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Mutations in the N-terminal region of RecA that disrupt the stability of free
protein oligomers but not RecA-DNA complexes.
J. Mol. Biol. 299, 91-101.
DeZutter,
J.A.K., Forget, A.L., Logan, K.M. and Knight, K.L. (2001).
Phe217 regulates allosteric information transfer across the subunit interface of
the RecA protein filament.
Structure 9, 47-55.
Ranatunga, W., Jackson, D., Lloyd, J.A., Forget, A.L., Flowers II, R.A., Knight,
K.L. and Borgstahl, G.E.O. (2001).
The human Rad52 protein has two modes of self-association.
J. Biol. Chem. 276, 15876-15880.
Logan,
K.M., Forget, A.L., Verderese, J.P. and Knight, K.L. (2001).
ATP-mediated changes in cross-subunit interactions in the RecA protein.
Biochemistry 40, 11382-11389.
Lloyd,
J.A., Forget, A.L. and Knight, K.L. (2002).
Correlation of oligomeric properties with the oligomeric state of human Rad52
protein.
J. Biol. Chem. 277, 46172-46178.
Forget,
A.L., Bennett, B.T. and Knight, K.L. (2004).
Xrcc3 is recruited to DNA double strand breaks early and independent of Rad51.
J Cell. Biochem. 93, 429-436.
Forget, A.L.,
Banfill, M., McGrew, D.A., Calmann, M., Schiffer, C. and Knight, K.L. (2006)
RecA dimers serve as a functional unit for assembly of active nucleoprotein
filaments.
Biochemistry 45(45), 13537-13542.
Forget, A.L.,
Loftus, M.S., McGrew, D.A., Bennett, B.T. and Knight, K.L. (2007)
The Human Rad51 K133A Mutant is Functional for DNA Double-Strand Break Repair in
Human Cells.
Biochemistry 46(11), 3566-3575.
Forget.
A.L. and Kowalczykowski, S.C.
(2010)
Single-molecule imaging brings Rad51 nucleoprotein filaments into focus.
Trends in Cell Biology, 20, 269-276 (published online
March 17, 2010, as doi:10.1016/j.tcb.2010.02.004).
PMID: 20299221;
PMCID: PMC2862779
[Abstract] [Full Text] [PDF]
(see Trends in Cell Biology - Most
Read Articles
[PDF])
Forget, A.L. and
Kowalczykowski, S.C.
(2012)
Single-molecule imaging of DNA pairing by RecA reveals a
three-dimensional
homology search.
Nature, 482, 423–427 (published online February 8,
2012, doi:10.1038/nature10782). PMID: 22318518; PMCID: PMC3288143
[Abstract] [Full Text]
[PDF]
[Supplementary Information]
[Supplementary Movie 1]
[Supplementary Movie 2]
[Supplementary Movie 3]
(see Biocompare, Life Sciences Articles, News:
How DNA finds its match
[PDF])
(see biotic-blog:
How DNA finds its match
[PDF])
(see California Aggie:
Protein plays DNA matchmaker role
[PDF])
(see Cancer-z blogspot:
How
DNA finds its match
[PDF])
(see Cell.com News:
UC Davis study shows how DNA finds its match
[PDF])
(see Crop Biotech Update:
How DNA finds its match
[PDF])
(see Current Biology Dispatch:
Homologous Recombination: How RecA Finds the Perfect Partner
[PDF])
(see EurekAlert:
How
DNA finds its match
[PDF])
(see InvestigaMedicina.com:
El proceso de recombinación
ha sido una incógnita desde el descubrimiento del ADN
[PDF])
(see National Cancer Institute News:
UC Davis study shows how DNA finds its match
[PDF])
(see Nikon Instruments Research Papers:
New insights into DNA repair
[PDF])
(see Phys.Org News:
Study shows how DNA finds its match
[PDF])
(see ScienceDaily:
How DNA
finds it match
[PDF])
(see UC Davis News and Information:
How DNA
finds its match
[PDF])
(see YouTube video: Scientists show DNA matchup
[Video])
Forget, A.L.,
Dombrowski, C.C.,
Amitani, I.,
and Kowalczykowski, S.C.
(2013)
Exploring protein-DNA interactions in 3D using in situ construction,
manipulation, and visualization of individual DNA dumbbells with optical traps, microfluidics, and fluorescence microscopy.
Nature Protocols, 8, 525-538. PMID:
23411634; PMCID: PMC4329291. [Abstract]
[Full Text]
[PDF]
[Supplementary Figure 1]
Rad, B.,
Forget, A.L., Baskin, R.J.,
and Kowalczykowski, S.C. (2015)
Single-molecule visualization of RecQ helicase reveals DNA melting,
nucleation, and assembly are required for processive DNA unwinding.
Proc. Natl. Acad. Sci. USA 112, E6852-6861 (published online November
4, 2015 as doi: 10.1073/pnas.1518028112). PMID: 26540728; PMCID: PMC4687592.
[Abstract]
[Full Text]
[PDF]
[Supporting
Information]