Literature DB >> 6206643

Reovirus RNA transcriptase: evidence for a conformational change during activation of the core particle.

K F Powell, J D Harvey, A R Bellamy.   

Abstract

Reovirus cores contain an RNA transcriptase capable of synthesizing messenger RNA. When cores are suspended in 1 X SSC at 37 degrees they are quiescent and synthesize no product, but in the presence of the components of an RNA transcriptase reaction mixture they actively synthesize mRNA. Photochemical crosslinking has been used to investigate the arrangement of RNA and protein in both "quiescent" and "active" cores. Irradiation induces the formation of a noncovalent RNA:protein complex in "quiescent" but not in "active" cores. This difference is attributed to a conformational change in the reovirus core which results from the transition between the "quiescent" and "active" states of the particle.

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Year:  1984        PMID: 6206643     DOI: 10.1016/0042-6822(84)90002-3

Source DB:  PubMed          Journal:  Virology        ISSN: 0042-6822            Impact factor:   3.616


  3 in total

1.  Conformational changes accompany activation of reovirus RNA-dependent RNA transcription.

Authors:  Israel I Mendez; Scott G Weiner; Yi-Min She; Mark Yeager; Kevin M Coombs
Journal:  J Struct Biol       Date:  2008-01-26       Impact factor: 2.867

2.  Characterization of an ATPase activity in reovirus cores and its genetic association with core-shell protein lambda1.

Authors:  S Noble; M L Nibert
Journal:  J Virol       Date:  1997-03       Impact factor: 5.103

3.  Structure of L-A virus: a specialized compartment for the transcription and replication of double-stranded RNA.

Authors:  J R Castón; B L Trus; F P Booy; R B Wickner; J S Wall; A C Steven
Journal:  J Cell Biol       Date:  1997-09-08       Impact factor: 10.539

  3 in total

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