Nicholas R. Cozzarelli

TL;DR: Gyrase is a prototype for a growing class of prokaryotic and eukaryotic topoisomerases that interconvert complex forms by way of transient double-strand breaks.

TL;DR: Temperature-sensitive nalA mutants of Escherichia coli have been used to investigate the structure and functions of deoxyribonucleic acid (DNA) gyrase, proving definitively that n alA is the structural gene for subunit A and the nalidixic acid target are one and the same protein.

TL;DR: Gyrase is representative of a general class of enzymes, found in both procaryotic and eucaryotic cells, that facilitate diffusion of duplex DNA segments through each other and may solve topological problems arising from the replication, recombination and condensation of DNA.

TL;DR: Analysis of cleavage fragments showed that cutting between a TG doublet is common to most, or all, gyrase cleavages, and this diverse recognition sequence with common elements is a pattern shared with several other specific nucleic acid-protein interactions.

TL;DR: The results suggest that adenosine 3',5'-monophosphate results in induction of excessively high levels of an early rate-limiting step in xylose metabolism, which may be the transport ofxylose into the cell.