The AddAB helicase–nuclease catalyses rapid and processive DNA unwinding using a single Superfamily 1A motor domain
The oligomeric state of Superfamily I DNA helicases is the subject of considerable and ongoing debate. While models based on crystal structures imply that a single helicase core domain is sufficient for DNA unwinding activity, biochemical data from several related enzymes suggest that a higher order...
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| Published in | Nucleic acids research Vol. 39; no. 6; pp. 2271 - 2285 |
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| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
| Published |
England
Oxford University Press
01.03.2011
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| Subjects | |
| Online Access | Get full text |
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| Abstract | The oligomeric state of Superfamily I DNA helicases is the subject of considerable and ongoing debate. While models based on crystal structures imply that a single helicase core domain is sufficient for DNA unwinding activity, biochemical data from several related enzymes suggest that a higher order oligomeric species is required. In this work we characterize the helicase activity of the AddAB helicase-nuclease, which is involved in the repair of double-stranded DNA breaks in Bacillus subtilis. We show that the enzyme is functional as a heterodimer of the AddA and AddB subunits, that it is a rapid and processive DNA helicase, and that it catalyses DNA unwinding using one single-stranded DNA motor of 3' → 5' polarity located in the AddA subunit. The AddB subunit contains a second putative ATP-binding pocket, but this does not contribute to the observed helicase activity and may instead be involved in the recognition of recombination hotspot sequences. |
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| AbstractList | The oligomeric state of Superfamily I DNA helicases is the subject of considerable and ongoing debate. While models based on crystal structures imply that a single helicase core domain is sufficient for DNA unwinding activity, biochemical data from several related enzymes suggest that a higher order oligomeric species is required. In this work we characterize the helicase activity of the AddAB helicase-nuclease, which is involved in the repair of double-stranded DNA breaks in Bacillus subtilis. We show that the enzyme is functional as a heterodimer of the AddA and AddB subunits, that it is a rapid and processive DNA helicase, and that it catalyses DNA unwinding using one single-stranded DNA motor of 3'[rightward arrow]5' polarity located in the AddA subunit. The AddB subunit contains a second putative ATP-binding pocket, but this does not contribute to the observed helicase activity and may instead be involved in the recognition of recombination hotspot sequences. The oligomeric state of Superfamily I DNA helicases is the subject of considerable and ongoing debate. While models based on crystal structures imply that a single helicase core domain is sufficient for DNA unwinding activity, biochemical data from several related enzymes suggest that a higher order oligomeric species is required. In this work we characterize the helicase activity of the AddAB helicase-nuclease, which is involved in the repair of double-stranded DNA breaks in Bacillus subtilis. We show that the enzyme is functional as a heterodimer of the AddA and AddB subunits, that it is a rapid and processive DNA helicase, and that it catalyses DNA unwinding using one single-stranded DNA motor of 3' arrow right 5' polarity located in the AddA subunit. The AddB subunit contains a second putative ATP-binding pocket, but this does not contribute to the observed helicase activity and may instead be involved in the recognition of recombination hotspot sequences. The oligomeric state of Superfamily I DNA helicases is the subject of considerable and ongoing debate. While models based on crystal structures imply that a single helicase core domain is sufficient for DNA unwinding activity, biochemical data from several related enzymes suggest that a higher order oligomeric species is required. In this work we characterize the helicase activity of the AddAB helicase-nuclease, which is involved in the repair of double-stranded DNA breaks in Bacillus subtilis. We show that the enzyme is functional as a heterodimer of the AddA and AddB subunits, that it is a rapid and processive DNA helicase, and that it catalyses DNA unwinding using one single-stranded DNA motor of 3' → 5' polarity located in the AddA subunit. The AddB subunit contains a second putative ATP-binding pocket, but this does not contribute to the observed helicase activity and may instead be involved in the recognition of recombination hotspot sequences.The oligomeric state of Superfamily I DNA helicases is the subject of considerable and ongoing debate. While models based on crystal structures imply that a single helicase core domain is sufficient for DNA unwinding activity, biochemical data from several related enzymes suggest that a higher order oligomeric species is required. In this work we characterize the helicase activity of the AddAB helicase-nuclease, which is involved in the repair of double-stranded DNA breaks in Bacillus subtilis. We show that the enzyme is functional as a heterodimer of the AddA and AddB subunits, that it is a rapid and processive DNA helicase, and that it catalyses DNA unwinding using one single-stranded DNA motor of 3' → 5' polarity located in the AddA subunit. The AddB subunit contains a second putative ATP-binding pocket, but this does not contribute to the observed helicase activity and may instead be involved in the recognition of recombination hotspot sequences. The oligomeric state of Superfamily I DNA helicases is the subject of considerable and ongoing debate. While models based on crystal structures imply that a single helicase core domain is sufficient for DNA unwinding activity, biochemical data from several related enzymes suggest that a higher order oligomeric species is required. In this work we characterize the helicase activity of the AddAB helicase–nuclease, which is involved in the repair of double-stranded DNA breaks in Bacillus subtilis . We show that the enzyme is functional as a heterodimer of the AddA and AddB subunits, that it is a rapid and processive DNA helicase, and that it catalyses DNA unwinding using one single-stranded DNA motor of 3′→5′ polarity located in the AddA subunit. The AddB subunit contains a second putative ATP-binding pocket, but this does not contribute to the observed helicase activity and may instead be involved in the recognition of recombination hotspot sequences. The oligomeric state of Superfamily I DNA helicases is the subject of considerable and ongoing debate. While models based on crystal structures imply that a single helicase core domain is sufficient for DNA unwinding activity, biochemical data from several related enzymes suggest that a higher order oligomeric species is required. In this work we characterize the helicase activity of the AddAB helicase-nuclease, which is involved in the repair of double-stranded DNA breaks in Bacillus subtilis. We show that the enzyme is functional as a heterodimer of the AddA and AddB subunits, that it is a rapid and processive DNA helicase, and that it catalyses DNA unwinding using one single-stranded DNA motor of 3' → 5' polarity located in the AddA subunit. The AddB subunit contains a second putative ATP-binding pocket, but this does not contribute to the observed helicase activity and may instead be involved in the recognition of recombination hotspot sequences. |
| Author | Gwynn, Emma J. Yeeles, Joseph T.P. Webb, Martin R. Dillingham, Mark S. |
| AuthorAffiliation | 1 DNA-Protein Interactions Unit, School of Biochemistry, Medical Sciences Building, University of Bristol, University Walk, Bristol, BS8 1TD and 2 MRC National Institute for Medical Research, Mill Hill, London, NW7 1AA, UK |
| AuthorAffiliation_xml | – name: 1 DNA-Protein Interactions Unit, School of Biochemistry, Medical Sciences Building, University of Bristol, University Walk, Bristol, BS8 1TD and 2 MRC National Institute for Medical Research, Mill Hill, London, NW7 1AA, UK |
| Author_xml | – sequence: 1 givenname: Joseph T.P. surname: Yeeles fullname: Yeeles, Joseph T.P. – sequence: 2 givenname: Emma J. surname: Gwynn fullname: Gwynn, Emma J. – sequence: 3 givenname: Martin R. surname: Webb fullname: Webb, Martin R. – sequence: 4 givenname: Mark S. surname: Dillingham fullname: Dillingham, Mark S. |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/21071401$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1074/jbc.M604412200 10.1128/MMBR.00020-08 10.1038/nature01673 10.1093/emboj/19.14.3799 10.1038/nature01083 10.1146/annurev.biochem.76.052305.115300 10.1128/JB.184.7.1819-1826.2002 10.1093/nar/gkq100 10.1093/nar/gkh641 10.1016/S0021-9258(18)90834-3 10.1093/nar/gkq173 10.1073/pnas.95.2.626 10.1006/jmbi.1999.2873 10.1016/S0969-2126(98)00010-0 10.1006/jmbi.2000.3556 10.1074/jbc.M109.076133 10.1038/384379a0 10.1073/pnas.232401899 10.1101/gad.1805709 10.1128/jb.178.17.5130-5137.1996 10.1006/jmbi.2000.3861 10.1021/bi992105o 10.1021/bi900101h 10.1038/nrm2394 10.1021/bi00433a018 10.1038/35053131 10.1016/0022-2836(91)90926-W 10.1016/S0021-9258(19)50649-4 10.1074/jbc.M808526200 10.1038/nature01674 10.1073/pnas.0502886102 10.1128/JB.00254-09 10.1093/nar/27.6.1421 10.1016/S0021-9258(19)69401-9 10.1074/jbc.M505520200 10.1093/nar/26.11.2686 10.1016/S0022-2836(02)01277-9 10.1074/jbc.270.41.24451 10.1074/jbc.M600882200 10.1021/bi050703z 10.1529/biophysj.108.133512 10.1016/j.dnarep.2009.12.016 10.1016/j.cell.2006.10.049 10.1016/S0092-8674(00)80716-3 10.1093/nar/gkl450 10.1038/nature02988 10.1093/nar/gkm1174 10.1021/bi00193a013 10.1021/bi9822269 10.1046/j.1365-2958.1996.601424.x 10.1021/bi901743k 10.1016/j.cell.2009.03.036 10.1046/j.1365-2958.2002.02785.x 10.1074/jbc.M808030200 10.1074/jbc.M704399200 10.1016/S0959-440X(05)80116-2 10.1074/jbc.270.38.22236 10.1016/j.jmb.2007.05.053 10.1016/S0021-9258(17)44018-X |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 ObjectType-Article-2 ObjectType-Feature-1 Present address: Joseph T.P. Yeeles, Molecular Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY, USA. |
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| References | Soultanas ( key 20170510155314_B49) 1999; 290 Yeeles ( key 20170510155314_B26) 2010; 9 Singleton ( key 20170510155314_B5) 2002; 184 Sikora ( key 20170510155314_B24) 2006; 281 Singleton ( key 20170510155314_B55) 2004; 432 Chao ( key 20170510155314_B62) 1991; 221 Roman ( key 20170510155314_B32) 1989; 28 Cromie ( key 20170510155314_B35) 2009; 191 Kim ( key 20170510155314_B4) 1998; 6 Webb ( key 20170510155314_B40) 2003 Ha ( key 20170510155314_B11) 2002; 419 Dillingham ( key 20170510155314_B6) 2000; 39 Slatter ( key 20170510155314_B23) 2009; 48 Haijema ( key 20170510155314_B51) 1996; 178 Chedin ( key 20170510155314_B57) 2000; 298 Soultanas ( key 20170510155314_B9) 2000; 19 Fili ( key 20170510155314_B41) 2010; 38 Unciuleac ( key 20170510155314_B61) 2010; 285 Nanduri ( key 20170510155314_B17) 2002; 99 Gorbalenya ( key 20170510155314_B1) 1993; 3 Subramanya ( key 20170510155314_B3) 1996; 384 Lee ( key 20170510155314_B7) 2006; 127 Matson ( key 20170510155314_B45) 1983; 258 Dillingham ( key 20170510155314_B30) 2005; 280 el Karoui ( key 20170510155314_B59) 1998; 95 Taylor ( key 20170510155314_B33) 1995; 270 Anand ( key 20170510155314_B54) 2004; 32 Haijema ( key 20170510155314_B58) 1996; 21 Brendza ( key 20170510155314_B12) 2005; 102 Singleton ( key 20170510155314_B2) 2007; 76 Niedziela-Majka ( key 20170510155314_B14) 2007; 282 Morris ( key 20170510155314_B44) 1999; 38 Dillingham ( key 20170510155314_B25) 2008; 72 Lohman ( key 20170510155314_B18) 2008; 9 Yeeles ( key 20170510155314_B42) 2009 Sinha ( key 20170510155314_B60) 2009; 23 Yeeles ( key 20170510155314_B36) 2009; 284 Velankar ( key 20170510155314_B8) 1999; 97 Chedin ( key 20170510155314_B34) 2002; 43 Yeeles ( key 20170510155314_B37) 2007; 371 Harding ( key 20170510155314_B43) 1992 Harding ( key 20170510155314_B63) 1994 Arnold ( key 20170510155314_B56) 2000; 300 Arai ( key 20170510155314_B21) 1981; 256 Reuter ( key 20170510155314_B48) 2010; 38 Chedin ( key 20170510155314_B46) 2006; 281 Dillingham ( key 20170510155314_B27) 2003; 423 Matson ( key 20170510155314_B20) 2006; 34 Yang ( key 20170510155314_B15) 2008; 36 Byrd ( key 20170510155314_B13) 2005; 44 Brune ( key 20170510155314_B50) 1994; 33 Roman ( key 20170510155314_B31) 1992; 267 Taylor ( key 20170510155314_B28) 2003; 423 Jongeneel ( key 20170510155314_B53) 1984; 259 Kunzelmann ( key 20170510155314_B47) 2010; 49 Dillingham ( key 20170510155314_B39) 2008; 95 Atkinson ( key 20170510155314_B19) 2009; 284 Maluf ( key 20170510155314_B16) 2003; 325 Raney ( key 20170510155314_B52) 1995; 270 Saikrishnan ( key 20170510155314_B10) 2009; 137 Bird ( key 20170510155314_B38) 1998; 26 Bianco ( key 20170510155314_B29) 2001; 409 Soultanas ( key 20170510155314_B22) 1999; 27 |
| References_xml | – volume: 281 start-page: 36110 year: 2006 ident: key 20170510155314_B24 article-title: DNA unwinding by Escherichia coli DNA helicase I (TraI) provides evidence for a processive monomeric molecular motor publication-title: J. Biol. Chem. doi: 10.1074/jbc.M604412200 – volume: 72 start-page: 642 year: 2008 ident: key 20170510155314_B25 article-title: RecBCD enzyme and the repair of double-stranded DNA breaks publication-title: Microbiol. Mol. Biol. Rev. doi: 10.1128/MMBR.00020-08 – volume: 423 start-page: 893 year: 2003 ident: key 20170510155314_B27 article-title: RecBCD enzyme is a bipolar DNA helicase publication-title: Nature doi: 10.1038/nature01673 – year: 2009 ident: key 20170510155314_B42 article-title: The initiation of double-stranded DNA break repair by an AddAB-type helicase-nuclease – volume-title: Analytical Ultracentrifugation in Biochemistry and Polymer Science year: 1992 ident: key 20170510155314_B43 – volume: 19 start-page: 3799 year: 2000 ident: key 20170510155314_B9 article-title: Uncoupling DNA translocation and helicase activity in PcrA: direct evidence for an active mechanism publication-title: EMBO J. doi: 10.1093/emboj/19.14.3799 – volume: 419 start-page: 638 year: 2002 ident: key 20170510155314_B11 article-title: Initiation and re-initiation of DNA unwinding by the Escherichia coli Rep helicase publication-title: Nature doi: 10.1038/nature01083 – volume: 76 start-page: 23 year: 2007 ident: key 20170510155314_B2 article-title: Structure and mechanism of helicases and nucleic acid translocases publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev.biochem.76.052305.115300 – volume: 184 start-page: 1819 year: 2002 ident: key 20170510155314_B5 article-title: Modularity and specialization in superfamily 1 and 2 helicases publication-title: J. Bacteriol. doi: 10.1128/JB.184.7.1819-1826.2002 – volume: 38 start-page: 3721 year: 2010 ident: key 20170510155314_B48 article-title: Single-molecule imaging of Bacteroides fragilis AddAB reveals the highly processive translocation of a single motor helicase publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkq100 – volume: 32 start-page: 3190 year: 2004 ident: key 20170510155314_B54 article-title: Structure-specific DNA binding and bipolar helicase activities of PcrA publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkh641 – volume: 259 start-page: 12925 year: 1984 ident: key 20170510155314_B53 article-title: Purification and characterization of the bacteriophage T4 dda protein. A DNA helicase that associates with the viral helix-destabilizing protein publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)90834-3 – volume: 38 start-page: 4448 year: 2010 ident: key 20170510155314_B41 article-title: Visualizing helicases unwinding DNA at the single molecule level publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkq173 – volume: 95 start-page: 626 year: 1998 ident: key 20170510155314_B59 article-title: Identification of the lactococcal exonuclease/recombinase and its modulation by the putative Chi sequence publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.95.2.626 – start-page: 131 volume-title: Kinetic Analysis: A Practical Approach year: 2003 ident: key 20170510155314_B40 article-title: In – volume: 290 start-page: 137 year: 1999 ident: key 20170510155314_B49 article-title: DNA binding mediates conformational changes and metal ion coordination in the active site of PcrA helicase publication-title: J. Mol. Biol. doi: 10.1006/jmbi.1999.2873 – volume: 6 start-page: 89 year: 1998 ident: key 20170510155314_B4 article-title: Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding publication-title: Structure doi: 10.1016/S0969-2126(98)00010-0 – volume: 298 start-page: 7 year: 2000 ident: key 20170510155314_B57 article-title: The Bacillus subtilis AddAB helicase/nuclease is regulated by its cognate Chi sequence in vitro publication-title: J. Mol. Biol. doi: 10.1006/jmbi.2000.3556 – volume: 285 start-page: 2632 year: 2010 ident: key 20170510155314_B61 article-title: Characterization of the mycobacterial AdnAB DNA motor provides insights into the evolution of bacterial motor-nuclease machines publication-title: J. Biol. Chem. doi: 10.1074/jbc.M109.076133 – volume: 384 start-page: 379 year: 1996 ident: key 20170510155314_B3 article-title: Crystal structure of a DExx box DNA helicase publication-title: Nature doi: 10.1038/384379a0 – volume: 99 start-page: 14722 year: 2002 ident: key 20170510155314_B17 article-title: Pre-steady-state DNA unwinding by bacteriophage T4 Dda helicase reveals a monomeric molecular motor publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.232401899 – volume: 23 start-page: 1423 year: 2009 ident: key 20170510155314_B60 article-title: AdnAB: a new DSB-resecting motor-nuclease from mycobacteria publication-title: Genes Dev. doi: 10.1101/gad.1805709 – volume: 178 start-page: 5130 year: 1996 ident: key 20170510155314_B51 article-title: Effects of lysine-to-glycine mutations in the ATP-binding consensus sequences in the AddA and AddB subunits on the Bacillus subtilis AddAB enzyme activities publication-title: J. Bacteriol. doi: 10.1128/jb.178.17.5130-5137.1996 – volume: 300 start-page: 469 year: 2000 ident: key 20170510155314_B56 article-title: A novel, 11 nucleotide variant of chi, chi*: one of a class of sequences defining the Escherichia coli recombination hotspot chi publication-title: J. Mol. Biol. doi: 10.1006/jmbi.2000.3861 – volume: 39 start-page: 205 year: 2000 ident: key 20170510155314_B6 article-title: Demonstration of unidirectional single-stranded DNA translocation by PcrA helicase: measurement of step size and translocation speed publication-title: Biochemistry doi: 10.1021/bi992105o – volume: 48 start-page: 6326 year: 2009 ident: key 20170510155314_B23 article-title: PcrA helicase tightly couples ATP hydrolysis to unwinding double-stranded DNA, modulated by the initiator protein for plasmid replication, RepD publication-title: Biochemistry. doi: 10.1021/bi900101h – volume: 9 start-page: 391 year: 2008 ident: key 20170510155314_B18 article-title: Non-hexameric DNA helicases and translocases: mechanisms and regulation publication-title: Nat. Rev. Mol. Cell. Biol. doi: 10.1038/nrm2394 – volume: 28 start-page: 2863 year: 1989 ident: key 20170510155314_B32 article-title: Characterization of the helicase activity of the Escherichia coli RecBCD enzyme using a novel helicase assay publication-title: Biochemistry doi: 10.1021/bi00433a018 – volume: 409 start-page: 374 year: 2001 ident: key 20170510155314_B29 article-title: Processive translocation and DNA unwinding by individual RecBCD enzyme molecules publication-title: Nature doi: 10.1038/35053131 – volume: 221 start-page: 1165 year: 1991 ident: key 20170510155314_B62 article-title: DNA-induced dimerization of the Escherichia coli Rep helicase publication-title: J. Mol. Biol. doi: 10.1016/0022-2836(91)90926-W – volume: 267 start-page: 4207 year: 1992 ident: key 20170510155314_B31 article-title: Processivity of the DNA helicase activity of Escherichia coli recBCD enzyme publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)50649-4 – volume: 284 start-page: 7746 year: 2009 ident: key 20170510155314_B36 article-title: An iron-sulfur cluster is essential for the binding of broken DNA by AddAB-type helicase-nucleases publication-title: J. Biol. Chem. doi: 10.1074/jbc.M808526200 – volume: 423 start-page: 889 year: 2003 ident: key 20170510155314_B28 article-title: RecBCD enzyme is a DNA helicase with fast and slow motors of opposite polarity publication-title: Nature doi: 10.1038/nature01674 – volume: 102 start-page: 10076 year: 2005 ident: key 20170510155314_B12 article-title: Autoinhibition of Escherichia coli Rep monomer helicase activity by its 2B subdomain publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.0502886102 – volume: 191 start-page: 5076 year: 2009 ident: key 20170510155314_B35 article-title: Phylogenetic ubiquity and shuffling of the bacterial RecBCD and AddAB recombination complexes publication-title: J. Bacteriol. doi: 10.1128/JB.00254-09 – volume: 27 start-page: 1421 year: 1999 ident: key 20170510155314_B22 article-title: Plasmid replication initiator protein RepD increases the processivity of PcrA DNA helicase publication-title: Nucleic Acids Res. doi: 10.1093/nar/27.6.1421 – start-page: 75 volume-title: Microscopy, Optical Spectroscopy, and Macroscopic Techniques year: 1994 ident: key 20170510155314_B63 article-title: In – volume: 256 start-page: 5294 year: 1981 ident: key 20170510155314_B21 article-title: Rep protein as a helicase in an active, isolatable replication fork of duplex phi X174 DNA publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)69401-9 – volume: 280 start-page: 37069 year: 2005 ident: key 20170510155314_B30 article-title: Bipolar DNA translocation contributes to highly processive DNA unwinding by RecBCD enzyme publication-title: J. Biol. Chem. doi: 10.1074/jbc.M505520200 – volume: 26 start-page: 2686 year: 1998 ident: key 20170510155314_B38 article-title: Characterisation of Bacillus stearothermophilus PcrA helicase: evidence against an active rolling mechanism publication-title: Nucleic Acids Res. doi: 10.1093/nar/26.11.2686 – volume: 325 start-page: 913 year: 2003 ident: key 20170510155314_B16 article-title: A Dimer of Escherichia coli UvrD is the active form of the helicase in vitro publication-title: J. Mol. Biol. doi: 10.1016/S0022-2836(02)01277-9 – volume: 270 start-page: 24451 year: 1995 ident: key 20170510155314_B33 article-title: Monomeric RecBCD enzyme binds and unwinds DNA publication-title: J. Biol. Chem. doi: 10.1074/jbc.270.41.24451 – volume: 281 start-page: 18610 year: 2006 ident: key 20170510155314_B46 article-title: The AddAB helicase/nuclease forms a stable complex with its cognate chi sequence during translocation publication-title: J. Biol. Chem. doi: 10.1074/jbc.M600882200 – volume: 44 start-page: 12990 year: 2005 ident: key 20170510155314_B13 article-title: Increasing the length of the single-stranded overhang enhances unwinding of duplex DNA by bacteriophage T4 Dda helicase publication-title: Biochemistry doi: 10.1021/bi050703z – volume: 95 start-page: 3330 year: 2008 ident: key 20170510155314_B39 article-title: Fluorescent single-stranded DNA binding protein as a probe for sensitive, real-time assays of helicase activity publication-title: Biophys. J. doi: 10.1529/biophysj.108.133512 – volume: 9 start-page: 276 year: 2010 ident: key 20170510155314_B26 article-title: The processing of double-stranded DNA breaks for recombinational repair by helicase-nuclease complexes publication-title: DNA Repair doi: 10.1016/j.dnarep.2009.12.016 – volume: 127 start-page: 1349 year: 2006 ident: key 20170510155314_B7 article-title: UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke publication-title: Cell doi: 10.1016/j.cell.2006.10.049 – volume: 97 start-page: 75 year: 1999 ident: key 20170510155314_B8 article-title: Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism publication-title: Cell doi: 10.1016/S0092-8674(00)80716-3 – volume: 34 start-page: 4089 year: 2006 ident: key 20170510155314_B20 article-title: The UvrD helicase and its modulation by the mismatch repair protein MutL publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkl450 – volume: 432 start-page: 187 year: 2004 ident: key 20170510155314_B55 article-title: Crystal structure of RecBCD enzyme reveals a machine for processing DNA breaks publication-title: Nature doi: 10.1038/nature02988 – volume: 36 start-page: 1976 year: 2008 ident: key 20170510155314_B15 article-title: Evidence for a functional dimeric form of the PcrA helicase in DNA unwinding publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkm1174 – volume: 33 start-page: 8262 year: 1994 ident: key 20170510155314_B50 article-title: Direct, real-time measurement of rapid inorganic phosphate release using a novel fluorescent probe and its application to actomyosin subfragment 1 ATPase publication-title: Biochemistry doi: 10.1021/bi00193a013 – volume: 38 start-page: 5164 year: 1999 ident: key 20170510155314_B44 article-title: DNA helicases displace streptavidin from biotin-labeled oligonucleotides publication-title: Biochemistry doi: 10.1021/bi9822269 – volume: 21 start-page: 989 year: 1996 ident: key 20170510155314_B58 article-title: Replacement of the lysine residue in the consensus ATP-binding sequence of the AddA subunit of AddAB drastically affects chromosomal recombination in transformation and transduction of Bacillus subtilis publication-title: Mol. Microbiol. doi: 10.1046/j.1365-2958.1996.601424.x – volume: 49 start-page: 843 year: 2010 ident: key 20170510155314_B47 article-title: Mechanism of interaction between single-stranded DNA binding protein and DNA publication-title: Biochemistry doi: 10.1021/bi901743k – volume: 137 start-page: 849 year: 2009 ident: key 20170510155314_B10 article-title: Mechanistic basis of 5′-3′ translocation in SF1B helicases publication-title: Cell doi: 10.1016/j.cell.2009.03.036 – volume: 43 start-page: 823 year: 2002 ident: key 20170510155314_B34 article-title: A novel family of regulated helicases/nucleases from Gram-positive bacteria: insights into the initiation of DNA recombination publication-title: Mol. Microbiol. doi: 10.1046/j.1365-2958.2002.02785.x – volume: 284 start-page: 9612 year: 2009 ident: key 20170510155314_B19 article-title: Stimulation of UvrD helicase by UvrAB publication-title: J. Biol. Chem. doi: 10.1074/jbc.M808030200 – volume: 282 start-page: 27076 year: 2007 ident: key 20170510155314_B14 article-title: Bacillus stearothermophilus PcrA monomer is a single-stranded DNA translocase but not a processive helicase in vitro publication-title: J. Biol. Chem. doi: 10.1074/jbc.M704399200 – volume: 3 start-page: 419 year: 1993 ident: key 20170510155314_B1 article-title: Helicases - amino-acid-sequence comparisons and structure-function-relationships publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/S0959-440X(05)80116-2 – volume: 270 start-page: 22236 year: 1995 ident: key 20170510155314_B52 article-title: Bacteriophage T4 Dda helicase translocates in a unidirectional fashion on single-stranded DNA publication-title: J. Biol. Chem. doi: 10.1074/jbc.270.38.22236 – volume: 371 start-page: 66 year: 2007 ident: key 20170510155314_B37 article-title: A Dual-nuclease mechanism for DNA break processing by AddAB-type helicase-nucleases publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2007.05.053 – volume: 258 start-page: 14017 year: 1983 ident: key 20170510155314_B45 article-title: The gene 4 protein of bacteriophage T7. Characterization of helicase activity publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)44018-X |
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| Snippet | The oligomeric state of Superfamily I DNA helicases is the subject of considerable and ongoing debate. While models based on crystal structures imply that a... |
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| SubjectTerms | Amino Acid Motifs Bacillus subtilis binding sites Biocatalysis crystal structure Dimerization DNA - metabolism DNA damage DNA helicases DNA Helicases - chemistry DNA Helicases - genetics DNA Helicases - metabolism DNA, Single-Stranded - metabolism Exodeoxyribonucleases - chemistry Exodeoxyribonucleases - genetics Exodeoxyribonucleases - metabolism Mutation Nucleic Acid Enzymes Protein Structure, Tertiary Protein Subunits - metabolism single-stranded DNA |
| Title | The AddAB helicase–nuclease catalyses rapid and processive DNA unwinding using a single Superfamily 1A motor domain |
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