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. Author manuscript; available in PMC: 2011 Nov 1.
Published in final edited form as: Mol Microbiol. 2010 Sep 24;78(4):916–931. doi: 10.1111/j.1365-2958.2010.07378.x

Figure 2.

Figure 2

Amino acid substitutions F36S and R41P specifically interfere with the ability of MvaT to form higher-order oligomers. (A) Effect of λCINTD, λCINTD-MvaT, λCINTD-MvaT (F36S) or λCINTD-MvaT (R41P) proteins on transcription in vivo from PRM in the presence of α-MvaT. BN30 cells containing compatible plasmids directing the synthesis of the indicated proteins were grown and assayed for β-galactosidase activity. (B) Transcription repression by the λCINTD-MvaT, λCINTD-MvaT (F36S), and λCINTD-MvaT (R41P) fusion proteins. FW123 cells harboring plasmids directing the IPTG-dependent synthesis of the indicated proteins were grown in the presence of 20 µM IPTG and assayed for β-galactosidase activity.