Initiation and re-initiation of DNA unwinding by the Escherichia coli Rep helicase

Nature

Volumn 419, Issue 6907, 2002, Pages 638-641

  Ha, Taekjip ^a   Rasnik, Ivan ^a   Cheng, Wei ^b   Babcock, Hazen P ^c   Gauss, George H ^b   Lohman, Timothy M ^b   Chu, Steven ^c  

^a University of Illinois at Urbana Champaign   (United States)

^b WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c STANFORD UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DISEASES; DNA; FLUORESCENCE; HYDROLYSIS; NUCLEIC ACIDS;

HEXAMERIC RINGS;

ESCHERICHIA COLI;

ADENOSINE TRIPHOSPHATE; DOUBLE STRANDED DNA; HELICASE; SINGLE STRANDED DNA;

DISEASE;

ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DNA DENATURATION; ESCHERICHIA COLI; FLUORESCENCE; HYDROLYSIS; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DNA INTERACTION;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; DNA HELICASES; DNA, BACTERIAL; ENZYME STABILITY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HYDROLYSIS; SPECTROMETRY, FLUORESCENCE;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0037057630     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01083     Document Type: Article

References (24)

1. Lohman, T. M. & Bjornson, K. P. Mechanisms of helicase-catalyzed DNA unwinding. Annu. Rev. Biochem. 65, 169-214 (1996).
2. Hall, M. C. & Matson, S. W. Helicase motifs: The engine that powers DNA unwinding. Mol. Microbiol. 34, 867-877 (1999).
3. von Hippel, P. H. & Delagouette, E. A general model for nucleic acid helicases and their "coupling" within macromolecular machines. Cell 104, 177-190 (2001).
4. Patel, S. S. & Picha, K. M. Structure and function of hexameric helicases. Annu Rev. Biochem. 69, 651-697 (2000).
5. Velankar, S. S., Soultanas, P., Dillingham, M. S., Subramanya, H. S. & Wigley, D. B. Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism. Cell 97, 75-84 (1999).
6. Mechanic, L. E., Hall, M. C. & Matson, S. W. Escherichia coli DNA helicase 11 is active as a monomer. J. Biol. Chem. 274, 12488-12498 (1999).
7. Levin, M. K. & Patel, S. S. The helicase from hepatitis C virus is active as an oligomer. J. Biol. Chem. 274, 31839-31846 (1999).
8. Ali, J. A., Maluf, N. K. & Lohman, T. M. An oligomeric form of E-coli UvrD is required for optimal helicase activity. J. Mol. Biol. 293, 815-834 (1999).
9. Dillingham, M. S., Wigley, D. B. & Webb, M. R. Demonstration of unidirectional single-stranded DNA translocation by PcrA helicase: Measurement of step size and translocation speed. Biochemistry 39, 205-212 (2000).
10. Cheng, W, Hsieh, J., Brendza, K. M. & Lohman, T. M. E. Coli Rep oligomers are required to initiate DNA unwinding in vitro. J. Mol. Biol. 310, 327-350 (2001).
11. Bianco, P. R. et al. Processive translocation and DNA unwinding by individual RecBCD enzyme molecules. Nature 409, 374-378 (2001).
12. Dohoney, K. M. & Gelles, J. x-Sequence recognition and DNA translocation by single RecBCD helicase/nuclease molecules. Nature 409, 370-374 (2001).
13. Weiss, S. Measuring conformational dynamics of biomolecules by single molecule fluorescence spectroscopy. Nature Struct. Biol. 7, 724-729 (2000).
14. Ha, T. et al. Probing the interaction between two single molecules-fluorescence resonance energy transfer between a single donor and a single acceptor. Proc. Natl Acad. Sci. USA 93, 6264-6268 (1996).
15. Zhuang, X. W. et al. A single-molecule study of RNA catalysis and folding, Science 288, 2048-2051 (2000).
16. Ha, T. Single molecule fluorescence resonance energy transfer. Methods 25, 78-86 (2001).
17. Sofia, S. J., Premnath, V. & Merrill, E. W. Poly(ethylene oxide) grafted to silicon surfaces: grafting density and protein adsorption. Macromolecules 31, 5059-5070 (1998).
18. Chao, K. & Lohman, T. M. DNA-induced dimerization of the Escherichia coli Rep helicase. J. Mol. Biol. 221, 1165-1181 (1991).
19. Bjornson, K. P., Amaratunga, M., Moore, K. J. M. & Lohman, T. M. Single-turnover kinetics of helicase-catalyzed DNA unwinding monitored continuously by fluorescence energy transfer. Biochemistry 33, 14306-14316 (1994).
20. Moore, K. J. M. & Lohman, T. M. Kinetic mechanism of adenine nucleotide binding to and hydrolysis by the Escherichia coli Rep monomer. 1. Use of fluorescent nucleotide analogues. Biochemistry 33, 14550-14564 (1994).
21. Wong, I. & Lohman, T. M. A two-site mechanism for ATP hydrolysis by the asymmetric Rep dimer P2S as revealed by site-specific inhibition with ADP-AIF4. Biochemistry 36, 3115-3125 (1997).
22. Dillingham, M. S., Wigley, D. B. & Webb, M. R. Direct measurement of single-stranded DNA translocation by PcrA helicase using the fluorescent base analogue 2-aminopurine. Biochemistry 41, 643-651 (2002).
23. Yarranton, G. T. & Gefter, M. L. Enzyme-catalyzed DNA unwinding: studies on Escherichia coli rep protein. Proc. Natl Acad. Sci. USA 76, 1658-1662 (1979).
24. Lohman, T. M., Chao, K., Green, J. M., Sage, S. & Runyon, G. T. Large-scale purification and characterization of the Escherichia coli rep gene product. J. Biol. Chem. 264, 10139-10147 (1989).