9
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Comparative analysis data of SF1 and SF2 helicases from three domains of life

      other
      a , b , c , d , e , *
      Data in Brief
      Elsevier
      Helicase, Archaea, SF1, SF2, Phylogenetics

      Read this article at

      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          SF1 and SF2 helicases are important molecular motors that use the energy of ATP to unwind nucleic acids or nucleic-acid protein complexes. They are ubiquitous enzymes and found in almost all organisms sequenced to date. This article provides a comparative analysis for SF1 and SF2 helicase families from three domains of life archaea, human, bacteria. Seven families are conserved in these three representatives and includes Upf1-like, UvrD-like, Rad3-like, DEAD-box, RecQ-like. Snf2 and Ski2-like. The data highlight conservation of the helicase core motifs for each of these families. Phylogenetic analysis presented on certain protein families are essential for further studies tracing the evolutionary history of helicase families. The data supplied in this article support publication “Genome-wide identification of SF1 and SF2 helicases from archaea” (Chamieh et al., 2016) [1].

          Related collections

          Most cited references5

          • Record: found
          • Abstract: found
          • Article: found
          Is Open Access

          TOPALi v2: a rich graphical interface for evolutionary analyses of multiple alignments on HPC clusters and multi-core desktops

          Summary: TOPALi v2 simplifies and automates the use of several methods for the evolutionary analysis of multiple sequence alignments. Jobs are submitted from a Java graphical user interface as TOPALi web services to either run remotely on high-performance computing clusters or locally (with multiple cores supported). Methods available include model selection and phylogenetic tree estimation using the Bayesian inference and maximum likelihood (ML) approaches, in addition to recombination detection methods. The optimal substitution model can be selected for protein or nucleic acid (standard, or protein-coding using a codon position model) data using accurate statistical criteria derived from ML co-estimation of the tree and the substitution model. Phylogenetic software available includes PhyML, RAxML and MrBayes. Availability: Freely downloadable from http://www.topali.org for Windows, Mac OS X, Linux and Solaris. Contact: iain.milne@scri.ac.uk
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            PROMALS3D: multiple protein sequence alignment enhanced with evolutionary and three-dimensional structural information.

            Multiple sequence alignment (MSA) is an essential tool with many applications in bioinformatics and computational biology. Accurate MSA construction for divergent proteins remains a difficult computational task. The constantly increasing protein sequences and structures in public databases could be used to improve alignment quality. PROMALS3D is a tool for protein MSA construction enhanced with additional evolutionary and structural information from database searches. PROMALS3D automatically identifies homologs from sequence and structure databases for input proteins, derives structure-based constraints from alignments of three-dimensional structures, and combines them with sequence-based constraints of profile-profile alignments in a consistency-based framework to construct high-quality multiple sequence alignments. PROMALS3D output is a consensus alignment enriched with sequence and structural information about input proteins and their homologs. PROMALS3D Web server and package are available at http://prodata.swmed.edu/PROMALS3D.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              The major role of human AP-endonuclease homolog Apn2 in repair of abasic sites in Schizosaccharomyces pombe.

              The abasic (AP) sites, the major mutagenic and cytotoxic genomic lesions, induced directly by oxidative stress and indirectly after excision of damaged bases by DNA glycosylases, are repaired by AP-endonucleases (APEs). Among two APEs in Saccharomyces cerevisiae, Apn1 provides the major APE activity, and Apn2, the ortholog of the mammalian APE, provides back-up activity. We have cloned apn1 and apn2 genes of Schizosaccharomyces pombe, and have shown that inactivation of Apn2 and not Apn1 sensitizes this fission yeast to alkylation and oxidative damage-inducing agents, which is further enhanced by Apn1 inactivation. We also show that Uve1, present in S.pombe but not in S.cerevisiae, provides the back-up APE activity together with Apn1. We confirmed the presence of APE activity in recombinant Apn2 and in crude cell extracts. Thus S.pombe is distinct from S.cerevisiae, and is similar to mammalian cells in having Apn2 as the major APE.
                Bookmark

                Author and article information

                Contributors
                Journal
                Data Brief
                Data Brief
                Data in Brief
                Elsevier
                2352-3409
                03 March 2017
                April 2017
                03 March 2017
                : 11
                : 510-516
                Affiliations
                [a ]Hloul Business Analytics, Omar Daouk Street, Beirut, Lebanon
                [b ]Beirut Arab University, Faculty of Science, Tripoli, Lebanon
                [c ]Université Saint Esprit, Jounieh, Lebanon
                [d ]Azm Center for Research in Biotechnology and its Applications, Lebanese University, Lebanon
                [e ]Department of Biology, Lebanese University, Faculty of Science, Tripoli, Lebanon
                Author notes
                [* ]Corresponding author at: Lebanese University, Faculty of Science, Department of Biology, Tripoli, Lebanon.Lebanese University, Faculty of Science, Department of BiologyTripoliLebanon hala.chamieh@ 123456ul.edu.lb
                Article
                S2352-3409(17)30066-5
                10.1016/j.dib.2017.02.047
                5349461
                1d6995b8-2bda-43a9-9ad6-d0a8cb457ea2
                © 2017 The Authors

                This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

                History
                : 10 June 2016
                : 23 January 2017
                : 27 February 2017
                Categories
                Data Article

                helicase,archaea,sf1,sf2,phylogenetics
                helicase, archaea, sf1, sf2, phylogenetics

                Comments

                Comment on this article