicases: caretakers of the genome.” Nat. Rev. Cancer 3:169-78 (2003) Review PMID: (This product was used in Ref. 12612652 2) 2) Hishida T et al “Role of the Escherichia coli RecQ DNA helicase in SOS signaling and genome stabilization at stalled replication forks.”Genes Dev 18:1886-1897 (2004) PMID: 15289460 www.cosmobio.com E. coli RecQ DNA Helicase Fig.1 Polyacrylamide gel electrophoresis of RecQ protein. For research use only. Not for clinical diagnosis. Manufactured by BioAcademia,Inc. TOYO 2CHOME, KOTO-KU, TOKYO, 135-0016, JAPAN http://www.cosmobio.co.jp/index_e.asp E-mail: [email protected] Phone : +81-3-5632-9617 FAX : +81-3-5632-9618 .

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Structure and Function of the Human Recq DNA Helicases
Zurich Open Repository and Archive University of Zurich Main Library Strickhofstrasse 39 CH-8057 Zurich www.zora.uzh.ch Year: 2005 Structure and function of the human RecQ DNA helicases Garcia, P L Posted at the Zurich Open Repository and Archive, University of Zurich ZORA URL: https://doi.org/10.5167/uzh-34420 Dissertation Published Version Originally published at: Garcia, P L. Structure and function of the human RecQ DNA helicases. 2005, University of Zurich, Faculty of Science. Structure and Function of the Human RecQ DNA Helicases Dissertation zur Erlangung der naturwissenschaftlichen Doktorwürde (Dr. sc. nat.) vorgelegt der Mathematisch-naturwissenschaftlichen Fakultat¨ der Universitat¨ Z ürich von Patrick L. Garcia aus Unterseen BE Promotionskomitee Prof. Dr. Josef Jiricny (Vorsitz) Prof. Dr. Ulrich H übscher Dr. Pavel Janscak (Leitung der Dissertation) Z ürich, 2005 For my parents ii Summary The RecQ DNA helicases are highly conserved from bacteria to man and are required for the maintenance of genomic stability. All unicellular organisms contain a single RecQ helicase, whereas the number of RecQ homologues in higher organisms can vary. Mu- tations in the genes encoding three of the five human members of the RecQ family give rise to autosomal recessive disorders called Bloom syndrome, Werner syndrome and Rothmund-Thomson syndrome. These diseases manifest commonly with genomic in- stability and a high predisposition to cancer. However, the genetic alterations vary as well as the types of tumours in these syndromes. Furthermore, distinct clinical features are observed, like short stature and immunodeficiency in Bloom syndrome patients or premature ageing in Werner Syndrome patients. Also, the biochemical features of the human RecQ-like DNA helicases are diverse, pointing to different roles in the mainte- nance of genomic stability.
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Plugged Into the Ku-DNA Hub: the NHEJ Network Philippe Frit, Virginie Ropars, Mauro Modesti, Jean-Baptiste Charbonnier, Patrick Calsou
Plugged into the Ku-DNA hub: The NHEJ network Philippe Frit, Virginie Ropars, Mauro Modesti, Jean-Baptiste Charbonnier, Patrick Calsou To cite this version: Philippe Frit, Virginie Ropars, Mauro Modesti, Jean-Baptiste Charbonnier, Patrick Calsou. Plugged into the Ku-DNA hub: The NHEJ network. Progress in Biophysics and Molecular Biology, Elsevier, 2019, 147, pp.62-76. 10.1016/j.pbiomolbio.2019.03.001. hal-02144114 HAL Id: hal-02144114 https://hal.archives-ouvertes.fr/hal-02144114 Submitted on 29 May 2019 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Progress in Biophysics and Molecular Biology xxx (xxxx) xxx Contents lists available at ScienceDirect Progress in Biophysics and Molecular Biology journal homepage: www.elsevier.com/locate/pbiomolbio Plugged into the Ku-DNA hub: The NHEJ network * Philippe Frit a, b, Virginie Ropars c, Mauro Modesti d, e, Jean Baptiste Charbonnier c, , ** Patrick Calsou a, b, a Institut de Pharmacologie et Biologie Structurale, IPBS, Universite de Toulouse, CNRS, UPS, Toulouse, France b Equipe Labellisee Ligue Contre
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Evolutionary History of Ku Proteins: Evidence of Horizontal Gene Transfer from Archaea to Eukarya
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Probes. These molecules have low photobleaching emission dipole orientation. However, the 1.25-NA (1977); J. Opt. Soc. Am. 67, 1607 (1977). rates(10-6 to 10-8 per excitation),near-unityquan- oil-immersion objective used here collected a calcu- 22. For a dipole on the air side of the interface,LlllLoois tum yield in a semirigid environment, and an absorp- lated 65% of the total light emitted by a molecule at 0.92, L~/Loo is 1.6,andthe radiativelifetimeIsde- tion cross section of 1.35 x 10-16 cm2 at 532 nm, the PMMA-alr interface [E. H. Helen and D. Axelrod, creased for a perpendicular emission dipole. estimated by us on the basis of the measured ab- J. Opt. Soc. Am. B 4, 337 (1987)], nearly indepen- 23. Aliphatic hydrocarbon immersion oil, type FF; sorption in methanol. dent of the emission-dipole orientation. The total col- Cargille Laboratories, Cedar Grove, NJ. 15. A quartz cover slip was first spin-coated with one lection or detection efficiency was 15%. 24. We deposited several micrometers of PMMA by spin- drop (0.2 ml) of 0.1 % by weight PMMA in chloroben- 18. A focused laser beam has a very small longitudinal coating several drops of a solution of 5% by weight zene and then spin-coated with one drop of a 1-nM field component along the z axis, on the order of PMMA in toluene and heating the sample to dry. solution of Dil'2C(12) in toluene. The nanomolar Elkw, whereEis the tangential laser field, k is 2'IT11.., 25.
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