5guj
Crystal structure of the Bacillus subtilis DnaG RNA Polymerase Domain, natural degradation of full length DnaGCrystal structure of the Bacillus subtilis DnaG RNA Polymerase Domain, natural degradation of full length DnaG
Structural highlights
FunctionDNAG_BACSU RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.[HAMAP-Rule:MF_00974] Publication Abstract from PubMedBacterial primase initiates the repeated synthesis of short RNA primers that are extended by DNA polymerase to synthesize Okazaki fragments on the lagging strand at replication forks. It remains unclear how the enzyme recognizes specific initiation sites. In this study, the DnaG primase from Bacillus subtilis (BsuDnaG) was characterized and the crystal structure of the RNA polymerase domain (RPD) was determined. Structural comparisons revealed that the tethered zinc binding domain plays an important role in the interactions between primase and specific template sequence. Structural and biochemical data defined the ssDNA template binding surface as an L shape, and a model for the template ssDNA binding to primase is proposed. The flexibility of the DnaG primases from B. subtilis and G. stearothermophilus were compared, and the results implied that the intrinsic flexibility of the primase may facilitate the interactions between primase and various partners in the replisome. These results shed light on the mechanism by which DnaG recognizes the specific initiation site. Structural Insight into the Specific DNA Template Binding to DnaG primase in Bacteria.,Zhou Y, Luo H, Liu Z, Yang M, Pang X, Sun F, Wang G Sci Rep. 2017 Apr 6;7(1):659. doi: 10.1038/s41598-017-00767-8. PMID:28386108[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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