Efficient complementation by chimeric Microviridae internal scaffolding proteins is a function of the COOH-terminus of the encoded protein

Virology

Volumn 270, Issue 2, 2000, Pages 286-290

  Burch, April D ^a   Fane, Bentley A ^a  

^a UNIVERSITY OF ARIZONA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHIMERIC PROTEIN; COAT PROTEIN; STRUCTURAL PROTEIN;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; GENE DELETION; GENETIC COMPLEMENTATION; MICROVIRIDAE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN EXPRESSION; TEMPERATURE DEPENDENCE; VIRUS MORPHOGENESIS;

MICROVIRIDAE; UNIDENTIFIED BACTERIOPHAGE;

EID: 0034630932     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.2000.0306     Document Type: Article

References (16)

1. Baudet-Miller M., Zhang R., Durkin J., Gibson W., Kwong A. D., Hong Z. Virus-specific interaction between the Human Cytomegalovirus major capsid protein and the C terminus of the assembly protein precursor. J. Virol. 70:1996;8081-8088.
2. Bazinet C., King J. Initiation of P22 procapsid assembly in vivo. J. Mol. Biol. 202:1988;77-86.
3. Burch A. D., Ta J., Fane B. A. Cross-functional analysis of the Microviridae internal scaffolding protein. J. Mol. Biol. 286:1999;95-104.
4. Casjens S., Hendrix R. Control mechanisms in dsDNA bacteriophage assembly. Calendar R. The Bacteriophages. 1988;15-91 Plenum, New York.
5. Dokland T., Bernal R. A., Burch A., Pletnev S., Fane B. A., Rossmann M. G. The role of scaffolding proteins in the assembly of the small, single-stranded DNA virus φX174. J. Mol. Biol. 288:1999;595-608.
6. Dokland T., McKenna R., Ilag L. L., Bowman B. R., Incardona N. L., Fane B. A., Rossmann M. G. Structure of a viral procapsid with molecular scaffolding. Nature. 389:1997;308-313.
7. Ekechukwu M. C., Fane B. A. Characterization of the morphogenetic defects conferred by cold-sensitive prohead accessory and scaffolding proteins of φX174. J. Bacteriol. 177:1995;829-830.
8. Fane B. A., Hayashi M. Second-site suppressors of a cold-sensitive prohead accessory protein of bacteriophage φX174. Genetics. 128:1991;663-671.
9. Hayashi M., Aoyama A., Richardson D. L., Hayashi M. N. Biology of the bacteriophage φX174. Calendar R. The Bacteriophages. 1988;1-71 Plenum, New York.
10. King J., Griffin-Shea R., Fuller M. T. Scaffolding proteins and the genetic control of virus shell assembly. Quart. Rev. Biol. 55:1980;369-393.
11. Parker M. H., Casjens S., Prevelige P. E. Jr. Functional domains of bacteriophage P22 scaffolding protein. J. Mol. Biol. 281:1998;69-79.
12. Preston V. G., Kennard J., Rixon F. J., Logan A. J., Mansfield R. W., McDougall I. M. Efficient herpes simplex virus type 1 (HSV-1) capsid formation directed by the varicella-zoster virus scaffolding protein requires the carboxy-terminal sequences from the HSV-1 homologue. J. Gen. Virol. 78:1997;1633-1646.
13. Siden E. J., Hayashi M. Role of the gene B product in bacteriophage φX174 development. J. Mol. Biol. 89:1974;1-16.
14. Thuman-Commike P. A., Greene B., Jakana J., Prasad B. V. V., King J., Prevelige P. E., Chi W. Three-dimensional structure of scaffolding-containing phage P22 procapsids by electron cryo-microscopy. J. Mol. Biol. 260:1996;85-98.
15. Tuma R., Parker M. H., Weigele P., Sampson L., Sun Y., Krishna N. R., Casjens S., Thomas G. J., Prevelige P. E. A helical coat protein recognition domain of the bacteriophage P22 scaffolding protein. J. Mol Biol. 281:1998;81-94.
16. Zhou Z. H., Macnab S. J., Jakana J., Scott L. R., Chiu W. Identification of the sites of interaction between the scaffold and outer shell in herpes simplex virus-1 capsids by difference electron imaging. Proc. Natl. Acad. Sci. USA. 95:1998;2778-2783.