Interaction of Hantavirus Nucleocapsid Protein with Ribosomal Protein S19
نویسندگان
چکیده
منابع مشابه
Interaction between molecules of hantavirus nucleocapsid protein.
Intermolecular interactions of Tula hantavirus N (nucleocapsid) protein were detected in the yeast two-hybrid system, prompting further attempts to study this phenomenon. Using chemical cross-linking and immunoblotting it was shown that the N protein from purified virus and from infected cell lysates as well as recombinant protein produced in a baculovirus expression system are capable of formi...
متن کاملHantavirus nucleocapsid protein oligomerization.
Hantaviruses are enveloped, negative-strand RNA viruses which can be lethal to humans, causing either a hemorrhagic fever with renal syndrome or a hantaviral pulmonary syndrome. The viral genomes consist of three RNA segments: the L segment encodes the viral polymerase, the M segment encodes the viral surface glycoproteins G1 and G2, and the S segment encodes the nucleocapsid (N) protein. The N...
متن کاملRibosomal protein S19 expression during erythroid differentiation.
The gene encoding ribosomal protein S19 (RPS19) has been shown to be mutated in 25% of the patients affected by Diamond-Blackfan anemia (DBA), a congenital erythroblastopenia. As the role of RPS19 in erythropoiesis is still to be defined, we performed studies on RPS19 expression during terminal erythroid differentiation. Comparative analysis of the genomic sequences of human and mouse RPS19 gen...
متن کاملCharacterization of the RNA chaperone activity of hantavirus nucleocapsid protein.
Hantaviruses are tripartite negative-sense RNA viruses and members of the Bunyaviridae family. The nucleocapsid (N) protein, encoded by the smallest of the three genome segments (S), has nonspecific RNA chaperone activity. This activity results in transient dissociation of misfolded RNA structures, may be required for facilitating correct higher-order RNA structure, and may function in viral ge...
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ژورنال
عنوان ژورنال: Journal of Virology
سال: 2010
ISSN: 0022-538X,1098-5514
DOI: 10.1128/jvi.01388-10