Abstract
It has been reported that tobacco mosaic virus capsid protein encapsidates discretesized truncated portions of host 18 S rRNA in vitro. This paper presents further information concerning the nature and specificity of this reaction. We have found that it is only the 5′ portions of 18 S rRNA that are encapsidated. The structure recognized by capsid protein is highly conserved; bovine as well as plant 18 S rRNA becomes encapsidated. It is further demonstrated that assembly of 18 S rRNA is slow in comparison to assembly of TMV RNA and that this is due to a slow rate of initiation. Synthetic 18 S rRNA, prepared by in vitro transcription of an 18 S rRNA coding sequence, differs from native 18 S rRNA in that full length, rather than a truncated portion, is encapsidated. The possible reasons for this are discussed.
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