An Unstable Head-Rod Junction May Promote Folding into the Compact Off-State Conformation of Regulated Myosins

Jerry H. Brown, Yuting Yang, Ludmilla Reshetnikova, S. Gourinath, Dániel Süveges, J. Kardos, Fruzsina Hóbor, Robbie Reutzel, L. Nyitray, Carolyn Cohen

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

The N-terminal region of myosin's rod-like subfragment 2 (S2) joins the two heads of this dimeric molecule and is key to its function. Previously, a crystal structure of this predominantly coiled-coil region was determined for a short fragment (51 residues plus a leucine zipper) of the scallop striated muscle myosin isoform. In that study, the N-terminal 10-14 residues were found to be disordered. We have now determined the structure of the same scallop peptide in three additional crystal environments. In each of two of these structures, improved order has allowed visualization of the entire N-terminus in one chain of the dimeric peptide. We have also compared the melting temperatures of this scallop S2 peptide with those of analogous peptides from three other isoforms. Taken together, these experiments, along with examination of sequences, point to a diminished stability of the N-terminal region of S2 in regulated myosins, compared with those myosins whose regulation is thin filament linked. It seems plain that this isoform-specific instability promotes the off-state conformation of the heads in regulated myosins. We also discuss how myosin isoforms with varied thermal stabilities share the basic capacity to transmit force efficiently in order to produce contraction in their on states.

Original languageEnglish
Pages (from-to)1434-1443
Number of pages10
JournalJournal of Molecular Biology
Volume375
Issue number5
DOIs
Publication statusPublished - Feb 1 2008

Fingerprint

Myosins
Pectinidae
Head
Protein Isoforms
Peptides
Myosin Subfragments
Leucine Zippers
Striated Muscle
Freezing
Hot Temperature
Temperature

Keywords

  • α-helical coiled coil
  • myosin subfragment 2
  • off state
  • thermal stability
  • X-ray diffraction

ASJC Scopus subject areas

  • Virology

Cite this

An Unstable Head-Rod Junction May Promote Folding into the Compact Off-State Conformation of Regulated Myosins. / Brown, Jerry H.; Yang, Yuting; Reshetnikova, Ludmilla; Gourinath, S.; Süveges, Dániel; Kardos, J.; Hóbor, Fruzsina; Reutzel, Robbie; Nyitray, L.; Cohen, Carolyn.

In: Journal of Molecular Biology, Vol. 375, No. 5, 01.02.2008, p. 1434-1443.

Research output: Contribution to journalArticle

Brown, JH, Yang, Y, Reshetnikova, L, Gourinath, S, Süveges, D, Kardos, J, Hóbor, F, Reutzel, R, Nyitray, L & Cohen, C 2008, 'An Unstable Head-Rod Junction May Promote Folding into the Compact Off-State Conformation of Regulated Myosins', Journal of Molecular Biology, vol. 375, no. 5, pp. 1434-1443. https://doi.org/10.1016/j.jmb.2007.11.071
Brown, Jerry H. ; Yang, Yuting ; Reshetnikova, Ludmilla ; Gourinath, S. ; Süveges, Dániel ; Kardos, J. ; Hóbor, Fruzsina ; Reutzel, Robbie ; Nyitray, L. ; Cohen, Carolyn. / An Unstable Head-Rod Junction May Promote Folding into the Compact Off-State Conformation of Regulated Myosins. In: Journal of Molecular Biology. 2008 ; Vol. 375, No. 5. pp. 1434-1443.
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