期刊
PLOS BIOLOGY
卷 5, 期 3, 页码 558-567出版社
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pbio.0050059
关键词
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资金
- NIDCR NIH HHS [R01 DE003606, DE-03606] Funding Source: Medline
- NIGMS NIH HHS [R01 GM071552, GM-071552] Funding Source: Medline
The bacteriophage phi 29 generates large forces to compact its double-stranded DNA genome into a protein capsid by means of a portal motor complex. Several mechanical models for the generation of these high forces by the motor complex predict coupling of DNA translocation to rotation of the head-tail connector dodecamer. Putative connector rotation is investigated here by combining the methods of single-molecule force spectroscopy with polarizationsensitive single-molecule fluorescence. In our experiment, we observe motor function in several packaging complexes in parallel using video microscopy of bead position in a magnetic trap. At the same time, we follow the orientation of single fluorophores attached to the portal motor connector. From our data, we can exclude connector rotation with greater than 99% probability and therefore answer a long-standing mechanistic question.
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