Abstract
The structure and function of tobacco mosaic virus (TMV) protein modified by N-bromosuccinimide (NBS-protein) was found to differ from native TMV-protein, NBS-protein differed only by the replacement of a single tyrosine by dibromotyrosine at position 139. Under optimum conditions for the in vitro assembly of TMV from its RNA and protein, NBS-protein did not reconstitute with TMV-RNA. However, partially reconstituted RNA (PRR) prepared from TMV-RNA and a small amount of native TMV-protein was able to form an infectious TMV particle by further addition of NBS-protein. Under conditions favorable for the reconstitution of TMV, NBS-protein did not form a 20 S aggregate. These results confirm our model for the process of assembly of TMV in which we propose that the 20 S aggregate is an essential component for initiation of the reconstitution reaction and that rod elongation proceeds by the stepwise addition of protein subunits, not by the addition of 20 S aggregates.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
