Abstract
The crystal structure of the recA protein from Escherichia coli at 2.3-Å resolution reveals a major domain that binds ADP and probably single- and double-stranded DNA. Two smaller subdomains at the N and C termini protrude from the protein and respectively stabilize a 61 helical polymer of protein subunits and interpolymer bundles. This polymer structure closely resembles that of recA/DNA filaments determined by electron microscopy. Mutations in recA protein that enhance coprotease, DNA-binding and/or strand-exchange activity can be explained if the interpolymer interactions in the crystal reflect a regulatory mechanism in vivo.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Clark, A. J. & Margulies, A. D. Proc. natn. Acad. Sci. U.S.A. 53, 451–459 (1965).
Sancar, A., Stachelek, C., Konigsberg, W. & Rupp, W. D. Proc. natn. Acad. Sci. U.S.A. 77, 2611–2615 (1980).
Horii, T., Ogawa, T. & Ogawa, H. Proc. natn. Acad. Sci. U.S.A. 77, 313–317 (1980).
Roca, A. I. & Cox, M. M. Crit. Rev. Biochem. Molec. Biol. 25, 415–456 (1990).
Kowalczykowski, S. C. A. Rev. Biophys. biophys. Chem. 20, 539–575 (1991).
Radding, C. M. J. biol. Chem. 266, 5355–5358 (1991).
Register, J. C. & Griffith, J. J. biol. Chem. 260, 12308–12312 (1985).
Pugh, B. F. & Cox, M. M. J. biol. Chem. 262, 1326–1336 (1987).
McEntee, K., Weinstock, G. M. & Lehman, I. R. J. biol. Chem. 256, 8835–8844 (1981).
DasGupta, C., Wu, A. M., Kahn, R., Cunningham, R. P. & Radding, C. M. Cell 25, 507–516 (1981).
Little, J. W. & Mount, D. W. Cell 29, 11–22 (1982).
Nohmi, T., Battista, J. R., Dodson, L. A. & Walker, G. C. Proc. natn. Acad. Sci. U.S.A. 85, 1816–1820 (1988).
Little, J. W. Proc. natn. Acad. Sci. U.S.A. 81, 1375–1379 (1984).
Egelman, E. H. & Stasiak, A. J. molec. Biol. 191, 677–697 (1986).
Yu, X. & Egelman, E. H. Biophys. J. 57, 555–566 (1990).
Stasiak, A. & Di Capua, E. Nature 299, 185–186 (1982).
Di Capua, E., Engel, A., Stasiak, A. & Koller, T. J. molec. Biol 157, 87–103 (1982).
Brenner, S. L., Zlotnick, A. & Griffith, J. D. J. molec. Biol. 204, 959–972 (1988).
Di Capua, E., Schnarr, M., Ruigrok, R. W. H., Lindner, P. & Timmins, P. A. J. molec. Biol 214, 557–570 (1990).
Williams, R. C. & Spengler, S. J. J. molec. Biol. 187, 109–118 (1986).
Pugh, B. F. & Cox, M. M. J. biol. Chem. 263, 76–83 (1988).
DiCapua, E., Ruigrok, R. W. H., Timmins, P. A. J. struct. Biol. 104, 91–96 (1990).
McKay, D. B., Steitz, T. A., Weber, I. T., West, S. C. & Howard-Flanders, P. J. biol. Chem. 255, 6662 (1980).
Rould, M. A., Perona, J. J., Soll, D. & Steitz, T. A. Science 246, 1135–1142 (1989).
Hol, W. G. J., van Duijnen, P. T. & Berendsen, H. J. C. Nature 273, 443–446 (1978).
Story, R. M. & Steitz, T. A. Nature 355, 374–376 (1992).
Blanar, M. A. et al. Cold Spring Harbor Symp. quant. Biol. 49, 507–511 (1983).
Rossman, M. G., Moras, D. & Olsen, K. W. Nature 250, 194–199 (1974).
Kobayashi, N., Knight, K. & McEntee, K. Biochemistry 26, 6801–6810 (1987).
Lee, B. & Richards, F. M. J. molec. Biol. 55, 379–400 (1971).
Miller, S., Lesk, A. M., Janin, J. & Chothia, C. Nature 328, 834–836 (1987).
Stasiak, A., Egelman, E. H. & Howard-Flanders, P. J. molec. Biol. 202, 659–662 (1988).
Yarranton, G. T. & Sedgwick, S. G. Molec. gen. Genet. 185, 99–104 (1982).
Müller, B., Koller, T. & Stasiak, A. J. molec. Biol. 212, 97–112 (1990).
Zlotnick, A., Mitchell, R. S. & Brenner, S. L. J. biol. Chem. 265, 17050–17054 (1990).
Kawashima, H., Horii, T., Ogawa, T. & Ogawa, H. Molec. gen. Genet. 193, 288–292 (1984).
Morand, P., Blanco, M. & Devoret, R. J. Bact. 131, 572–582 (1977).
Menetski, J. P. & Kowalczykowski, S. C. J. molec. Biol. 211, 845–855 (1990).
Cazaux, C., Larminat, F. & Defais, M. Biochimie 73, 281–284 (1991).
Wierenga, R. K., De Maeyer, M. C. H. & Hol, W. G. J. Biochemistry. 24, 1346–1357 (1985).
West, S. C., Cassuto, E., Mursalim, J. & Howard-Flanders, P. Proc. natn. Acad. Sci. U.S.A. 77, 2569–2573 (1980).
Bryant, F. R. & Lehman, I. R. J. biol. Chem. 261, 12988–12993 (1986).
Bryant, F. R. J. biol. Chem. 263, 8716–8723 (1988).
Muench, K. A. & Bryant, F. R. J. biol. Chem. 266, 844–850 (1991).
Wang, W.-B. & Tessman, F. S. J. Bact. 168, 901–910 (1986).
Zlotnick, A. & Brenner, S. L. J. molec. Biol. 209, 447–457 (1989).
de Jong, E. A. M. et al. J. molec. Biol. 206, 133–152 (1989).
Dutreix, M. et al. J. Bact. 171, 2415–2423 (1989).
Ogawa, H. & Ogawa, T. Adv. Biophys. 21, 135–148 (1986).
Knight, K. L., Aoki, K. H., Ujita, E. L. & McEntee, K. J. biol. Chem. 259, 11279–11283 (1984).
Kirby, E. P., Jacob, F. & Goldthwait, D. A. Proc. natn. Acad. Sci. U.S.A. 58, 1903–1910 (1967).
Lavery, P. E. & Kowalczykowski, S. C. J. molec. biol. 203, 861–874 (1988).
Wang, W.-B. & Tessman, E. S. J. Bact. 168, 901–910 (1986).
Wang, W.-B., Tessman, E. S. & Tessman, I. J. Bact. 170, 4823–4827 (1988).
Griffith, J. & Shores, C. G. Biochemistry 24, 158–162 (1985).
Wilson, D. H. & Benight, A. S. J. biol. Chem. 265, 7351–7359 (1990).
Morrical, S. W. & Cox, M. M. Biochemistry 24, 760–767 (1985).
Benedict, R. C. & Kowalczykowski, S. C. J. biol. Chem. 263, 15513–15520 (1988).
Salles, B. & Paoletti, C. Proc. natn. Acad. Sci. U.S.A. 80, 65–69 (1983).
Lauder, S. D. & Kowalczykowski, S. C. J. biol. Chem. 266, 5450–5458 (1991).
Egelman, E. H. & Stasiak, A. J. molec. biol. 200, 329–349 (1988).
Sancar, A. & Rupp, W. D. Proc. natn. Acad. Sci. U.S.A. 76, 3144–3148 (1979).
Wang, B. C. Meth. Enzym. 115, 90–112 (1985).
Brunger, A. T. Program X-PLOR Version 2.1 (Yale Univ., Connecticut, 1990).
Priestle, J. P. J. appl. Crystallogr. 21, 572–576 (1988).
Weisemann, J. M. & Weinstock, G. M. DNA 7, 389–398 (1988).
Madiraju, M. V. V. S., Templin, A. & Clark, A. J. Proc. natn. Acad. Sci. U.S.A. 85, 6592–6596 (1988).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Story, R., Weber, I. & Steitz, T. The structure of the E. coli recA protein monomer and polymer. Nature 355, 318–325 (1992). https://doi.org/10.1038/355318a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/355318a0
This article is cited by
-
Structure and efflux mechanism of the yeast pleiotropic drug resistance transporter Pdr5
Nature Communications (2021)
-
Escherichia coli recombinant sperm immobilizing factor RecX as a potential vaginal contraceptive
Reproductive Biology and Endocrinology (2018)
-
Enhancement of RecA-mediated self-assembly in DNA nanostructures through basepair mismatches and single-strand nicks
Scientific Reports (2017)
-
Cryo-EM structures of human RAD51 recombinase filaments during catalysis of DNA-strand exchange
Nature Structural & Molecular Biology (2017)
-
Reversible lysine acetylation is involved in DNA replication initiation by regulating activities of initiator DnaA in Escherichia coli
Scientific Reports (2016)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.