Discovery of a new motion mechanism of biomotors similar to the earth revolving around the sun without rotation.
Biomotors have been classified into linear and rotational motors. For 35 years, it has been popularly believed that viral dsDNA-packaging apparatuses are pentameric rotation motors. Recently, a third class of hexameric motor has been found in bacteriophage phi29 that utilizes a mechanism of revolution without rotation, friction, coiling, or torque. This review addresses how packaging motors control dsDNA one-way traffic; how four electropositive layers in the channel interact with the electronegative phosphate backbone to generate four steps in translocating one dsDNA helix; how motors resolve the mismatch between 10.5 bases and 12 connector subunits per cycle of revolution; and how ATP regulates sequential action of motor ATPase. Since motors with all number of subunits can utilize the revolution mechanism, this finding helps resolve puzzles and debates concerning the oligomeric nature of packaging motors in many phage systems. This revolution mechanism helps to solve the undesirable dsDNA supercoiling issue involved in rotation.
Nanobiotechnology Center, and Markey Cancer Center, Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington, KY 40536, USA. Electronic address: peixuan.guo@uky.edu.
Peixuan
P
Guo
Chad
C
Schwartz
Jeannie
J
Haak
Zhengyi
Z
Zhao
D000255:Adenosine Triphosphate / Q000378:metabolism; D042003:DNA Packaging; D004279:DNA, Viral / Q000378:metabolism*; D008954:Models, Biological; D014764:Viral Proteins / Q000378:metabolism*; D018406:Virus Physiological Phenomena
D004279:DNA, Viral; D014764:Viral Proteins; D000255:Adenosine Triphosphate
AAA+ ATPase Superfamily; Bionanomotor; DNA packaging; Nanobiotechnology; One-way Traffic Mechanism; Virus Assembly