scholarly journals ERRATUM: Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA

Nature ◽  
1995 ◽  
Vol 376 (6541) ◽  
pp. 616-616 ◽  
Author(s):  
Yousif Shamoo ◽  
Alan M. Friedman ◽  
Mark R. Parsons ◽  
William H. Konigsberg ◽  
Thomas A. Steitz
Keyword(s):  
Crystal Structure ◽  
Dna Binding ◽  
Replication Fork ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Single Stranded Dna

Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA

Nature ◽  
1995 ◽  
Vol 376 (6538) ◽  
pp. 362-366 ◽  
Author(s):  
Yousif Shamoo ◽  
Alan M. Friedman ◽  
Mark R. Parsons ◽  
William H. Konigsberg ◽  
Thomas A. Steitz
Keyword(s):  
Crystal Structure ◽  
Dna Binding ◽  
Replication Fork ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Single Stranded Dna

scholarly journals Dual Functions of Single-stranded DNA-binding Protein in Helicase Loading at the Bacteriophage T4 DNA Replication Fork

2004 ◽  
Vol 279 (18) ◽  
pp. 19035-19045 ◽  
Author(s):  
Yujie Ma ◽  
Tongsheng Wang ◽  
Jana L. Villemain ◽  
David P. Giedroc ◽  
Scott W. Morrical
Keyword(s):  
Dna Replication ◽  
Dna Binding ◽  
Replication Fork ◽  
Binding Protein ◽  
Bacteriophage T4 ◽  
Dna Binding Protein ◽  
Single Stranded Dna ◽  
Helicase Loading ◽  
Dual Functions

Crystal structure of human mitochondrial single-stranded DNA binding protein at 2.4 Å resolution

1997 ◽  
Vol 4 (2) ◽  
pp. 153-157 ◽  
Author(s):  
Cheng Yang ◽  
Ute Curth ◽  
Claus Urbanke ◽  
ChulHee Kang
Keyword(s):  
Crystal Structure ◽  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Single Stranded Dna

scholarly journals Parvovirus Initiator Protein NS1 and RPA Coordinate Replication Fork Progression in a Reconstituted DNA Replication System

2002 ◽  
Vol 76 (13) ◽  
pp. 6518-6531 ◽  
Author(s):  
Jesper Christensen ◽  
Peter Tattersall
Keyword(s):  
Dna Binding ◽  
Replication Fork ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Small Subunit ◽  
Dna Helicase ◽  
Enzyme Linked Immunosorbent Assay ◽  
Helicase Activity ◽  
Single Stranded Dna ◽  
Initiator Protein

ABSTRACT We show here that the DNA helicase activity of the parvoviral initiator protein NS1 is highly directional, binding to the single strand at a recessed 5′ end and displacing the other strand while progressing in a 3′-to-5′ direction on the bound strand. NS1 and a cellular site-specific DNA binding factor, PIF, also known as glucocorticoid modulating element binding protein, bind to the left-end minimal replication origin of minute virus of mice, forming a ternary complex. In this complex, NS1 is activated to nick one DNA strand, becoming covalently attached to the 5′ end of the nick in the process and providing a 3′ OH for priming DNA synthesis. In this situation, the helicase activity of NS1 did not displace the nicked strand, but the origin duplex was distorted by the NS1-PIF complex, as assayed by its sensitivity to KMnO4 oxidation, and a stretch of about 14 nucleotides on both strands of the nicked origin underwent limited unwinding. Addition of Escherichia coli single-stranded DNA binding protein (SSB) did not lead to further unwinding. However, addition of recombinant human single-stranded DNA binding protein (RPA) to the initiation reaction catalyzed extensive unwinding of the nicked origin, suggesting that RPA may be required to form a functional replication fork. Accordingly, the unwinding mediated by NS1 and RPA promoted processive leading-strand synthesis catalyzed by recombinant human DNA polymerase δ, PCNA, and RFC, using the minimal left-end origin cloned in a plasmid as a template. The requirement for RPA, rather than SSB, in the unwinding reaction indicated that specific NS1-RPA protein interactions were formed. NS1 was tested by enzyme-linked immunosorbent assay for binding to two- or three-subunit RPA complexes expressed from recombinant baculoviruses. NS1 efficiently bound each of the baculovirus-expressed complexes, indicating that the small subunit of RPA is not involved in specific NS1 binding. No NS1 interactions were observed with E. coli SSB or other proteins included as controls.

Crystal structure of a single-stranded DNA-binding protein (TM0604) from Thermotoga maritima at 2.60 Å resolution

2006 ◽  
Vol 63 (1) ◽  
pp. 256-260 ◽  
Author(s):  
Michael DiDonato ◽  
S. Sri Krishna ◽  
Robert Schwarzenbacher ◽  
Daniel McMullan ◽  
Lukasz Jaroszewski ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Dna Binding ◽  
Thermotoga Maritima ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Single Stranded Dna
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