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Orcid Publication

Detalle de: Quaternary Polymorphism in Helicases and the DnaB.DnaC Complex

Title Quaternary Polymorphism in Helicases and the DnaB.DnaC Complex
Abstract

Strand separation in double stranded DNA is achieved in vivo by a class of enzymes called helicases in a process fuelled by hydrolysis of nucleoside triphosphates. DnaB is the major replicative helicase in E.coli. For chromosomal replication to initiate, DnaB needs to interact with a partner protein, namely DnaC, which after properly loading DnaB onto the DNA template at the origin of replication is subsequently released from the complex. DnaB turns to be functionally active as a helicase only after DnaC has been released from the complex. The native DnaB is a homohexamer of molecular weight 318 kD. In the presence of ATP and Mg2+, the hexameric DnaB has been shown to form a complex with six molecules of DnaC (total molecular weight of the complex: 480 kD). The reconstructed 3D volume of the DnaB hexamer obtained from frozen-hydrated specimens showed the DnaB oligomer as a particle possessing three-fold rather than six-fold symmetry, despite DnaB being made up by six identical subunits.

Apa Reference Donate, L., Bárcena, M., Llorca, O., Dixon, N. & Carazo, J. (2000). Quaternary Polymorphism in Helicases and the DnaB.DnaC Complex. Microscopy and Microanalysis, 6(S2), 272-273. 10.1017/s1431927600033857
Doi 10.1017/s1431927600033857
Publication Date 1 Aug 2000
Publication Type Article
Researcher Jose María Salvador Carazo Garcia
Ontology
Research Groups
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