scholarly journals Cloning and characterization of uracil-DNA glycosylase and the biological consequences of the loss of its function in the nematode Caenorhabditis elegans

Mutagenesis ◽  
2008 ◽  
Vol 23 (5) ◽  
pp. 407-413 ◽  
Author(s):  
N. Nakamura ◽  
H. Morinaga ◽  
M. Kikuchi ◽  
S.-I. Yonekura ◽  
N. Ishii ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Dna Glycosylase ◽  
Nematode Caenorhabditis Elegans ◽  
Uracil Dna Glycosylase

scholarly journals Embryonic extracts derived from the nematode Caenorhabditis elegans remove uracil from DNA by the sequential action of uracil-DNA glycosylase and AP (apurinic/apyrimidinic) endonuclease

2002 ◽  
Vol 365 (2) ◽  
pp. 547-553 ◽  
Author(s):  
Andrea SHATILLA ◽  
Dindial RAMOTAR
Keyword(s):  
Caenorhabditis Elegans ◽  
Excision Repair ◽  
Specific Inhibitor ◽  
Dna Glycosylase ◽  
Dependent Manner ◽  
Nematode Caenorhabditis Elegans ◽  
Uracil Dna Glycosylase ◽  
Ap Endonuclease ◽  
C Elegans ◽  
Ap Site

DNA bases continuously undergo modifications in response to endogenous reactions such as oxidation, alkylation or deamination. The modified bases are primarily removed by DNA glycosylases, which cleave the N-glycosylic bond linking the base to the sugar, to generate an apurinic/apyrimidinic (AP) site, and this latter lesion is highly mutagenic. Previously, no study has demonstrated the processing of these lesions in the nematode Caenorhabditis elegans. Herein, we report the existence of uracil-DNA glycosylase and AP endonuclease activities in extracts derived from embryos of C. elegans. These enzyme activities were monitored using a defined 5′-end 32P-labelled 42-bp synthetic oligonucleotide substrate bearing a single uracil residue opposite guanine at position 21. The embryonic extract rapidly cleaved the substrate in a time-dependent manner to produce a 20-mer product. The extract did not excise adenine or thymine opposite guanine, although uracil opposite either adenine or thymine was processed. Addition of the highly specific inhibitor of uracil-DNA glycosylase produced by Bacillus subtilis to the extract prevented the formation of the 20-mer product, indicating that removal of uracil is catalysed by uracil-DNA glycosylase. The data suggest that the 20-mer product was generated by a sequential reaction, i.e., removal of the uracil base followed by 5′-cleavage of the AP site. Further analysis revealed that product formation was dependent upon the presence of Mg2+, suggesting that cleavage of the AP site, following uracil excision, is carried out by a Mg2+-dependent AP endonuclease. It would appear that these activities correspond to the first two steps of a putative base-excision-repair pathway in C. elegans.

Characterization of GM-CSF-inhibitory factor and Uracil DNA glycosylase encoding genes from camel pseudocowpoxvirus

2015 ◽  
Vol 100 ◽  
pp. 291-296 ◽  
Author(s):  
G. Nagarajan ◽  
Shelesh Kumar Swami ◽  
Shyam Singh Dahiya ◽  
S.D. Narnaware ◽  
S.C. Mehta ◽  
...  
Keyword(s):  
Inhibitory Factor ◽  
Dna Glycosylase ◽  
Uracil Dna Glycosylase ◽  
Gm Csf ◽  
Encoding Genes

Characterization of cold-active uracil-DNA glycosylase from Bacillus sp. HJ171 and its use for contamination control in PCR

2008 ◽  
Vol 80 (5) ◽  
pp. 785-794 ◽  
Author(s):  
Gun A. Kim ◽  
Mi Sun Lee ◽  
Younguk Sun ◽  
Byung Doo Lee ◽  
Jong Il Lee ◽  
...  
Keyword(s):  
Dna Glycosylase ◽  
Bacillus Sp ◽  
Uracil Dna Glycosylase ◽  
Contamination Control ◽  
Cold Active

scholarly journals Cloning and biochemical characterization of the cyclophilin homologues from the free-living nematode Caenorhabditis elegans

1996 ◽  
Vol 317 (1) ◽  
pp. 179-185 ◽  
Author(s):  
Antony P. PAGE ◽  
Kenneth MacNIVEN ◽  
Michael O. HENGARTNER
Keyword(s):  
Signal Transduction ◽  
Protein Folding ◽  
Caenorhabditis Elegans ◽  
Biochemical Characterization ◽  
Single Species ◽  
Immunosuppressive Agent ◽  
Specific Substrate ◽  
Nematode Caenorhabditis Elegans ◽  
Isomerase Activity

Cyclosporin A (CsA) is the most widely used immunosuppressive agent, whose properties are exerted via an interaction with cyclophilin, resulting in down-regulation of signal-transduction events in the T-cell. Cyclophilin is identical with peptidylprolyl cis–trans isomerase (PPI; EC 5.2.1.8), an enzyme which catalyses the isomerization between the two proline conformations in proteins, thereby acting as a catalyst in protein-folding events. Several reports indicate that CsA has potent anti-parasitic activity, effective against both protozoan and helminth species. In order to understand the various biological roles that cyclophilins play we have initiated a study of these proteins in the genetically tractable nematode Caenorhabditis elegans. Here we describe the cloning and characterization of 11 cyclophilin genes (cyp-1 to -11) derived from this nematode; this is currently the greatest number of isoforms described in a single species. Southern blotting and physical mapping indicated that these genes are dispersed throughout the nematode genome. A high degree of conservation exists between several isoforms, which also share characteristics with the ubiquitous isoforms previously described. The remaining isoforms are divergent, having altered CsA-binding domains and additional non-cyclophilin domains, which may impart compartmental specificity. Ten of these isoforms have been expressed in Escherichia coli, and the resultant fusion proteins have been examined biochemically for PPI activity, which they all possess. Isomerase activity is highest in the conserved and lowest in divergent isoforms, perhaps indicating a more specific substrate for the latter. Analysis of the C. elegans cyp genes will provide answers as to the roles played by cyclophilins in protein folding and signal transduction.

scholarly journals Characterization of an archaeal family 4 uracil DNA glycosylase and its interaction with PCNA and chromatin proteins

2005 ◽  
Vol 387 (3) ◽  
pp. 859-863 ◽  
Author(s):  
Isabelle DIONNE ◽  
Stephen D. BELL
Keyword(s):  
Protein S ◽  
Dna Glycosylase ◽  
Nuclear Antigen ◽  
Uracil Dna Glycosylase ◽  
Sliding Clamp ◽  
C Terminus ◽  
Marked Preference ◽  
Chromatin Proteins ◽  
Mechanistic Basis

We describe the characterization of a family 4 UDG1 (uracil DNA glycosylase) from the crenarchaeote Sulfolobus solfataricus. UDG1 is found to have a marked preference for substrates containing a G:U base pair over either A:U or single-stranded uracil-containing DNA substrates. UDG1 is found to interact with the sliding clamp PCNA (proliferating cell nuclear antigen), and does so by a conserved motif in the C-terminus of the protein. S. solfataricus has a heterotrimeric PCNA, and only one of the subunits, PCNA3, interacts with UDG1. We have been unable to detect any stimulation of UDG activity by PCNA, in contrast with the observed effects of PCNA on a number of DNA metabolic enzymes. However, analysis of the effects of Sulfolobus chromatin proteins on UDG1 leads us to propose a mechanistic basis for coupling UDG1 to the replication fork.

scholarly journals Isolatio and characterization of metallothionein from nematode(Caenorhabditis elegans)

Eisei kagaku ◽  
1986 ◽  
Vol 32 (1) ◽  
pp. 22-27 ◽  
Author(s):  
KOHJI MARUYAMA ◽  
RITSUKO HORI ◽  
TSUTOMU NISHIHARA ◽  
MASAOMI KONDO
Keyword(s):  
Caenorhabditis Elegans ◽  
Nematode Caenorhabditis Elegans
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