Characterization of the Hantaan nucleocapsid protein-ribonucleic acid interaction - PubMed (original) (raw)
. 1999 Nov 19;274(47):33732-9.
doi: 10.1074/jbc.274.47.33732.
Affiliations
- PMID: 10559265
- DOI: 10.1074/jbc.274.47.33732
Free article
Characterization of the Hantaan nucleocapsid protein-ribonucleic acid interaction
W Severson et al. J Biol Chem. 1999.
Free article
Abstract
The nucleocapsid (N) protein functions in hantavirus replication through its interactions with the viral genomic and antigenomic RNAs. To address the biological functions of the N protein, it was critical to first define this binding interaction. The dissociation constant, K(d), for the interaction of the Hantaan virus (HTNV) N protein and its genomic S segment (vRNA) was measured under several solution conditions. Overall, increasing the NaCl and Mg(2+) in these binding reactions had little impact on the K(d). However, the HTNV N protein showed an enhanced specificity for HTNV vRNA as compared with the S segment open reading frame RNA or a nonviral RNA with increasing ionic strength and the presence of Mg(2+). In contrast, the assembly of Sin Nombre virus N protein-HTNV vRNA complexes was inhibited by the presence of Mg(2+) or an increase in the ionic strength. The K(d) values for HTNV and Sin Nombre virus N proteins were nearly identical for the S segment open reading frame RNA, showing weak affinity over several binding reaction conditions. Our data suggest a model in which specific recognition of the HTNV vRNA by the HTNV N protein resides in the noncoding regions of the HTNV vRNA.