Characterisation of the interaction between the nucleoprotein and phosphoprotein of pneumonia virus of mice.
A protein blotting technique was used to study the interaction occurring between the pneumonia virus of mice N protein and other PVM encoded proteins expressed in infected cells. Measurement of the degree of binding indicated that the N protein specifically interacted only with the full-length 39 kDa P protein in infected cells. Truncated N-related proteins were synthesised in vitro and incubated with filter-bound full-length and truncated P proteins. The data suggested that many regions of the N protein are cooperatively involved in the binding process. It was also determined that both the amino and the carboxyl-terminal regions of the PVM P protein were essential for binding to N protein.
Barr
J
J
Department of Biological Sciences, University of Warwick, Coventry, UK.
Easton
A J
AJ
D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D002460:Cell Line; D017931:DNA Primers; D051379:Mice; D008969:Molecular Sequence Data; D019251:Nucleocapsid / Q000235:genetics / Q000378:metabolism*; D009698:Nucleoproteins / Q000235:genetics / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism*; D018111:Pneumovirus / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D017931:DNA Primers; D009698:Nucleoproteins; D010750:Phosphoproteins