Site-specific DNA Inversion by Serine Recombinases

2015 ◽  
pp. 199-236
Author(s):  
Reid C. Johnson
eLife ◽  
2013 ◽  
Vol 2 ◽  
Author(s):  
Meghan M McLean ◽  
Yong Chang ◽  
Gautam Dhar ◽  
John K Heiss ◽  
Reid C Johnson

Serine recombinases are often tightly controlled by elaborate, topologically-defined, nucleoprotein complexes. Hin is a member of the DNA invertase subclass of serine recombinases that are regulated by a remote recombinational enhancer element containing two binding sites for the protein Fis. Two Hin dimers bound to specific recombination sites associate with the Fis-bound enhancer by DNA looping where they are remodeled into a synaptic tetramer competent for DNA chemistry and exchange. Here we show that the flexible beta-hairpin arms of the Fis dimers contact the DNA binding domain of one subunit of each Hin dimer. These contacts sandwich the Hin dimers to promote remodeling into the tetramer. A basic region on the Hin catalytic domain then contacts enhancer DNA to complete assembly of the active Hin tetramer. Our results reveal how the enhancer generates the recombination complex that specifies DNA inversion and regulates DNA exchange by the subunit rotation mechanism.


1993 ◽  
Vol 175 (3) ◽  
pp. 693-700 ◽  
Author(s):  
L Dorgai ◽  
J Oberto ◽  
R A Weisberg
Keyword(s):  

2000 ◽  
Vol 182 (10) ◽  
pp. 2787-2792 ◽  
Author(s):  
Atsuko Gyohda ◽  
Teruya Komano

ABSTRACT The shufflon, a multiple DNA inversion system in plasmid R64, consists of four invertible DNA segments which are separated and flanked by seven 19-bp repeat sequences. The product of a site-specific recombinase gene, rci, promotes site-specific recombination between any two of the inverted 19-bp repeat sequences of the shufflon. To analyze the molecular mechanism of this recombination reaction, Rci protein was overproduced and purified. The purified Rci protein promoted the in vitro recombination reaction between the inverted 19-bp repeats of supercoiled DNA of a plasmid carrying segment A of the R64 shufflon. The recombination reaction was enhanced by the bacterial host factor HU. Gel electrophoretic analysis indicated that the Rci protein specifically binds to the DNA segments carrying the 19-bp sequences. The binding affinity of the Rci protein to the four shufflon segments as well as four synthetic 19-bp sequences differed greatly: among the four 19-bp repeat sequences, the repeat-a and -d sequences displayed higher affinity to Rci protein. These results suggest that the differences in the affinity of Rci protein for the 19-bp repeat sequences determine the inversion frequencies of the four segments.


1985 ◽  
Vol 82 (11) ◽  
pp. 3776-3780 ◽  
Author(s):  
H. E. Huber ◽  
S. Iida ◽  
W. Arber ◽  
T. A. Bickle

BioEssays ◽  
1987 ◽  
Vol 7 (5) ◽  
pp. 195-200 ◽  
Author(s):  
Roland Kanaar ◽  
Pieter van de Putte
Keyword(s):  

2001 ◽  
Vol 39 (3) ◽  
pp. 641-651 ◽  
Author(s):  
Deborah M. Tobiason ◽  
John M. Buchner ◽  
William H. Thiel ◽  
Kim M. Gernert ◽  
Anna C. Glasgow Karls

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