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. 2011 Jan 28;39(10):4360–4372. doi: 10.1093/nar/gkr021

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© The Author(s) 2011. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 2. — Analysis of the SacT P26S mutant. The isolated SacT P26S variant was tested against all RAT structures in B. subtilis. The wild-type RNA-binding domains of SacT, LicT and GlcT were used as controls. The β-galactosidase activity is shown in percentage of the wild type activity. In the case of bglP^R RAT SacT was set 100% because in this artificial system SacT has a higher activity towards this RAT structure. 1: SacT 2: LicT 3: GlcT 4: SacT P26S.