Doore, S. M., Baird, C., The 2012 University of Arizona Virology Undergraduate Lab, ., Roznowski, A. P., & Fane, B. A. (2014). The evolution of genes within genes and the control of DNA replication in Microviruses. Molecular Biology and Evolution, 31(6), 1421-1431.
Approximately 20% of the data in this manuscript was generated by students enrolled in the 2012 Summer Virology Lab Course.
Fane, B. A., & Hayashi, M. (1991). Second-site suppressors of a cold-sensitive prohead accessory protein of bacteriophage ΦX174. Genetics, 128(4), 663-671.
PMID: 1833267;PMCID: PMC1204541;Abstract:
This study describes the isolation of second-site suppressors which correct for the defects associated with cold-sensitive (cs) prohead accessory proteins of bacteriophage ΦX174. Five phenotypically different suppressors were isolated. Three of these suppressors confer novel temperature-sensitive (ts) phenotypes. They were unable to complement a ts mutation in gene F which encodes the major coat protein of the phage. All five suppressor mutations confer nucleotide changes in the gene F DNA sequence. These changes define four amino acid sites in the gene F protein. Three suppressor mutations placed into an otherwise wild-type background display a cold resistant phenotype in liquid culture infections when compared to a wild-type ΦX174 control.
Fane, B. A., & Prevelige Jr., P. E. (2003). Mechanism of scaffolding-assisted viral assembly. Advances in Protein Chemistry, 64, 259-299.
Fane, B. A., Head, S., & Hayashi, M. (1992). Functional relationship between the J proteins of bacteriophages φX174 and G4 during phage morphogenesis. Journal of Bacteriology, 174(8), 2717-2719.
PMID: 1532571;PMCID: PMC205913;Abstract:
The functions of the small DNA-binding protein, gpJ, of bacteriophages φX174 and G4 were examined by in vivo cross-complementation and sucrose gradient sedimentation. The morphogenetic roles of the two proteins may differ. The φX174 J protein may be required for the formation or stabilization of the φX174 prohead.
Uchiyama, A., Heiman, P., & Fane, B. A. (2009). N-terminal deletions of the øX174 external scaffolding protein affect the timing and fidelity of assembly. Virology, 386(2), 303-309.
PMID: 19237183;Abstract:
The first α-helices of Microviridae external scaffolding proteins function as coat protein substrate specificity domains. Mutations in this helix can lengthen the lag phase before progeny production. 5′ deletion genes, encoding N-terminal deletion proteins, were constructed on plasmids and in the øX174 genome. Proteins lacking the first seven amino acids were able to rescue a nullD mutant when expressed from a plasmid. However, the lag phase before progeny production was lengthened. The øX174 mutant with the corresponding genomic gene grew very poorly. The molecular basis of the defective phenotype was complex. External scaffolding protein levels were reduced compared to wild-type and most of the viral coat protein in mutant infected cells appears to be siphoned off the assembly pathway. Second-site suppressors of the growth defects were isolated and appear to act via two different mechanisms. One class of suppressors most likely acts by altering mutant external scaffolding protein expression while the second class of suppressors appears to act on the level of protein-protein interactions. © 2009 Elsevier Inc. All rights reserved.
