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.

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 Direct Interaction between Uracil-DNA Glycosylase and a Proliferating Cell Nuclear Antigen Homolog in the CrenarchaeonPyrobaculum aerophilum

2002 ◽  
Vol 277 (25) ◽  
pp. 22271-22278 ◽  
Author(s):  
Hanjing Yang ◽  
Ju-Huei Chiang ◽  
Sorel Fitz-Gibbon ◽  
Michel Lebel ◽  
Alessandro A. Sartori ◽  
...  
Keyword(s):  
Proliferating Cell Nuclear Antigen ◽  
Direct Interaction ◽  
Dna Glycosylase ◽  
Nuclear Antigen ◽  
Uracil Dna Glycosylase ◽  
Proliferating Cell

scholarly journals Latency-Associated Nuclear Antigen of Kaposi's Sarcoma-Associated Herpesvirus Recruits Uracil DNA Glycosylase 2 at the Terminal Repeats and Is Important for Latent Persistence of the Virus

2006 ◽  
Vol 80 (22) ◽  
pp. 11178-11190 ◽  
Author(s):  
Subhash C. Verma ◽  
Bharat G. Bajaj ◽  
Qiliang Cai ◽  
Huaxin Si ◽  
Todd Seelhammer ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Cell Line ◽  
Viral Genome ◽  
Kaposi's Sarcoma ◽  
Kaposi’S Sarcoma ◽  
Dna Glycosylase ◽  
Nuclear Antigen ◽  
Affinity Column ◽  
Uracil Dna Glycosylase ◽  
Kaposi’S Sarcoma Associated Herpesvirus

ABSTRACT Latency-associated nuclear antigen (LANA) of KSHV is expressed in all forms of Kaposi's sarcoma-associated herpesvirus (KSHV)-mediated tumors and is important for TR-mediated replication and persistence of the virus. LANA does not exhibit any enzymatic activity by itself but is critical for replication and maintenance of the viral genome. To identify LANA binding proteins, we used a LANA binding sequence 1 DNA affinity column and determined the identities of a number of proteins associated with LANA. One of the identified proteins was uracil DNA glycosylase 2 (UNG2). UNG2 is important for removing uracil residues yielded after either misincorporation of dUTP during replication or deamination of cytosine. The specificity of the ′LANA-UNG2 interaction was confirmed by using a scrambled DNA sequence affinity column. Interaction of LANA and UNG2 was further confirmed by in vitro binding and coimmunoprecipitation assays. Colocalization of these proteins was also detected in primary effusion lymphoma (PEL) cells, as well as in a cotransfected KSHV-negative cell line. UNG2 binds to the carboxyl terminus of LANA and retains its enzymatic activity in the complex. However, no major effect on TR-mediated DNA replication was observed when a UNG2-deficient (UNG−/−) cell line was used. Infection of UNG−/− and wild-type mouse embryonic fibroblasts with KSHV did not reveal any difference; however, UNG−/− cells produced a significantly reduced number of virion particles after induction. Interestingly, depletion of UNG2 in PEL cells with short hairpin RNA reduced the number of viral genome copies and produced infection-deficient virus.

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