ArticleBMC structural biology2005
An inactivated nuclease-like domain in RecC with novel function: implications for evolution.
Article in BMC structural biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- E. coli RecB Nuclease Domain Regulates RecBCD Helicase Activity but not Single Stranded DNA Translocase Activity.Journal of molecular biology · 2024Article
- Heterogeneity in E. coli RecBCD Helicase-DNA Binding and Base Pair Melting.Journal of molecular biology · 2021Article
- Structures and single-molecule analysis of bacterial motor nuclease AdnAB illuminate the mechanism of DNA double-strand break resection.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Processive DNA Unwinding by RecBCD Helicase in the Absence of Canonical Motor Translocation.Journal of molecular biology · 2016Article
- Nuclease activity of Saccharomyces cerevisiae Dna2 inhibits its potent DNA helicase activity.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Asymmetric regulation of bipolar single-stranded DNA translocation by the two motors within Escherichia coli RecBCD helicase.The Journal of biological chemistry · 2013Article
- Structure and Mechanisms of SF1 DNA Helicases.Advances in experimental medicine and biology · 2013Article
- The primary and secondary translocase activities within E. coli RecBC helicase are tightly coupled to ATP hydrolysis by the RecB motor.Journal of molecular biology · 2012Article
- The DNA Exonucleases of Escherichia coli.EcoSal Plus · 2011Article
- Escherichia coli RecBC helicase has two translocase activities controlled by a single ATPase motor.Nature structural & molecular biology · 2010Article
- Characterization of the mycobacterial AdnAB DNA motor provides insights into the evolution of bacterial motor-nuclease machines.The Journal of biological chemistry · 2010Article
- Domain interplay mediated by an essential disulfide linkage is critical for the activity and secretion of the metastasis-promoting enzyme autotaxin.The Journal of biological chemistry · 2009Article
- An iron-sulfur cluster is essential for the binding of broken DNA by AddAB-type helicase-nucleases.The Journal of biological chemistry · 2009Article
- RecBCD enzyme and the repair of double-stranded DNA breaks.Microbiology and molecular biology reviews : MMBR · 2008Review
- Kinetic control of Mg2+-dependent melting of duplex DNA ends by Escherichia coli RecBC.Journal of molecular biology · 2008Article
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1 author.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundThe PD-(D/E)xK superfamily, containing a wide variety of other exo- and endonucleases, is a notable example of general function conservation in the face of extreme sequence and structural variation. Almost all members employ a small number of shared conserved residues to bind catalytically essential metal ions and thereby effect DNA cleavage. The crystal structure of the RecBCD prokaryotic DNA repair machinery shows that RecB contains such a nuclease domain at its C-terminus. The RecC C-terminal region was reported as having a novel fold.
resultsThe RecC C-terminal region can be divided into an alpha/beta domain and a smaller alpha-helical bundle domain. Here we show that the alpha/beta domain is homologous to the RecB nuclease domain but lacks the features necessary for catalysis. Instead, the domain has a novel function within the nuclease superfamily--providing a hoop through which single-stranded DNA passes. Comparison with other structures of nuclease domains bound to DNA reveals strikingly different modes of ligand binding. The alpha-helical bundle domain contributes the pin which splits the DNA duplex.
conclusionThe demonstrated homology of RecB and RecC shows how evolution acted to produce the present RecBCD complex through aggregation of new domains as well as functional divergence and structural redeployment of existing domains. Distantly homologous nuclease(-like) domains bind DNA in highly diverse manners.
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