title: Hantavirus nucleocapsid protein coiled-coil domains.
abstract: The nucleocapsid (N) proteins of hantaviruses such as the Sin Nombre virus (SNV) bind to membranes and viral RNAs, associate with transcription and replication complexes, and oligomerize during the process of virus assembly. N proteins trimerize in vitro and in vivo, and associate via assembly domains at their amino- and carboxyl-terminal ends. Because structure prediction algorithms suggested that N protein residues 3-75 form two coiled-coil motifs separated by an intervening kink or turn sequence, we examined the properties of peptides representing SNV N protein residues 3-35, 43-75, and 3-75. Of the three peptides, N-(3-35) assembled coiled-coil oligomers only at high concentration and low temperature. In contrast, N-(43-75) efficiently trimerized at low concentration, implying that it carries a coiled-coil trigger sequence. Interestingly, while the longer peptide, N-(3-75), assembled dimers and/or trimers at high concentration, at low concentration it appeared to adopt an intramolecular helix-turn-helix conformation. These results suggest that N protein oligomerization involves the bundling of intramolecular antiparallel coils or a conformational switch from intra- to intermolecular coiled-coils.
authors.affiliation: Department of Microbiology, Vollum Institute, Oregon Health & Sciences University, Portland, OR 97201-3098, USA.
authors.forename: Ayna
authors.initials: A
authors.lastname: Alfadhli
authors.forename: Eric
authors.initials: E
authors.lastname: Steel
authors.forename: Liam
authors.initials: L
authors.lastname: Finlay
authors.forename: Hans Peter
authors.initials: HP
authors.lastname: Bächinger
authors.forename: Eric
authors.initials: E
authors.lastname: Barklis
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D002213:Capsid / Q000737:chemistry* / Q000378:metabolism*; D036022:Capsid Proteins; D002942:Circular Dichroism; D003432:Cross-Linking Reagents / Q000494:pharmacology; D019281:Dimerization; D005976:Glutaral / Q000494:pharmacology; D008027:Light; D008969:Molecular Sequence Data; D010452:Peptide Biosynthesis; D010455:Peptides / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012542:Scattering, Radiation; D017386:Sequence Homology, Amino Acid; D013696:Temperature; D014461:Ultracentrifugation; D014758:Viral Core Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D036022:Capsid Proteins; D003432:Cross-Linking Reagents; D010455:Peptides; D014758:Viral Core Proteins; C111782:nucleocapsid protein, Hantaan virus; D005976:Glutaral