Biopolym. Cell. 1991; 7(3):54-59.
http://dx.doi.org/10.7124/bc.0002D0
Interaction RecA -protein with nuclei chromatin (the cytological aspect)
1Shpilevaya S. P., 1Kostetsky I. E., 1Stolar T. V., 1Likhachova L. L., 1Zharova L. G., 1Spivak I. M., 1Zhestyanikov V. D., 1Kordyum V. A., 1Irodov D. M.
  1. Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR
    Kiev, USSR

Abstract

Gene recA can be used as a model gene when studying the expression on exogenic DNA in vitro and in vivo. The indirect immunofluorescent method has been used for RecA protein visualization in cytoplasm and nuclei. The bacterial RecA protein has been tested in HeLa culture after treatment with RecA protein alone or included in lyposomes, and after transfection of culture by plasmid pKCR2. RecA protein was shown to contrast nucleus chromatin intensively and this process depended on the phase of mitotic cycle. Bacterial β-galactosidase and RecA protein have been observed in vivo 48 hours after cotransformation of mouse liver with pGA293A and pKCR2 plasmids, included in liposomes. High level of recA gene expression in hepatocytes of liver allows to use it in model systems when studying the exogenic DNA expression in vivo.
Full text: (PDF, in Russian)

References

[1] Mallick U, Pahmsdorf HJ, Herrlich P. Protein «X» synthesis in mammalian cells. Chromosome damage and repair: Proc. NATO Adv. Study Ins. New York, 1981:199-204.
[2] Lantsov VA. Bacterial RecA protein: a biochemical, genetic and physicochemical analysis. Genetika. 1985;21(9):1413-27.
[3] Kmiec EB, Kroeger PE, Brougham MJ, Holloman WK. Topological linkage of circular DNA molecules promoted by Ustilago rec 1 protein and topoisomerase. Cell. 1983;34(3):919-29.
[4] Cassuto E, Lightfoot LA, Howard-Flanders P. Partial purification of an activity from human cells that promotes homologous pairing and the formation of heteroduplex DNA in the presence of ATP. Mol Gen Genet. 1987;208(1-2):10-4.
[5] Taidi-Laskowski B, Tyan D, Honigberg SM, Radding CR, Grumet FC. Use of RecA protein to enrich for homologous genes in a genomic library. Nucleic Acids Res. 1988;16(16):8157-69.
[6] Angulo JF, Moreau PL, Maunoury R, Laporte J, Hill AM, Bertolotti R, Devoret R. KIN, a mammalian nuclear protein immunologically related to E. coli RecA protein. Mutat Res. 1989;217(2):123-34.
[7] O'Hare K, Benoist C, Breathnach R. Transformation of mouse fibroblasts to methotrexate resistance by a recombinant plasmid expressing a prokaryotic dihydrofolate reductase. Proc Natl Acad Sci U S A. 1981;78(3):1527-31.
[8] Kostetsky IE, Shpilevaya SP, Likhacheva LI, Zharova LC, Irodov DM, Kirillova VS, Kordium VA. Expression of Escherichia coli ?-Galactosidase in murine hepatocytes. Biopolym Cell. 1989; 5(2):51-8.
[9] Shpilevaya SP, Kostetsky IE, Likhacheva LI, Zharova LG, Irodov DM, Usenko EV, Stolyar TV, Kordium VA. Comparative studies in efficiency of expression of bacterial ?-galactosidase in vivo by the immunofluorescence method. Biopolym Cell. 1990; 6(1):63-6.
[10] Bilich KM, Irodov DM, Kordium VA. Some ultrastructural aspects of direct injection of liposomes with inclosed plasmid DNA into mice liver. Biopolym Cell. 1990; 6(1):73-82.
[11] Spivak IM, Kostetski? IE, Shpilevaia SP, Kordium VA, Zhestianikov VD. The restoration by Escherichia coli RecA protein of the survival of gamma-irradiated HeLa cells reduced by the DNA repair inhibitors caffeine and 3-aminobenzamide. Tsitologiia. 1991;33(2):103-9.