Ionic inhibition of formation of RecA nucleoprotein networks blocks homologous pairing
- PMID: 2994038
- PMCID: PMC390608
- DOI: 10.1073/pnas.82.17.5646
Ionic inhibition of formation of RecA nucleoprotein networks blocks homologous pairing
Abstract
Conditions that favor the complete coating of single-stranded DNA by RecA protein promote the association of these presynaptic filaments with naked double-stranded DNA to form large nucleoprotein networks before homologous pairing occurs. These RecA nucleoprotein networks sequester virtually all of the DNA in the reaction mixture. Conditions that are suboptimal for the formation of the RecA presynaptic filament rendered both the formation of RecA-DNA networks and the subsequent formation of joint molecules sensitive to inhibition by excess ATP or by pyrophosphate when these were added during synapsis. The rate of homologous pairing was directly related to the degree of inhibition of network formation. Various multivalent cations added during synapsis restored both the formation of networks and the pairing of homologous molecules. These observations support the view that the nucleoprotein network is a synaptic intermediate by means of which RecA protein facilitates the conjunction of DNA molecules and the subsequent processive search for homology. Inhibition by multivalent anions and restoration by multivalent cations suggests in addition, that negative charge repulsion inhibits the binding of naked duplex DNA to presynaptic filaments.
Similar articles
-
Isolation and visualization of active presynaptic filaments of recA protein and single-stranded DNA.Proc Natl Acad Sci U S A. 1984 Nov;81(22):7026-30. doi: 10.1073/pnas.81.22.7026. Proc Natl Acad Sci U S A. 1984. PMID: 6594678 Free PMC article.
-
The pairing activity of stable nucleoprotein filaments made from recA protein, single-stranded DNA, and adenosine 5'-(gamma-thio)triphosphate.J Biol Chem. 1985 Sep 25;260(21):11845-51. J Biol Chem. 1985. PMID: 3840165
-
The synapsis event in the homologous pairing of DNAs: RecA recognizes and pairs less than one helical repeat of DNA.Proc Natl Acad Sci U S A. 1992 Jul 15;89(14):6492-6. doi: 10.1073/pnas.89.14.6492. Proc Natl Acad Sci U S A. 1992. PMID: 1631148 Free PMC article.
-
Helical RecA nucleoprotein filaments mediate homologous pairing and strand exchange.Biochim Biophys Acta. 1989 Jul 7;1008(2):131-45. doi: 10.1016/0167-4781(80)90001-9. Biochim Biophys Acta. 1989. PMID: 2660904 Review. No abstract available.
-
Interchangeable parts of the Escherichia coli recombination machinery.Cell. 2003 Mar 21;112(6):741-4. doi: 10.1016/s0092-8674(03)00197-1. Cell. 2003. PMID: 12654241 Review.
Cited by
-
DNA Sequence Alignment during Homologous Recombination.J Biol Chem. 2016 May 27;291(22):11572-80. doi: 10.1074/jbc.R116.724807. Epub 2016 Apr 15. J Biol Chem. 2016. PMID: 27129270 Free PMC article. Review.
-
Reappearance from Obscurity: Mammalian Rad52 in Homologous Recombination.Genes (Basel). 2016 Sep 14;7(9):63. doi: 10.3390/genes7090063. Genes (Basel). 2016. PMID: 27649245 Free PMC article. Review.
-
Hallmarks of homology recognition by RecA-like recombinases are exhibited by the unrelated Escherichia coli RecT protein.EMBO J. 2003 Jan 15;22(2):324-34. doi: 10.1093/emboj/cdg027. EMBO J. 2003. PMID: 12514138 Free PMC article.
-
Homologous genetic recombination as an intrinsic dynamic property of a DNA structure induced by RecA/Rad51-family proteins: a possible advantage of DNA over RNA as genomic material.Proc Natl Acad Sci U S A. 2001 Jul 17;98(15):8425-32. doi: 10.1073/pnas.111005198. Proc Natl Acad Sci U S A. 2001. PMID: 11459985 Free PMC article. Review.
-
Repair of deletions and double-strand gaps by homologous recombination in a mammalian in vitro system.Mol Cell Biol. 1991 Jan;11(1):445-57. doi: 10.1128/mcb.11.1.445-457.1991. Mol Cell Biol. 1991. PMID: 1986239 Free PMC article.
References
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources