[Temporary acquisition of intra-chain disulphide bonds by nucleocapsid protein of influenza virus].
The in vitro reducing agents were shown to promote the NP-NP association and to stabilize the NP oligomers, which dissociate when heated in non-reducing buffer. This confirms that non-covalent linkages in electrophoresis stabilize the influenza virus NP oligomers. The mobility of pulse-labeled and chased NPs in PAGE as well as their sensitivity to protease were investigated. The S-S bonds reduce at later stages of conformational maturation of NP; the disulfide-containing NP transforms itself into an NP free of S-S bonds with non-covalently linked NP-oligomers being subsequently formed. Presumably, the early disulfide-dependent stage in NP maturation is needed for the correct NP-NP association and for the protection of early monomeric NPs against protease action.
Semenova
N P
NP
Prokudina
E N
EN
Chumakov
V M
VM
Grigor'eva
T A
TA
Rudneva
I A
IA
D004220:Disulfides / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D006361:Heating; D009980:Influenza A virus / Q000378:metabolism*; D009698:Nucleoproteins / Q000737:chemistry / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism; D017510:Protein Folding; D014779:Virus Replication
D004220:Disulfides; D009698:Nucleoproteins; D010447:Peptide Hydrolases