An accessory protein enhances both DNA binding and activity of DNA polymerase α isolated from normal, but not transformed, human fibroblasts

1996 ◽  
Vol 316 (5-6) ◽  
pp. 237-248 ◽  
Author(s):  
Matthew Schroeder ◽  
Susan Miller ◽  
Vinod Srivastava ◽  
Elizabeth Merriam-Crouch ◽  
Shawn Holt ◽  
...  
PLoS ONE ◽  
2008 ◽  
Vol 3 (5) ◽  
pp. e2221 ◽  
Author(s):  
Toyoaki Natsume ◽  
Yasuhiro Tsutsui ◽  
Takashi Sutani ◽  
Elaine M. Dunleavy ◽  
Alison L. Pidoux ◽  
...  

2003 ◽  
Vol 23 (8) ◽  
pp. 3013-3028 ◽  
Author(s):  
Mary Truscott ◽  
Lélia Raynal ◽  
Peter Premdas ◽  
Brigitte Goulet ◽  
Lam Leduy ◽  
...  

ABSTRACT CDP/Cux (CCAAT-displacement protein/cut homeobox) contains four DNA binding domains, namely, three Cut repeats (CR1, CR2, and CR3) and a Cut homeodomain. CCAAT-displacement activity involves rapid but transient interaction with DNA. More stable DNA binding activity is up-regulated at the G1/S transition and was previously shown to involve an N-terminally truncated isoform, CDP/Cux p110, that is generated by proteolytic processing. CDP/Cux has been previously characterized as a transcriptional repressor. However, here we show that expression of reporter plasmids containing promoter sequences from the human DNA polymerase α (pol α), CAD, and cyclin A genes is stimulated in cotransfections with N-terminally truncated CDP/Cux proteins but not with full-length CDP/Cux. Moreover, expression of the endogenous DNA pol α gene was stimulated following the infection of cells with a retrovirus expressing a truncated CDP/Cux protein. Chromatin immunoprecipitation (ChIP) assays revealed that CDP/Cux was associated with the DNA pol α gene promoter specifically in the S phase. Using linker scanning analyses, in vitro DNA binding, and ChIP assays, we established a correlation between binding of CDP/Cux to the DNA pol α promoter and the stimulation of gene expression. Although we cannot exclude the possibility that stimulation of gene expression by CDP/Cux involved the repression of a repressor, our data support the notion that CDP/Cux participates in transcriptional activation. Notwithstanding its mechanism of action, these results establish CDP/Cux as an important transcriptional regulator in the S phase.


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