Skip Navigation

This Article
Right arrow Print PDF (1639K)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (19)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Kirkpatirck, D. P.
Right arrow Articles by Radding, C. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kirkpatirck, D. P.
Right arrow Articles by Radding, C. M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1992, Vol. 20, No. 16 4339-4346
© 1992

MOLECULAR BIOLOGY

RNA-DNA hybridization promoted by E.coli RecA portein

Dwight P. Kirkpatirck, B. Jagdeeshwar Rao and Charles M. Radding*

Department of Molecular Biophysics and Biochemistry and Department of Genetics, Yale University School of Medicine New Haven, CT 06510, USA

*To whom correspondence should be addressed

Received March 11, 1992. Revised July 15, 1992. RecA protein of E.coli plays a central regulatory role that is induced by damage to DNA and results in the inactivation of LexA repressor. In vitro, RecA protein binds preferentially to single-stranded DNA to form a nucleoprotein filament that can recognize homology in naked duplex DNA and promote extensive strand exchange. Although RecA protein shows little tendency at neutral pH to bind to RNA, we found that It nonetheless catalyzed at 37°C the hybridization of complementary RNA and single-stranded DNA sequences. Hybrids made by RecA protein at 37°C appeared indistinguishable from ones prepared by thermal annealing. RNA-DNA hybridization by RecA protein at neutral pH required, as does RecA-promoted homologous pairing, optimal conditions for the formation of RecA nucleoprotein filaments. The cosedimentation of RNA with those filaments further paralleled observations made on the formation of networks of nucleoprotein filaments with doublestranded DNA, an Instrumental intermediate in homologous pairing In vitro. These similarities with the pairing reaction support the view that RecA protein acts specifically in the hybridization reaction.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Nucleic Acids ResHome page
C. Arnaudeau, L. Rozier, C. Cazaux, M. Defais, D. Jenssen, and T. Helleday
RAD51 supports spontaneous non-homologous recombination in mammalian cells, but not the corresponding process induced by topoisomerase inhibitors
Nucleic Acids Res., February 1, 2001; 29(3): 662 - 667.
[Abstract] [Full Text] [PDF]

Home page
 Genes Dev.Home page
E. N. Zaitsev and S. C. Kowalczykowski
A novel pairing process promoted by Escherichia coli RecA protein: inverse DNA and RNA strand exchange
Genes & Dev., March 15, 2000; 14(6): 740 - 749.
[Abstract] [Full Text]

Home page
 Genes Dev.Home page
M. Kasahara, J. A. Clikeman, D. B. Bates, and T. Kogoma
RecA protein-dependent R-loop formation in vitro
Genes & Dev., February 1, 2000; 14(3): 360 - 365.
[Abstract] [Full Text]

Home page
 Proc. Natl. Acad. Sci. USAHome page
T. Nishinaka, Y. Ito, S. Yokoyama, and T. Shibata
An extended DNA structure through deoxyribose-base stacking induced by RecA protein
PNAS, June 24, 1997; 94(13): 6623 - 6628.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.