Detection of RNA-protein complex in vaccinia virus core in vitro transcription system

• Published in: Journal of general virology Vol. 73; no. 5; pp. 1243 - 1249
• Main Authors: Damaso, Clarissa R. A, Moussatche, Nissin
• Format: Journal Article
• Language: English
• Published: Reading Soc General Microbiol 01.05.1992; Society for General Microbiology
• Subjects: Biological and medical sciences; Fundamental and applied biological sciences. Psychology; Microbiology; Micrococcal Nuclease - metabolism; Morphology, structure, chemical composition, physicochemical properties; Ribonucleoproteins - chemistry; Ribonucleoproteins - metabolism; RNA, Messenger - biosynthesis; RNA, Viral - biosynthesis; Transcription, Genetic; vaccinia virus; Vaccinia virus - chemistry; Vaccinia virus - genetics; Vaccinia virus - metabolism; Viral Core Proteins - metabolism; Virology; Virus; Proteins; Vaccinia virus; Chordopoxvirinae; Ribonucleoprotein; Messenger RNA; Poxviridae; Orthopoxvirus; Molecular complex
• ISSN: 0022-1317; 1465-2099
• DOI: 10.1099/0022-1317-73-5-1243

Laboratório de Biologia Molecular de Virus, Instituto de Biofisica Carlos Chagas Filho, CCS-UFRJ, 21941 Rio de Janeiro, RJ, Brazil The incubation of vaccinia virus cores in appropriate conditions promotes the release of core proteins into a supernatant fraction. Under transcription assay conditions core mRNAs are extruded in association with viral core proteins, however the presence of these proteins within the core particle is not essential for RNA synthesis and extrusion. The RNA-protein complex is resistant to micrococcal nuclease. Five proteins of 60K, 43K, 28K, 18K and 14.5K with RNA-binding abilities have been identified by [ 32 P]RNA overlay protein blot assays. These proteins are likely to be a component of the viral ribonucleoprotein complex since core basic proteins with similar M r s have been identified and at least one RNA-binding protein is predicted in the vaccinia virus genome. Received 11 October 1991; accepted 20 January 1992.