Abstract
A plasmid carrying the Deinococcus radiodurans recX gene under the control of a lactose promoter decreases the Escherichia coli cell resistance to UV irradiation and γ irradiation and also influences the conjugational recombination process. The D. radiodurans RecX protein functions in the Escherichia coli cells similarly to the E. coli RecX protein. Isolated and purified D. radiodurans RecX and E. coli RecX proteins are able to replace each other interacting with the E. coli RecA and D. radiodurans RecA proteins in vitro. Data obtained demonstrated that regulatory interaction of RecA and RecX proteins preserves a high degree of conservatism despite all the differences in the recombination reparation system between E. coli and D. radiodurans.
Similar content being viewed by others
References
Cox, M.M., Recombinational DNA repair in bacteria and the RecA protein, Prog. Nucleic Acid Res. Mol. Biol., 1999, vol. 63, pp. 311–366.
Kowalczykowski, S.C., Initiation of genetic recombination and recombination-dependent replication, Trends Biochem. Sci., 2000, vol. 25, pp. 156–165.
Morimatsu, K. and Kowalczykowski, S.C., RecFOR proteins load RecA protein onto gapped DNA to accelerate DNA strand exchange: a universal step of recombinational repair, Mol. Cell, 2003, vol. 11, pp. 1337–1347.
Dillingham, M.S. and Kowalczykowski, S.C., RecBCD enzyme and the repair of double-stranded DNA breaks, Microbiol. Mol. Biol. Rev., 2008, vol. 72, pp. 642–671.
Gutman, P.D., Carroll, J.D., Masters, C.I., and Minton, K.W., Sequencing, targeted mutagenesis and expression of a recA gene required for the extreme radioresistance of Deinococcus radiodurans, Gene, 1994, vol. 141, pp. 31–37.
Minton, K.W., Repair of ionizing-radiation damage in the radiation resistant bacterium Deinococcus radiodurans, Mutat. Res., 1996, vol. 363, pp. 1–7.
Carroll, J.D. and Minton, K.W., Expression of RecA in Deinococcus radiodurans, J. Bacteriol., 1996, vol. 178, pp. 130–135.
Cox, M.M. and Battista, J.R., Deinococcus radiodurans—the consummate survivor, Nat. Rev. Microbiol., 2005, vol. 3, pp. 882–892.
Zahradka K., Slade, D., Bailone, A., Sommer, S., Averbeck, D., Petranovic, M., Lindner, A., and Radman, M., Reassembly of shattered chromosomes in Deinococcus radiodurans, Nature, 2006, vol. 443, pp. 569–573.
Slade, D., Lindner, A.B., Paul, G., and Radman, M., Recombination and replication in DNA repair of heavily irradiated Deinococcus radiodurans, Cell, 2009, vol. 136, pp. 1044–1055.
Verbenko, V.N., Kuznetsova, L.N., Krup’yan, E.R., and Shalguev, V.I., Expression of recA gene of Deinococcus radiodurans in Escherichia coli cells, Russ. J. Genet., 2009, vol. 45, no. 10, pp. 1192–1199.
Narumi, I., Satoh, K., Kikuchi, M., Funayama, T., Yanagisawa, T., Kobayashi, Y., Watanabe, H. and Yamamoto, K., The LexA protein from Deinococcus radiodurans is not involved in RecA induction following gamma irradiation, J. Bacteriol., 2001, vol. 183, pp. 6951–6956.
Earl, A.M., Mohundro, M.M., Mian, I.S., and Battista, J.R., The IrrE protein of Deinococcus radiodurans R1 is a novel regulator of RecA expression, J. Bacteriol., 2002, vol. 184, pp. 6216–6224.
Montague M., Barnes, C. Smith, H.O., Chuang., R.Y., and Vashee, S., The evolution of RecD outside of the RecBCD complex, J. Mol. Evol., 2009, vol. 69, pp. 360–371.
Satoh, K., Kikuchi, M., Ishaque, A.M., Ohba, H., Yamada, M., Tejima, K., Onodera, T., and Narumi I., The role of Deinococcus radiodurans RecFOR proteins in homologous recombination, DNA Repair (Amsterdam), 2012, vol. 11, pp. 410–418.
Eggington, J.M., Haruta, N., Wood, E.A., and Cox, M.M., The single-stranded DNA-binding protein of Deinococcus radiodurans, BMC Microbiol., 2004, vol. 4, p. 2.
Kim, J.I.1., Sharma, A.K., Abbott, S.N., Wood, E.A., Dwyer, D.W., Jambura, A., Minton, K.W., Inman, R.B., Daly, M.J., and Cox, M.M., RecA protein from the extremely radioresistant bacterium Deinococcus radiodurans: expression, purification, and characterization, J. Bacteriol., 2002, vol. 184, pp. 1649–1660.
Drees, J.C., Lusetti, S.L., Chitteni Pattu, S., Inman, R.B., and Cox, M.M., A RecA filament capping mechanism for RecX protein, Mol. Cell, 2004, vol. 15, pp. 789–798.
Ragone, S., Maman, J.D., Furnham, N., and Pellegrini, L., Structural basis for inhibition of homologous recombination by the RecX protein, EMBO J., 2008, vol. 16, pp. 2259–2269.
Baitin, D.M., Gruenig, M.C., and Cox, M.M., SSB antagonizes RecX–RecA interaction, J. Biol. Chem., 2008, vol. 283, pp. 14198–14204.
Dudkina, A.V., Shvetsov, A.V., Bakhlanova, I.V., and Baitin, D.M., Change of filamentation dynamics of RecA protein induced by D112R amino acid substitution or ATP to dATP replacement; results in filament resistance to RecX protein action, Mol. Biol. (Moscow), 2011, vol. 45, pp. 500–507.
Shvetsov, A.V., Lebedev, D.V., Chervyakova, D.B., Bakhlanova, I.V., Yung, I.A., Radulescu, A., Kuklin, A.I., Baitin, D.M., and Isaev-Ivanov, V.V., Structure of RecX protein complex with the presynaptic RecA filament: molecular dynamics simulations and small angle neutron scattering, FEBS Lett., 2014, vol. 588, pp. 948–955.
Sheng, D., Liu, R., Xu, Z., Singh, P., Shen, B., and Hua, Y., Dual negative regulatory mechanisms of RecX on RecA functions in radiation resistance, DNA recombination and consequent genome instability in Deinococcus radiodurans, DNA Repair (Amsterdam), 2005, vol. 4, pp. 671–678.
Sheng, D., Li, M., Jiao, J., Sheng, X., Deng, W. and Hua, Y., Repression of recA induction by RecX is independent of the RecA protein in Deinococcus radiodurans, J. Bacteriol., 2010, vol. 192, pp. 3540–3544.
Lusetti, S.L., Hobbs, M.D., Stohl, E.A., ChitteniPattu, S., Inman, R.B., Seifert, H.S., and Cox, M.M., The RecF protein antagonizes RecX function via direct interaction, Mol. Cell, 2006, vol. 21, pp. 41–50.
Lusetti, S.L., Drees, J.C., Stohl, E.A., Seifert, H.S., and Cox, M.M., The DinI and RecX proteins are competing modulators of RecA function, J. Biol. Chem., 2004, vol. 279, pp. 55073–55079.
Adelberg, E.A. and Burns, S.V., Genetic variation in the sex factor of Escherichia coli, J. Bacteriol., 1960, vol. 79, pp. 321–330.
Bresler, S.E. and Lantsov, V.A., Induced recombination in Escherichia coli K-12: recombinogenic effect of tif1 mutation, Dokl. Akad. Nauk SSSR, 1978, vol. 238, no. 3, pp. 715–717.
Kassandrova, O.N. and Lebedev, V.V., Obrabotka rezul’tatov izmerenii (Analysis of Observational Results), Moscow: Nauka, 1970.
Morrical, S.W., Lee, J., and Cox, M.M., Continuous association of Escherichia coli single-stranded DNA binding protein with stable complexes of recA protein and single-stranded DNA, Biochemistry, 1986, vol. 25, pp. 1482–1494.
Cox, M.M., McEntee, K., and Lehman, I.R., A simple and rapid procedure for the large scale purification of the recA protein of Escherichia coli, J. Biol. Chem., 1981, vol. 256, pp. 4676–4678.
Drees, J.C., Lusetti, S.L., and Cox, M.M., Inhibition of RecA protein by Escherichia coli RecX protein: modulation by the RecA C terminus and filament functional state, J. Biol. Chem., 2004, vol. 279, pp. 52991–52997.
Stohl, E.A., Brockman, J.P., Burkle, K.L., Morimatsu, K., Kowalczykowski, S.C. and Seifert, H.S., Escherichia coli RecX inhibits RecA recombinase and coprotease activities in vitro and in vivo, J. Biol. Chem., 2003, vol. 278, pp. 2278–2285.
Bakhlanova, I.V., Dudkina, A.V., Baitin, D.M., Knight, K.L., Cox, M.M., and Lanzov, V.A., Modulating cellular recombination potential through alterations in RecA structure and regulation, Mol. Microbiol., 2010, vol. 78, pp. 1523–1538.
Hsu, H.F., Ngo, K.V., Chitteni-Pattu, S., Cox, M.M., and Li, H.W., Investigating Deinococcus radiodurans RecA protein filament formation on double-stranded DNA by a real-time single-molecule approach, Biochemistry, 2011, vol. 50, pp. 8270–8280.
Author information
Authors and Affiliations
Corresponding author
Additional information
Original Russian Text © I.V. Bakhlanova, D.M. Baitin, 2016, published in Genetika, 2016, Vol. 52, No. 3, pp. 293–299.
Rights and permissions
About this article
Cite this article
Bakhlanova, I.V., Baitin, D.M. Deinococcus radiodurans RecX and Escherichia coli RecX proteins are capable to replace each other in vivo and in vitro. Russ J Genet 52, 257–262 (2016). https://doi.org/10.1134/S1022795416030030
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1134/S1022795416030030