'Let the phage do the work': using the phage P22 coat protein structures as a framework to understand its folding and assembly mutants.
The amino acid sequence of viral capsid proteins contains information about their folding, structure and self-assembly processes. While some viruses assemble from small preformed oligomers of coat proteins, other viruses such as phage P22 and herpesvirus assemble from monomeric proteins (Fuller and King, 1980; Newcomb et al., 1999). The subunit assembly process is strictly controlled through protein:protein interactions such that icosahedral structures are formed with specific symmetries, rather than aberrant structures. dsDNA viruses commonly assemble by first forming a precursor capsid that serves as a DNA packaging machine (Earnshaw, Hendrix, and King, 1980; Heymann et al., 2003). DNA packaging is accompanied by a conformational transition of the small precursor procapsid into a larger capsid for isometric viruses. Here we highlight the pseudo-atomic structures of phage P22 coat protein and rationalize several decades of data about P22 coat protein folding, assembly and maturation generated from a combination of genetics and biochemistry.
Department of Molecular and Cell Biology, 91 N. Eagleville Rd., U-3125, University of Connecticut, Storrs, CT 06269-3125, USA. Teschke@uconn.edu
Carolyn M
CM
Teschke
Kristin N
KN
Parent
D017100:Bacteriophage P22 / Q000737:chemistry* / Q000235:genetics; D036022:Capsid Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008954:Models, Biological; D050505:Mutant Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017510:Protein Folding; D055503:Protein Multimerization; D019065:Virus Assembly
D036022:Capsid Proteins; D050505:Mutant Proteins