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. 1998 Sep 29;95(20):11637–11642. doi: 10.1073/pnas.95.20.11637

Figure 3.

Figure 3

In vitro cleavage of RNAI (A) and 9S RNA (B) by the E. coli and Synechocystis sp. Rne proteins. Internally labeled RNAI or 9S RNA was incubated in RNase E reaction buffer for 3 and 30 min with either E. coli RNase E (EcoRne) or Synechocystis sp. Rne (SynRne), or without protein for 30 min (C), as a negative control. The positions of the original substrates (RNAI and 9S RNA) and their cleavage products (RNA I-5 and 5S rRNA (5S), respectively) are indicated. (C) Protein blots probed with RNAI and 9S RNA. Samples of the Synechocystis sp. Rne protein (Syn) and the E. coli RNA degradosome (Eco) were resolved by SDS/PAGE, electroblotted onto poly(vinylidene difluoride) membrane, and probed with 32P-labeled RNAI or 9S RNA as described in Materials and Methods. The Synechocystis sp. Rne (SynRne) and E. coli Rne (EcoRne) proteins complexed with RNA are indicated.