The positively charged region of the myosin IIC non-helical tailpiece promotes filament assembly

Daniel Ronen, Masha M. Rosenberg, Deborah E. Shalev, Michael Rosenberg, Shahar Rotem, Assaf Friedler, Shoshana Ravid

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

The motor protein, non-muscle myosin II (NMII), must undergo dynamic oligomerization into filaments to participate in cellular processes such as cell migration and cytokinesis. A small non-helical region at the tail of the long coiled-coil region (tailpiece) is a common feature of all dynamically assembling myosin II proteins. In this study, we investigated the role of the tailpiece in NMII-C self-assembly. We show that the tailpiece is natively unfolded, as seen by circular dichroism and NMR experiments, and is divided into two regions of opposite charge. The positively charged region (Tailpiece1946-1967) starts at residue 1946 and is extended by seven amino acids at its N terminus from the traditional coiled-coil ending proline (Tailpiece1953-1967). Pull-down and sedimentation assays showed that the positive Tailpiece 1946-1967 binds to assembly incompetent NMII-C fragments inducing filament assembly. The negative region, residues 1968-2000, is responsible for NMII paracrystal morphology as determined by chimeras in which the negative region was swapped between the NMII isoforms. Mixing the positive and negative peptides had no effect on the ability of the positive peptide to bind and induce filament assembly. This study provides molecular insight into the role of the structurally disordered tailpiece of NMII-C in shifting the oligomeric equilibrium of NMII-C toward filament assembly and determining its morphology.

Original languageEnglish
Pages (from-to)7079-7086
Number of pages8
JournalJournal of Biological Chemistry
Volume285
Issue number10
DOIs
StatePublished - 5 Mar 2010
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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