Structures of Helical Plant Virus Ribonucleoproteins as Assessed by Tritium Planigraphy and Theoretical Modeling.

Autor:	Dobrov, E. N., Efimov, A. V., Baratova, L. A.
Předmět:	NUCLEOPROTEINS PLANT viruses TRITIUM MACROMOLECULES RNA-protein interactions MOLECULAR biology
Zdroj:	Molecular Biology; Sep/Oct2004, Vol. 38 Issue 5, p806-817, 12p
Abstrakt:	This review considers the results of probing the structure of ribonucleoprotein particles of helical plant viruses by tritium planigraphy (TP). This method works by exposing macromolecular targets to a beam of tritium atoms and analyzing the tritium label distribution along the macromolecule length. The TP data combined with theoretical predictions made it possible to propose a structural model of the coat protein for the virions of potato viruses X (the type representative of potexviruses) and A (a potyvirus), which eluded X-ray diffraction analysis so far. TP revealed fine structural differences between the wild-type tobacco mosaic virus (strain U1) and its temperature-sensitive mutant with an altered coat protein and host specificity. The possibilities of using TP for studying the RNA–protein interactions in helical virus particles are discussed. [ABSTRACT FROM AUTHOR]
Databáze:	Complementary Index
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