Three-dimensional electron microscopy of the reverse gyrase from Sulfolobus tokodaii

Biochemical and Biophysical Research Communications

Volumn 297, Issue 4, 2002, Pages 749-755

  Matoba, Kyoko ^a   Mayanagi, Kouta ^a   Nakasu, Syo ^b   Kikuchi, Akihiko ^c   Morikawa, Kosuke ^a  

^a BIOMOL ENG RESEARCH INSTITUTE   (Japan)

^b AICHI CANCER CENTER HOSPITAL   (Japan)

^c NAGOYA UNIVERSITY SCHOOL OF MEDICINE   (Japan)

Author keywords

Archaea; DNA topology; Electron microscopy; Positive supercoiling; Reverse gyrase; Single particle analysis; Sulfolobus tokodaii; Thermophile; Three dimensional structure; Topoisomerase

Indexed keywords

ADENOSINE TRIPHOSPHATE; DNA TOPOISOMERASE; DOUBLE STRANDED DNA; HELICASE;

ANALYTIC METHOD; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DNA BINDING; DNA SUPERCOILING; ELECTRON MICROSCOPY; ENZYME BINDING; MORPHOLOGY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; SULFOLOBUS;

DNA TOPOISOMERASES, TYPE I; DNA, ARCHAEAL; IMAGE PROCESSING, COMPUTER-ASSISTED; MICROSCOPY, ELECTRON; PROTEIN CONFORMATION; SULFOLOBUS;

ARCHAEA; ARCHAEOGLOBUS; ARCHAEOGLOBUS FULGIDUS; SULFOLOBUS; SULFOLOBUS TOKODAII;

EID: 0036029944     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(02)02255-6     Document Type: Article

References (18)

1. J.J. Champoux, DNA topoisomerases: structure, function, and mechanism, Annu. Rev. Biochem. 70 (2001) 369-413.
2. A. Kikuchi, K. Asai, Reverse gyrase - a topoisomerase which introduces positive superhelical turns into DNA, Nature 309 (1984) 677-681.
3. P. Forterre, A hot topic: the origin of hyperthermophiles, Cell 85 (1996) 789-792.
4. A.-C. Déclais, C.B. de La Tour, M. Duguet, Reverse gyrases from bacteria and archaea, Methods Enzymol. 334 (2001) 146-162.
5. F. Confalonieri, C. Elie, M. Nadal, C.B. de La Tour, P. Forterre, M. Duguet, Reverse gyrase: a helicase-like domain and a type I topoisomerase in the same polypeptide, Proc. Natl. Acad. Sci. USA 90 (1993) 4753-4757.
6. A.-C. Déclais, J. Marsault, F. Confalonieri, C.B. de La Tour, M. Duguet, Reverse gyrase the two domains intimately cooperate to promote positive supercoiling, J. Biol. Chem. 275 (2000) 19498-19504.
7. C.D. Lima, J.C. Wang, A. Mondragón, Three-dimensional structure of the 67K N-terminal fragment of E. coli DNA topoisomerase I, Nature 367 (1994) 138-146.
8. H. Feinberg, A. Changela, A. Mondragón, Protein-nucleotide interactions in E. coli DNA topoisomerase I, Nat. Struct. Biol. 6 (1999) 961-968.
9. H. Feinberg, C.D. Lima, A. Mondragón, Conformational changes in E. coli DNA topoisomerase I, Nat. Struct. Biol. 6 (1999) 918-922.
10. A. Mondragón, R.J. DiGate, The structure of Escherichia coli DNA topoisomerase III, Struct. Fold. Des. 7 (1999) 1373-1383.
11. A. Changela, R.J. DiGate, A. Mondragón, Crystal structure of a complex of a type IA DNA topoisomerase with a single-stranded DNA molecule, Nature 411 (2001) 1077-1081.
12. A.C. Rodríguez, D. Stock, Crystal structure of reverse gyrase: insights into the positive supercoiling of DNA, EMBO J. 21 (2002) 418-426.
13. S. Nakasu, A. Kikuchi, Reverse gyrase; ATP-dependent type I topoisomerase from Sulfolobus, EMBO J. 4 (1985) 2705-2710.
14. M. Radermacher, Three-dimensional reconstruction of single particles from random and nonrandom tilt series, J. Electron Microsc. Tech. 9 (1988) 359-394.
15. T. Yasunaga, T. Wakabayashi, Extensible and object-oriented system Eos supplies a new environment for image analysis of electron micrographs of macromolecules, J. Struct. Biol. 116 (1996) 155-160.
16. J. Frank, M. Radermacher, P. Penczek, J. Zhu, Y. Li, M. Ladjadj, A. Leith, SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields, J. Struct. Biol. 116 (1996) 190-199.
17. P. Penczek, M. Radermacher, J. Frank, Three-dimensional reconstruction of single particles embedded in ice, Ultramicroscopy 40 (1992) 33-53.
18. C. Jaxel, M. Nadal, G. Mirambeau, P. Forterre, M. Takahashi, M. Duguet, Reverse gyrase binding to DNA alters the double helix structure and produces single-strand cleavage in the absence of ATP, EMBO J. 8 (1989) 3135-3139.