scholarly journals Bovine papillomavirus type 1 E1 and simian virus 40 large T antigen share regions of sequence similarity required for multiple functions.

1997 ◽  
Vol 71 (10) ◽  
pp. 7600-7608 ◽  
Author(s):  
K C Mansky ◽  
A Batiza ◽  
P F Lambert
Keyword(s):  
Sequence Similarity ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
T Antigen ◽  
Bovine Papillomavirus ◽  
Large T Antigen ◽  
Multiple Functions

scholarly journals Interactions of the Papovavirus DNA Replication Initiator Proteins, Bovine Papillomavirus Type 1 E1 and Simian Virus 40 Large T Antigen, with Human Replication Protein A

1999 ◽  
Vol 73 (6) ◽  
pp. 4899-4907 ◽  
Author(s):  
YuFeng Han ◽  
Yueh-Ming Loo ◽  
Kevin T. Militello ◽  
Thomas Melendy
Keyword(s):  
Dna Replication ◽  
Protein A ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
T Antigen ◽  
Bovine Papillomavirus ◽  
Replication Proteins ◽  
E1 Protein ◽  
Cellular Dna

ABSTRACT Papovaviruses utilize predominantly cellular DNA replication proteins to replicate their own viral genomes. To appropriate the cellular DNA replication machinery, simian virus 40 (SV40) large T antigen (Tag) binds to three different cellular replication proteins, the DNA polymerase α-primase complex, the replication protein A (RPA) complex, and topoisomerase I. The functionally similar papillomavirus E1 protein has also been shown to bind to the DNA polymerase α-primase complex. Enzyme-linked immunoassay-based protein interaction assays and protein affinity pull-down assays were used to show that the papillomavirus E1 protein also binds to the cellular RPA complex in vitro. Furthermore, SV40 Tag was able to compete with bovine papillomavirus type 1 E1 for binding to RPA. Each of the three RPA subunits was individually overexpressed in Escherichia colias a soluble fusion protein. These fusion proteins were used to show that the E1-RPA and Tag-RPA interactions are primarily mediated through the 70-kDa subunit of RPA. These results suggest that different viruses have evolved similar mechanisms for taking control of the cellular DNA replication machinery.

scholarly journals Association of p300 and CBP with simian virus 40 large T antigen.

1996 ◽  
Vol 16 (7) ◽  
pp. 3454-3464 ◽  
Author(s):  
R Eckner ◽  
J W Ludlow ◽  
N L Lill ◽  
E Oldread ◽  
Z Arany ◽  
...  
Keyword(s):  
Sequence Similarity ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
T Antigen ◽  
Binding Motif ◽  
Creb Binding Protein ◽  
Large T Antigen ◽  
Adenovirus E1a ◽  
Protein Ligands ◽  
Nuclear Phosphoproteins

p300 and the CREB-binding protein CBP are two large nuclear phosphoproteins that are structurally highly related. Both function, in part, as transcriptional adapters and are targeted by the adenovirus E1A oncoprotein. We show here that p300 and CBP interact with another transforming protein, the simian virus 40 large T antigen (T). This interaction depends on the integrity of a region of T which is critical for its transforming and mitogenic properties and includes its LXCXE Rb-binding motif. T interferes with normal p300 and CBP function on at least two different levels. The presence of T alters the phosphorylation states of both proteins and inhibits their transcriptional activities on certain promoters. Although E1A and T show little sequence similarity, they interact with the same domain of p300 and CBP, suggesting that this region exhibits considerable flexibility in accommodating diverse protein ligands.

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