Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 412, Issue 4, Pages 710-722Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2011.07.036
Keywords
bacteriophage; mobilization; virus assembly; NMR spectroscopy; cryo-electron microscopy
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Funding
- National Institutes of Health [R21 AI071982, R01 AI083255, R21 AI067654, R56 AI081837]
- A. D. Williams Trust
- Baruch Foundation Trust
- Ruth L. Kirschstein National Research Service award [F32 GM087994]
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Staphylococcus aureus pathogenicity island 1 (SaPI1) is a mobile genetic element that carries genes for several superantigen toxins. SaPI1 is normally stably integrated into the host genome but can become mobilized by helper bacteriophage 80 alpha, leading to the packaging of SaPI1 genomes into phage-like transducing particles that are composed of structural proteins supplied by the helper phage but having smaller capsids. We show that the SaPI1-encoded protein gp6 is necessary for efficient formation of small capsids. The NMR structure of gp6 reveals a dimeric protein with a helix loop helix motif similar to that of bacteriophage scaffolding proteins. The gp6 dimer matches internal densities that bridge capsid subunits in cryoelectron microscopy reconstructions of SaPI1 procapsids, suggesting that gp6 acts as an internal scaffolding protein in capsid size determination. (C) 2011 Elsevier Ltd. All rights reserved.
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