Interaction of packaging motor with the polymerase complex of dsRNA bacteriophage
- Institute of Biotechnology and Department of Biological and Environmental Sciences, University of Helsinki, Viikinkaari 1 PL 65, 00014 Helsinki (Finland)
- National High Magnetic Field Laboratory and Department of Chemistry and Biochemistry, 1800 E. Paul Dirac Dr., Florida State University, Tallahassee, FL 32310 (United States)
- Department of Microbiology and Immunology, Sophie Davis School of Biomedical Education, City College of New York, New York, NY 10031 (United States)
Many viruses employ molecular motors to package their genomes into preformed empty capsids (procapsids). In dsRNA bacteriophages the packaging motor is a hexameric ATPase P4, which is an integral part of the multisubunit procapsid. Structural and biochemical studies revealed a plausible RNA-translocation mechanism for the isolated hexamer. However, little is known about the structure and regulation of the hexamer within the procapsid. Here we use hydrogen-deuterium exchange and mass spectrometry to delineate the interactions of the P4 hexamer with the bacteriophage phi12 procapsid. P4 associates with the procapsid via its C-terminal face. The interactions also stabilize subunit interfaces within the hexamer. The conformation of the virus-bound hexamer is more stable than the hexamer in solution, which is prone to spontaneous ring openings. We propose that the stabilization within the viral capsid increases the packaging processivity and confers selectivity during RNA loading.
- OSTI ID:
- 20850533
- Journal Information:
- Virology, Vol. 351, Issue 1; Other Information: DOI: 10.1016/j.virol.2006.03.025; PII: S0042-6822(06)00178-4; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0042-6822
- Country of Publication:
- United States
- Language:
- English
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