VapC6, a ribonucleolytic toxin regulates thermophilicity in the crenarchaeote Sulfolobus solfataricus

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FIGURE 5.
FIGURE 5.

In vivo solubilization of VapC63′His and VapB63′His. SDS-PAGE analysis of E. coli crude extracts (lanes 2,4,6) or Ni-NTA column eluants (lanes 1,3,5). Extracts were prepared from strains containing plasmids expressing vapC63′His (lanes 1,2), both vapC63′His and dnaK (lanes 3,4), and vapB63′His (lanes 5,6). Protein identities that were determined by tandem mass spectrometry are indicated (arrowheads).

This Article

  1. Published in Advance May 27, 2011, doi: 10.1261/rna.2679911 RNA 17: 1381-1392

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