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The Human Cytomegalovirus UL44 C Clamp Wraps around DNA
- Source :
-
Structure . Aug2008, Vol. 16 Issue 8, p1214-1225. 12p. - Publication Year :
- 2008
-
Abstract
- Summary: Processivity factors tether the catalytic subunits of DNA polymerases to DNA so that continuous synthesis of long DNA strands is possible. The human cytomegalovirus DNA polymerase subunit UL44 forms a C clamp-shaped dimer intermediate in structure between monomeric herpes simplex virus UL42, which binds DNA directly via a basic surface, and the trimeric sliding clamp PCNA, which encircles DNA. To investigate how UL44 interacts with DNA, calculations were performed in which a 12 bp DNA oligonucleotide was docked to UL44. The calculations suggested that UL44 encircles DNA, which interacts with basic residues both within the cavity of the C clamp and in flexible loops of UL44 that complete the “circle.” The results of mutational and crosslinking studies were consistent with this model. Thus, UL44 is a “hybrid” of UL42 and PCNA: its structure is intermediate between the two and its mode of interaction with DNA has elements of both. [Copyright &y& Elsevier]
Details
- Language :
- English
- ISSN :
- 09692126
- Volume :
- 16
- Issue :
- 8
- Database :
- Academic Search Index
- Journal :
- Structure
- Publication Type :
- Academic Journal
- Accession number :
- 33527844
- Full Text :
- https://doi.org/10.1016/j.str.2008.05.008