Mar 25, 2011

Single-molecule FRET reveals nucleotide-driven conformational changes in molecular machines and their link to RNA unwinding and DNA supercoiling

Biochemical Society Transactions
Dagmar Klostermeier

Abstract

Many complex cellular processes in the cell are catalysed at the expense of ATP hydrolysis. The enzymes involved bind and hydrolyse ATP and couple ATP hydrolysis to the catalysed process via cycles of nucleotide-driven conformational changes. In this review, I illustrate how smFRET (single-molecule fluorescence resonance energy transfer) can define the underlying conformational changes that drive ATP-dependent molecular machines. The first example is a DEAD-box helicase that alternates between two different conformations in its catalytic cycle during RNA unwinding, and the second is DNA gyrase, a topoisomerase that undergoes a set of concerted conformational changes during negative supercoiling of DNA.

Mentioned in this Paper

RNA Conformation
Bacterial Proteins
Enzymes, antithrombotic
DEAD-box RNA Helicases
Topoisomerase
Enzymes for Treatment of Wounds and Ulcers
Topoisomerase Activity
Nucleotides
Natto Bacteria
DNA, Superhelical

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