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Science 14 July 1989:
Vol. 245. no. 4914, pp. 154 - 159
DOI: 10.1126/science.2749253
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Articles

Science, Vol 245, Issue 4914, 154-159
Copyright © 1989 by American Association for the Advancement of Science

articles

Protein-RNA interactions in an icosahedral virus at 3.0 A resolution

ZG Chen, C Stauffacher, Y Li, T Schmidt, W Bomu, G Kamer, M Shanks, G Lomonossoff, and JE Johnson

Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907.

Nearly 20 percent of the packaged RNA in bean-pod mottle virus (BPMV) binds to the capsid interior in a symmetric fashion and is clearly visible in the electron density map. The RNA displaying icosahedral symmetry is single-stranded with well-defined polarity and stereochemical properties. Interactions with protein are dominated by nonbonding forces with few specific contacts. The tertiary and quaternary structures of the BPMV capsid proteins are similar to those observed in animal picornaviruses, supporting the close relation between plant comoviruses and animal picornaviruses established by previous biological studies.


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