DNA recognition properties of the N-terminal DNA binding domain within the large subunit of replication factor C Journal Article

   


Authors: Allen, B. L.; Gaur, L. K.; Uhlmann, F.; Mulder, B. A.; Posey, K. L.; Jones, L. B.; Hardin, S. H.
Article Title: DNA recognition properties of the N-terminal DNA binding domain within the large subunit of replication factor C
Abstract: Replication Factor C (RFC) is a five-subunit protein complex required for eukaryotic DNA replication and repair. The large subunit within this complex contains a C-terminal DNA binding domain which provides specificity for PCNA loading at a primer-template and a second, N-terminal DNA binding domain of unknown function. We isolated the N-terminal DNA binding domain from Drosophila melanogasterand defined the region within this polypeptide required for DNA binding. The DNA determinants most efficiently recognized by both the Drosophila minimal DNA binding domain and the N-terminal half of the human large subunit consist of a double-stranded DNA containing a recessed 5' phosphate. DNA containing a recessed 5' phosphate was preferred 5-fold over hairpined DNA containing a recessed 3' hydroxyl. Combined with existing data, these DNA binding properties suggest a role for the N-terminal DNA binding domain in the recognition of phosphorylated DNA ends.
Keywords: controlled study; unclassified drug; dna binding protein; dna-binding proteins; nonhuman; dna replication; animals; protein binding; homeodomain proteins; structure activity relation; cloning, molecular; dna; double stranded dna; amino acid sequence; conserved sequence; amino terminal sequence; eukaryota; molecular recognition; nucleotide sequence; peptide fragments; binding sites; drosophila melanogaster; saccharomyces cerevisiae proteins; replication factor c; protein subunit; replication protein c; repressor proteins; phosphate; proto-oncogene proteins c-bcl-2; protein dna interaction; hydroxyl group; melanogaster; humans; priority journal; article
Journal Title: Nucleic Acids Research
Volume: 26
Issue: 17
ISSN: 0305-1048
Publisher: Oxford University Press  
Date Published: 1998-09-01
Start Page: 3877
End Page: 3882
Language: English
PUBMED: 9705493
PROVIDER: scopus
PMCID: PMC147807
DOI: 10.1093/nar/26.17.3877
DOI/URL:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032168765&partnerID=40&md5=86ea44411653cf02d0e04c7faccc65d8
Notes: Article -- Export Date: 12 December 2016 -- Source: Scopus
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