Analysis of vaccinia virus temperature-sensitive I7L mutants reveals two potential functional domains.
As an approach to initiating a structure-function analysis of the vaccinia virus I7L core protein proteinase, a collection of conditional-lethal mutants in which the mutation had been mapped to the I7L locus were subjected to genomic sequencing and phenotypic analyses. Mutations in six vaccinia virus I7L temperature sensitive mutants fall into two groups: changes at three positions at the N-terminal end between amino acids 29 and 37 and two different substitutions at amino acid 344, near the catalytic domain. Regardless of the position of the mutation, mutants at the non-permissive temperature failed to cleave core protein precursors and had their development arrested prior to core condensation. Thus it appears that the two clusters of mutations may affect two different functional domains required for proteinase activity.
Moerdyk
Megan J
MJ
Department of Microbiology, Oregon State University, Corvallis, OR 97331, USA. moerdykm@onid.orst.edu
Byrd
Chelsea M
CM
Hruby
Dennis E
DE
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D020134:Catalytic Domain; D017124:Conserved Sequence; D009154:Mutation; D016366:Open Reading Frames; D010447:Peptide Hydrolases / Q000235:genetics; D013696:Temperature; D014616:Vaccinia virus / Q000201:enzymology / Q000235:genetics*; D014758:Viral Core Proteins / Q000235:genetics*
D014758:Viral Core Proteins; D010447:Peptide Hydrolases