Structure and dynamics of the actin filament

Jing Qu Guan, Keiji Takamoto, Steven C. Almo, Emil Reisler, Mark R. Chance

Research output: Contribution to journalArticle

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Abstract

The structures of filamentous Mg-ATP-actin (F actin) in the presence and absence of KCl have been mapped with hydroxyl radicals (asterisk inside a circle signOH) generated by synchrotron X-ray radiolysis. Proteolysis and mass spectrometry (MS) analysis revealed 52 reactive side-chain sites from 27 distinct peptides within actin. The reactivities of these probe sites with asterisk inside a circle signOH in the F-actin states are compared with those of Mg-ATP-G-actin (monomers) analyzed previously [Guan, J.-Q. et al. (2003) Biochemistry 42, 11992-12000]. Filament-dependent protection within subdomains 2, 3, and 4 and at the C terminus is consistent with longitudinal contacts of monomers within the filament helical structure as predicted by the Holmes model. In the absence of KCl, the extent of filament-dependent protection rarely reached 3-fold, consistent with a highly dynamic filament characterized by relatively weak interactions between actin protomers. However, in the presence of KCl, the extents of protection are significantly increased, consistent with a well-ordered, more tightly packed filament structure. Filament-dependent enhancements of reactivity not predicted by the Holmes model are seen for a peptide that overlaps the "hydrophobic plug" (H-plug) region and for a peptide that forms contacts with the polyphosphate moiety of the bound nucleotide. Overall, these data are both consistent with and complementary to a recent deuterium-exchange MS study of filamentous actin [Chik, J. K., and Schriemer, D.C. (2003) J. Mol. Biol. 334, 373-385], which also did not detect any burial of the H plug upon formation of filaments.

Original languageEnglish (US)
Pages (from-to)3166-3175
Number of pages10
JournalBiochemistry
Volume44
Issue number9
DOIs
StatePublished - Mar 8 2005

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Actin Cytoskeleton
Actins
Peptides
Mass spectrometry
Mass Spectrometry
Monomers
Proteolysis
Burial
Polyphosphates
Radiolysis
Biochemistry
Synchrotrons
Deuterium
Protein Subunits
Hydroxyl Radical
Nucleotides
X-Rays
X rays
ATP-G-actin

ASJC Scopus subject areas

  • Biochemistry

Cite this

Guan, J. Q., Takamoto, K., Almo, S. C., Reisler, E., & Chance, M. R. (2005). Structure and dynamics of the actin filament. Biochemistry, 44(9), 3166-3175. https://doi.org/10.1021/bi048021j

Structure and dynamics of the actin filament. / Guan, Jing Qu; Takamoto, Keiji; Almo, Steven C.; Reisler, Emil; Chance, Mark R.

In: Biochemistry, Vol. 44, No. 9, 08.03.2005, p. 3166-3175.

Research output: Contribution to journalArticle

Guan, JQ, Takamoto, K, Almo, SC, Reisler, E & Chance, MR 2005, 'Structure and dynamics of the actin filament', Biochemistry, vol. 44, no. 9, pp. 3166-3175. https://doi.org/10.1021/bi048021j
Guan JQ, Takamoto K, Almo SC, Reisler E, Chance MR. Structure and dynamics of the actin filament. Biochemistry. 2005 Mar 8;44(9):3166-3175. https://doi.org/10.1021/bi048021j
Guan, Jing Qu ; Takamoto, Keiji ; Almo, Steven C. ; Reisler, Emil ; Chance, Mark R. / Structure and dynamics of the actin filament. In: Biochemistry. 2005 ; Vol. 44, No. 9. pp. 3166-3175.
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