Structure and function of phi29 hexameric RNA that drives the viral DNA packaging motor: review.
One notable feature of linear dsDNA viruses is that, during replication, their lengthy genome is squeezed with remarkable velocity into a preformed procapsid and packed into near crystalline density. A molecular motor using ATP as energy accomplishes this energetically unfavorable motion tack. In bacterial virus phi29, an RNA (pRNA) molecule is a vital component of this motor. This 120-base RNA has many novel and distinctive features. It contains strong secondary structure, is tightly folded, and unusually stable. Upon interaction with ion and proteins, it has a knack to adapt numerous conformations to perform versatile function. It can be easily manipulated to form stable homologous monomers, dimers, trimers and hexamers. As a result, many unknown properties of RNA have been and will be unfolded by the study of this extraordinary molecule. This article reviews the structure and function of this pRNA and focuses on novel methods and unique approaches that lead to the illumination of its structure and function.
Department of Pathobiology and Purdue Cancer Center, Purdue University, West Lafayette, Indiana 47907, USA.
Peixuan
P
Guo
D017103:Bacillus Phages / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D001483:Base Sequence; D002213:Capsid / Q000378:metabolism; D004279:DNA, Viral / Q000378:metabolism*; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D012367:RNA, Viral / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D013329:Structure-Activity Relationship; D019065:Virus Assembly / Q000502:physiology*
D004279:DNA, Viral; D012367:RNA, Viral