A model for dsDNA translocation revealed by a structural motif common to RecG and Mfd proteins

RecG protein differs from other helicases analysed to atomic resolution in that it mediates strand separation via translocation on double‐stranded (ds) rather than single‐stranded (ss) DNA. We describe a highly conserved helical hairpin motif in RecG and show it to be important for helicase activity...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	The EMBO journal 2003-02, Vol.22 (3), p.724-734
Hauptverfasser:	Mahdi, Akeel A., Briggs, Geoffrey S., Sharples, Gary J., Wen, Qin, Lloyd, Robert G.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - metabolism Amino Acid Sequence Arginine - metabolism Bacterial Proteins - chemistry Bacterial Proteins - metabolism Deoxyribonucleic acid DNA DNA - metabolism DNA Helicases - chemistry DNA Helicases - metabolism DNA replication DNA Replication - physiology DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism EMBO09 EMBO13 Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Holliday junctions Hydrogen Bonding Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Protein Structure, Secondary Protein Structure, Tertiary RecB recombination repair RuvABC Sequence Alignment Transcription Factors - chemistry Transcription Factors - metabolism Translocation
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!