Computational characterisation of potential RNA-binding sites in arenavirus nucleocapsid proteins.
A nucleocapsid protein of an RNA virus was characterised using computational methods. Similarity searches using standard algorithms and more sensitive methods based on profiles were performed. Also, secondary structure prediction and statistical methods were used. The results show that the protein belongs to a unique well-characterised family, with three regions with potential RNA binding capacity. The amino-terminal region is found to contain a mixed-charge segment similar to proteins that bear nucleic acid-protein interaction capacity. The middle-region has a slight homology to the nucleolar protein Fibrillarin containing an atypical RNP-1 conserved octamer. Finally, the carboxyl-terminal region has a putative zinc-finger.
Parisi
G
G
Centro de Estudios e Investigaciones, Universidad Nacional de Quilmes, Bernal, Argentina.
Echave
J
J
Ghiringhelli
D
D
Romanowski
V
V
D000465:Algorithms; D000595:Amino Acid Sequence; D018050:Arenavirus / Q000378:metabolism*; D001665:Binding Sites; D003205:Computing Methodologies; D017124:Conserved Sequence; D008969:Molecular Sequence Data; D019251:Nucleocapsid / Q000378:metabolism*; D012313:RNA / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000378:metabolism*; D016415:Sequence Alignment; D016335:Zinc Fingers
D016601:RNA-Binding Proteins; D012313:RNA