scholarly journals Cleavage of Single- and Double-Stranded DNAs Containing an Abasic Residue by Escherichia Coli Exonuclease III (AP Endonuclease VI)

1996 ◽  
Vol 24 (22) ◽  
pp. 4572-4576 ◽  
Author(s):  
T. Shida ◽  
M. Noda ◽  
J. Sekiguchi
1989 ◽  
Vol 259 (3) ◽  
pp. 761-768 ◽  
Author(s):  
V Bailly ◽  
W G Verly

Escherichia coli endonuclease IV hydrolyses the C(3′)-O-P bond 5′ to a 3′-terminal base-free deoxyribose. It also hydrolyses the C(3′)-O-P bond 5′ to a 3′-terminal base-free 2′,3′-unsaturated sugar produced by nicking 3′ to an AP (apurinic or apyrimidinic) site by beta-elimination; this explains why the unproductive end produced by beta-elimination is converted by the enzyme into a 3′-OH end able to prime DNA synthesis. The action of E. coli endonuclease IV on an internal AP site is more complex: in a first step the C(3′)-O-P bond 5′ to the AP site is hydrolysed, but in a second step the 5′-terminal base-free deoxyribose 5′-phosphate is lost. This loss is due to a spontaneous beta-elimination reaction in which the enzyme plays no role. The extreme lability of the C(3′)-O-P bond 3′ to a 5′-terminal AP site contrasts with the relative stability of the same bond 3′ to an internal AP site; in the absence of beta-elimination catalysts, at 37 degrees C the half-life of the former is about 2 h and that of the latter 200 h. The extreme lability of a 5′-terminal AP site means that, after nicking 5′ to an AP site with an AP endonuclease, in principle no 5′----3′ exonuclease is needed to excise the AP site: it falls off spontaneously. We have repaired DNA containing AP sites with an AP endonuclease (E. coli endonuclease IV or the chromatin AP endonuclease from rat liver), a DNA polymerase devoid of 5′----3′ exonuclease activity (Klenow polymerase or rat liver DNA polymerase beta) and a DNA ligase. Catalysts of beta-elimination, such as spermine, can drastically shorten the already brief half-life of a 5′-terminal AP site; it is what very probably happens in the chromatin of eukaryotic cells. E. coli endonuclease IV also probably participates in the repair of strand breaks produced by ionizing radiations: as E. coli endonuclease VI/exonuclease III, it is a 3′-phosphoglycollatase and also a 3′-phosphatase. The 3′-phosphatase activity of E. coli endonuclease VI/exonuclease III and E. coli endonuclease IV can also be useful when the AP site has been excised by a beta delta-elimination reaction.


1996 ◽  
Vol 17 (5) ◽  
pp. 1183-1185 ◽  
Author(s):  
Lucymara F. Agnez ◽  
Regina L.Costa de Oliveira ◽  
Paolo Di Mascio ◽  
Carlos F.M. Menck

1992 ◽  
Vol 70 (7) ◽  
pp. 605-608 ◽  
Author(s):  
Giselle Sanchez ◽  
Margaret D. Mamet-Bratley

The development of bacteriophage T7 was examined in an Escherichia coli double mutant defective for the two major apurinic, apyrimidinic endonucleases (exonuclease III and endonuclease IV, xth nfo). In cells infected with phages containing apurinic sites, the defect in repair enzymes led to a decrease of phage survival and a total absence of bacterial DNA degradation and of phage DNA synthesis. These results directly demonstrate the toxic action of apurinic sites on bacteriophage T7 at the intracellular level and its alleviation by DNA repair. In addition, untreated T7 phage unexpectedly displayed reduced plating efficiency and decreased DNA synthesis in the xth nfo double mutant.Key words: apurinic sites, DNA repair, T7 phage.


Mutagenesis ◽  
2006 ◽  
Vol 21 (2) ◽  
pp. 125-130 ◽  
Author(s):  
L.L. Souza ◽  
I.R. Eduardo ◽  
M. Pádula ◽  
A.C. Leitão

Author(s):  
Shuji Seki ◽  
Masao Hatsushika ◽  
Sekiko Watanabe ◽  
Kosuke Akiyama ◽  
Kazutaka Nagao ◽  
...  

1999 ◽  
Vol 70 (4) ◽  
pp. 505-511 ◽  
Author(s):  
Lucymara F. Agnez-Lima ◽  
Paolo Di Mascio ◽  
Rita L. Napolitano ◽  
Robert P. Fuchs ◽  
Carlos F. M. Menck

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