scholarly journals Mechanism of DNA strand nicking at apurinic/apyrimidinic sites by Escherichia coli [formamidopyrimidine]DNA glycosylase

1989 ◽  
Vol 262 (2) ◽  
pp. 581-589 ◽  
Author(s):  
V Bailly ◽  
W G Verly ◽  
T O'Connor ◽  
J Laval
Keyword(s):  
Escherichia Coli ◽  
Dna Glycosylase ◽  
Elimination Reaction ◽  
Phosphodiester Bonds ◽  
Beta Elimination ◽  
Dna Strand

Escherichia coli [formamidopyrimidine]DNA glycosylase catalyses the nicking of both the phosphodiester bonds 3′ and 5′ of apurinic or apyrimidinic sites in DNA so that the base-free deoxyribose is replaced by a gap limited by 3′-phosphate and 5′-phosphate ends. The two nickings are not the results of hydrolytic processes; the [formamidopyrimidine]DNA glycosylase rather catalyses a beta-elimination reaction that is immediately followed by a delta-elimination. The enzyme is without action on a 3′-terminal base-free deoxyribose or on a 3′-terminal base-free unsaturated sugar produced by a beta-elimination reaction nicking the DNA strand 3′ to an apurinic or apyrimidinic site.

UV endonuclease V from bacteriophage T4 catalyzes DNA strand cleavage at aldehydic abasic sites by a syn .beta.-elimination reaction

1989 ◽  
Vol 111 (20) ◽  
pp. 8029-8030 ◽  
Author(s):  
Abhijit Mazumder ◽  
John A. Gerlt ◽  
Lois Rabow ◽  
Michael J. Absalon ◽  
JoAnne Stubbe ◽  
...  
Keyword(s):  
Bacteriophage T4 ◽  
Elimination Reaction ◽  
Abasic Sites ◽  
Endonuclease V ◽  
Beta Elimination ◽  
Dna Strand

scholarly journals The multiple activities of Escherichia coli endonuclease IV and the extreme lability of 5′-terminal base-free deoxyribose 5-phosphates

1989 ◽  
Vol 259 (3) ◽  
pp. 761-768 ◽  
Author(s):  
V Bailly ◽  
W G Verly
Keyword(s):  
Escherichia Coli ◽  
Dna Polymerase ◽  
Rat Liver ◽  
Half Life ◽  
Elimination Reaction ◽  
Ap Endonuclease ◽  
Exonuclease Iii ◽  
E Coli ◽  
Beta Elimination ◽  
Ap Site

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.

Crystallization and preliminary X-ray diffraction studies of 3-methyladenine—DNA glycosylase II from Escherichia coli

1988 ◽  
Vol 204 (4) ◽  
pp. 1055-1056 ◽  
Author(s):  
Yuriko Yamagata ◽  
Kyoko Odawara ◽  
Ken-Ichi Tomita ◽  
Yusaku Nakabeppu ◽  
Mutsuo Sekiguchi
Keyword(s):  
Escherichia Coli ◽  
Dna Glycosylase ◽  
X Ray Diffraction ◽  
X Ray

scholarly journals Characterization of Escherichia coli DNA Lesions Generated within J774 Macrophages

2000 ◽  
Vol 182 (18) ◽  
pp. 5225-5230 ◽  
Author(s):  
Eliana Schlosser-Silverman ◽  
Maya Elgrably-Weiss ◽  
Ilan Rosenshine ◽  
Ron Kohen ◽  
Shoshy Altuvia
Keyword(s):  
Escherichia Coli ◽  
Dna Damage ◽  
Respiratory Burst ◽  
Defense Mechanism ◽  
Dna Lesions ◽  
Intracellular Bacteria ◽  
Bacterial Killing ◽  
Strand Breaks ◽  
E Coli ◽  
Dna Strand

ABSTRACT Macrophages are armed with multiple oxygen-dependent and -independent bactericidal properties. However, the respiratory burst, generating reactive oxygen species, is believed to be a major cause of bacterial killing. We exploited the susceptibility of Escherichia coli in macrophages to characterize the effects of the respiratory burst on intracellular bacteria. We show that E. coli strains recovered from J774 macrophages exhibit high rates of mutations. We report that the DNA damage generated inside macrophages includes DNA strand breaks and the modification 8-oxo-2′-deoxyguanosine, which are typical oxidative lesions. Interestingly, we found that under these conditions, early in the infection the majority of E. coli cells are viable but gene expression is inhibited. Our findings demonstrate that macrophages can cause severe DNA damage to intracellular bacteria. Our results also suggest that protection against the macrophage-induced DNA damage is an important component of the bacterial defense mechanism within macrophages.

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