RNA remodeling by hexameric RNA helicases.
The unwinding of RNA helices and the disruption of RNA-protein complexes are critical steps of cellular metabolism that are carried out by ubiquitous NTP-dependent enzymes named RNA helicases. Here, we review the structures, mechanisms, and biochemical properties of two RNA helicases known to adopt a homo-hexameric ring architecture: the P4 packaging motor of bacteriophage φ8, a Super-Family 4 helicase, and Escherichia coli's transcription termination factor Rho from the Super-Family 5 of helicases. We emphasize the many similarities as well as key differences that characterize the Rho and P4 motor mechanisms and highlight important questions that remain to be addressed.
CNRS UPR4301, Centre de Biophysique Moléculaire, Orléans cedex, France.
Makhlouf
M
Rabhi
Roman
R
Tuma
Marc
M
Boudvillain
D001435:Bacteriophages / Q000201:enzymology; D004706:Endodeoxyribonucleases / Q000737:chemistry / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology; D009711:Nucleotides / Q000378:metabolism; D012313:RNA / Q000737:chemistry* / Q000378:metabolism*; D020365:RNA Helicases / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity; D054460:rho-Associated Kinases / Q000737:chemistry / Q000378:metabolism
D009711:Nucleotides; D012313:RNA; D054460:rho-Associated Kinases; D004706:Endodeoxyribonucleases; D020365:RNA Helicases