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Updated: May 18, 2026

Synchronization of Caulobacter Crescentus for Investigation of the Bacterial Cell Cycle
Published on: April 8, 2015
Caulobacter crescentus harbours an evolutionarily distinct UDG (CC2084), UdgC, sharing features with family I and
Koyel Roy1, Elhassan Ali Fathi Emam1, Shruti Sharma1
1Departments of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560012, India.
Abstract:
Uracil arises in DNA either by spontaneous deamination of cytosine or misincorporation of dUMP by DNA polymerases. Cytosine deamination (to uracil), if unrepaired, may lead to GC to AT mutation. Uracil DNA glycosylases (UDGs) initiate the base excision repair (BER) pathway by excising uracil from DNA. Here, we report a novel uracil DNA glycosylase, CC2084, UdgC, from Caulobacter crescentus, an α-proteobacterium. Despite lacking significant overall sequence similarity with the known UDGs, CC2084 contains motif A (GQAPG) resembling to that of the family I UDGs (Ung), and motif B (HPSWRNT) similar to that of the family V UDGs (UdgB). In addition to uracil, CC2084 removes hypoxanthine and xanthine from single-, and double-, stranded DNAs; and ethenoadenine from double stranded DNA. Also, we notice that CC2084 activity is inhibited by the reaction products, uracil and AP site containing DNA, as well as by the phage-encoded Ugi, which was known to target only the family I UDGs. CC2084 rescues the mutator phenotype of E. coli ∆ung, an effect that is attenuated when co-expressed with Ugi. Phylogenetically, CC2084 forms a separate group of UDGs. The presence of CC2084 in the highly GC-rich genome of Caulobacter may compensate for the absence of the highly efficient Ung protein.
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