A single-molecule mechanical assay to study DNA replication coupled to DNA unwinding View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2008

AUTHORS

B. Ibarra , J. A. Morin , R. Arias , S. Hormeño , M. Salas , J. M. Valpuesta , J. L. Carrascosa

ABSTRACT

Mechanical force at the molecular level is involved in the action of many enzymes. For example, during DNA replication the mechanical unwinding of the DNA helix is required to separate the two complementary strands which are used by the DNA polymerases to generate two identical copies of DNA [1]. A tight coupling between these two activities (unwinding and replication) is required for the proper progress of the reaction. Some organisms like the bacteriophage Phi29 have coupled these two processes within the same protein. The Phi29 DNA polymerase unwinds the doublestranded DNA (dsDNA) helix as it replicates in a processive manner one of the DNA strands [2]. This polymerase works as a molecular motor converting the energy provided by the incoming nucleotides (dNTPs) into mechanical work as it moves unidirectionally along the DNA unwinding its helical structure. More... »

PAGES

223-224

Book

TITLE

EMC 2008 14th European Microscopy Congress 1–5 September 2008, Aachen, Germany

ISBN

978-3-540-85227-8
978-3-540-85228-5

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-3-540-85228-5_112

DOI

http://dx.doi.org/10.1007/978-3-540-85228-5_112

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1007873389


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