Topography of a flexible ribonucleoprotein helix: protein-protein contacts in Sendai virus nucleocapsids.
J Virol, 1979/6;30(3):701-10.
Raghow R, Kingsbury DW, Portner A, George S
PMID: 225539
Impact factor: 6.549
Abstract
Contacts among the three polypeptide species in the flexible helical nucleocapsids of a paramyxovirus were examined with bifunctional protein cross-linking reagents. Polypeptides L and P, minor components of Sendai virus nucleocapsids implicated in viral RNA polymerase activity, were efficiently cross-linked into large complexes, indicating that they enjoy abundant contacts with neighboring protein molecules in the helix. Less reactivity was found in the case of the major structural polypeptide, NP; about half of all molecules of NP formed large cross-linked complexes, most of the rest remaining as monomers along with a small proportion of homodimers and low-order oligomers. Marked heterogeneity in the cross-linking reactivity of NP molecules, which may reflect the conformational quasi-equivalence inherent in a flexible helix, was indicated by the production of several conformers of homodimers and other low-order oligomers of NP, and by failure of the kinetics of NP cross-linking to conform to a simple statistical model of random polmerization. The validity of the statistical model was shown by cross-linking experiments with the rigid helical virus, tobacco mosaic virus.
MeSH terms
Capsid; Dimethyl Suberimidate; Molecular Weight; Parainfluenza Virus 1, Human; Peptides; Protein Conformation; RNA, Viral; Viral Proteins
More resources
Full text:
Europe PubMed Central; PubMed Central
EndNote: Download