Structure of a Pentavalent G-Actin•MRTF-A Complex Reveals How G-Actin Controls Nucleocytoplasmic Shuttling of a Transcriptional Coactivator

Stéphane Mouilleron, Carola A. Langer, Sebastian Guettler, Neil Q. McDonald,* Richard Treisman*

*To whom correspondence should be addressed. E-mail: Neil.McDonald{at}cancer.org.uk (N.Q.M.); Richard.Treisman{at}cancer.org.uk (R.T.)

This PDF file includes:

• Fig. S1. CD spectrum for MRTF-A RPEL domain.
• Fig. S2. Arrangement of actin molecules and structural subdomains in the pentavalent actin•RPEL assembly compared with those in the actin filament.
• Fig. S3. Individual RPEL motifs and their extensions engage one or two actins within the pentameric complex.
• Fig. S4. Comparison of pentavalent and trivalent actin•RPEL domain complexes.
• Fig. S5. Actin S2 exhibits higher temperature factors than other actins in the pentavalent actin•RPEL domain assembly.
• Fig. S6. TLS refinement shows higher mobility of actin S2 in the crystal lattice.
• Fig. S7. Comparison of the interactions of RPELs and spacers close to the C terminus of actin in the pentameric actin•RPEL domain assembly.
• Fig. S8. Size exclusion chromatography of G-actin•RPEL peptide and actin•RPEL domain complexes.
• Fig. S9. Nuclear import properties of spacer mutants.
• Fig. S10. Relationships of the actin•RPEL assemblies to import and export.
• References
• Legends for movies S1 and S2
  

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Other Supplementary Material for this manuscript includes the following:

• Movie S1. The pentavalent actin•RPEL domain assembly.
• Movie S2. RPEL-actins R1, R2, and R3 align around the crank axis, in intimate contact with the RPEL domain.

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© 2011 American Association for the Advancement of Science