DNA topoisomerases: harnessing and constraining energy to govern chromosome topology

被引:382
作者
Schoeffler, Allyn J. [1 ]
Berger, James M. [1 ]
机构
[1] Univ Calif Berkeley, Dept Mol & Cell Biol, Calif Inst Quantitat Biol, Berkeley, CA 94720 USA
关键词
D O I
10.1017/S003358350800468X
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
DNA topoisomerases are a diverse set of essential enzymes responsible for maintaining chromosomes in an appropriate topological state. Although they vary considerably in structure and mechanism, the partner-ship between topoisomerases and DNA has engendered commonalities in how these enzymes engage nucleic acid substrates and control DNA strand manipulations. All topoisomerases can harness the free energy stored in supercoiled DNA to drive their reactions; some further use the energy of ATP to alter the topology of DNA away from an enzyme-free equilibrium ground state. In the cell, topoisomerases regulate DNA supercoiling and unlink tangled nucleic acid strands to actively maintain chromosomes in a topological state commensurate with particular replicative and transcriptional needs. To carry out these reactions, topoisomerases rely on dynamic macromolecular contacts that alternate between associated and dissociated states throughout the catalytic cycle. In this review, we describe how structural and biochemical studies have furthered our understanding of DNA topoisomerases, with an emphasis on how these complex molecular machines use interfacial interactions to harness and constrain the energy required to manage DNA topology.
引用
收藏
页码:41 / 101
页数:61
相关论文
共 304 条
  • [91] A physical and functional interaction between Escherichia coli FtsK and topoisomerase IV
    Espeli, O
    Lee, C
    Marians, KJ
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (45) : 44639 - 44644
  • [92] Fass D, 1999, NAT STRUCT BIOL, V6, P322
  • [93] Feinberg H, 1999, NAT STRUCT BIOL, V6, P918
  • [94] Feinberg H, 1999, NAT STRUCT BIOL, V6, P961
  • [95] Single mutation in the linker domain confers protein flexibility and camptothecin resistance to human topoisomerase I
    Fiorani, P
    Bruselles, A
    Falconi, M
    Chillemi, G
    Desideri, A
    Benedetti, P
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (44) : 43268 - 43275
  • [96] Forterre P, 1996, FEMS MICROBIOL REV, V18, P237
  • [97] Origin and evolution of DNA topoisomerases
    Forterre, Patrick
    Gribaldo, Simonetta
    Gadelle, Daniele
    Serre, Marie-Claude
    [J]. BIOCHIMIE, 2007, 89 (04) : 427 - 446
  • [98] Regions within the N-terminal domain of human topoisomerase I exert important functions during strand rotation and DNA binding
    Frohlich, RF
    Andersen, FF
    Westergaard, O
    Andersen, AH
    Knudsen, BR
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 2004, 336 (01) : 93 - 103
  • [99] Tryptophane-205 of human topoisomerase I is essential for camptothecin inhibition of negative but not positive supercoil removal
    Frohlich, Rikke From
    Veigaard, Christopher
    Andersen, Felicie Faucon
    McClendon, A. Kathleen
    Gentry, Amanda C.
    Andersen, Anni Hangaard
    Osheroff, Neil
    Stevnsner, Tinna
    Knudsen, Birgitta Ruth
    [J]. NUCLEIC ACIDS RESEARCH, 2007, 35 (18) : 6170 - 6180
  • [100] Phylogenomics of type II DNA topoisomerases
    Gadelle, D
    Filée, J
    Buhler, C
    Forterre, P
    [J]. BIOESSAYS, 2003, 25 (03) : 232 - 242