scholarly journals Replication Protein A from Saccharomyces cerevisiae Differently Binds to Photo-damaged DNA from Normal Single-stranded DNA

2006 ◽  
Vol 27 (11) ◽  
pp. 1731-1732 ◽  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein A ◽  
Replication Protein A ◽  
Replication Protein ◽  
Single Stranded Dna ◽  
Damaged Dna

scholarly journals A structural and dynamic model for the assembly of Replication Protein A on single-stranded DNA

2018 ◽  
Vol 9 (1) ◽  
Author(s):  
Luke A. Yates ◽  
Ricardo J. Aramayo ◽  
Nilisha Pokhrel ◽  
Colleen C. Caldwell ◽  
Joshua A. Kaplan ◽  
...  
Keyword(s):  
Dynamic Model ◽  
Protein A ◽  
Replication Protein A ◽  
Replication Protein ◽  
Single Stranded Dna

scholarly journals The RPA32 Subunit of Human Replication Protein A Contains a Single-stranded DNA-binding Domain

1998 ◽  
Vol 273 (7) ◽  
pp. 3932-3936 ◽  
Author(s):  
Elena Bochkareva ◽  
Lori Frappier ◽  
Aled M. Edwards ◽  
Alexey Bochkarev
Keyword(s):  
Dna Binding ◽  
Protein A ◽  
Replication Protein A ◽  
Binding Domain ◽  
Replication Protein ◽  
Dna Binding Domain ◽  
Single Stranded Dna

scholarly journals Recruitment of Replication Protein A by the Papillomavirus E1 Protein and Modulation by Single-Stranded DNA

2004 ◽  
Vol 78 (4) ◽  
pp. 1605-1615 ◽  
Author(s):  
Yueh-Ming Loo ◽  
Thomas Melendy
Keyword(s):  
Dna Replication ◽  
Protein A ◽  
Replication Protein A ◽  
T Antigen ◽  
Replication Protein ◽  
Enzyme Linked Immunosorbent Assay ◽  
Physical Interaction ◽  
Single Stranded Dna ◽  
Ssdna Binding ◽  
Papillomavirus Dna

ABSTRACT With the exception of viral proteins E1 and E2, papillomaviruses depend heavily on host replication machinery for replication of their viral genome. E1 and E2 are known to recruit many of the necessary cellular replication factors to the viral origin of replication. Previously, we reported a physical interaction between E1 and the major human single-stranded DNA (ssDNA)-binding protein, replication protein A (RPA). E1 was determined to bind to the 70-kDa subunit of RPA, RPA70. In this study, using E1-affinity coprecipitation and enzyme-linked immunosorbent assay-based interaction assays, we show that E1 interacts with the major ssDNA-binding domain of RPA. Consistent with our previous report, no measurable interaction between E1 and the two smaller subunits of RPA was detected. The interaction of E1 with RPA was substantially inhibited by ssDNA. The extent of this inhibition was dependent on the length of the DNA. A 31-nucleotide (nt) oligonucleotide strongly inhibited the E1-RPA interaction, while a 16-nt oligonucleotide showed an intermediate level of inhibition. In contrast, a 10-nt oligonucleotide showed no observable effect on the E1-RPA interaction. This inhibition was not dependent on the sequence of the DNA. Furthermore, ssDNA also inhibited the interaction of RPA with papillomavirus E2, simian virus 40 T antigen, human polymerase alpha-primase, and p53. Taken together, our results suggest a potential role for ssDNA in modulating RPA-protein interactions, in particular, the RPA-E1 interactions during papillomavirus DNA replication. A model for recruitment of RPA by E1 during papillomavirus DNA replication is proposed.

scholarly journals Single-stranded-DNA binding alters human replication protein A structure and facilitates interaction with DNA-dependent protein kinase.

1996 ◽  
Vol 16 (9) ◽  
pp. 4798-4807 ◽  
Author(s):  
L J Blackwell ◽  
J A Borowiec ◽  
I A Mastrangelo
Keyword(s):  
Protein Kinase ◽  
Dna Binding ◽  
Protein A ◽  
Replication Protein A ◽  
Replication Protein ◽  
Physical Interaction ◽  
Binding Modes ◽  
Dependent Protein Kinase ◽  
Single Stranded Dna ◽  
Dependent Protein

Human replication protein A (hRPA) is an essential single-stranded-DNA-binding protein that stimulates the activities of multiple DNA replication and repair proteins through physical interaction. To understand DNA binding and its role in hRPA heterologous interaction, we examined the physical structure of hRPA complexes with single-stranded DNA (ssDNA) by scanning transmission electron microscopy. Recent biochemical studies have shown that hRPA combines with ssDNA in at least two binding modes: by interacting with 8 to 10 nucleotides (hRPA8nt) and with 30 nucleotides (hRPA30nt). We find the relatively unstable hRPA8nt complex to be notably compact with many contacts between hRPA molecules. In contrast, on similar lengths of ssDNA, hRPA30nt complexes align along the DNA and make few intermolecular contacts. Surprisingly, the elongated hRPA30nt complex exists in either a contracted or an extended form that depends on ssDNA length. Therefore, homologous-protein interaction and available ssDNA length both contribute to the physical changes that occur in hRPA when it binds ssDNA. We used activated DNA-dependent protein kinase as a biochemical probe to detect alterations in conformation and demonstrated that formation of the extended hRPA30nt complex correlates with increased phosphorylation of the hRPA 29-kDa subunit. Our results indicate that hRPA binds ssDNA in a multistep pathway, inducing new hRPA alignments and conformations that can modulate the functional interaction of other factors with hRPA.

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