Relationship between the flexibility and the motility of actin filaments: effects of pH
- PMID: 18457659
- DOI: 10.1016/j.bbrc.2008.04.135
Relationship between the flexibility and the motility of actin filaments: effects of pH
Abstract
Both the sliding velocity of fluorescently labeled actin filament and its persistence length as an index of the bending flexibility of the filament were examined in the motility assay as varying the pH values of the solution for preparing actin filaments. When the pH value was varied from 5.0 to 9.0 in the solution in which actin filaments were formed from the constituent monomers, the motile performance of Mg(2+) bound actin filaments (Mg-F-actin) was apparently suppressed compared to the case of Ca(2+) bound ones (Ca-F-actin). The persistence length for Ca-F-actin gradually increased with the increase of the pH value while the similar length for Mg-F-actin remained rather independent of the value. The largest sliding velocity of the filament, on the other hand, obtained at the persistence length of roughly 6 microm for both cases of Mg-F-actin and Ca-F-actin.
Similar articles
-
Influence of tightly bound Mg2+ and Ca2+, nucleotides, and phalloidin on the microsecond torsional flexibility of F-actin.Biochemistry. 1998 Oct 13;37(41):14529-38. doi: 10.1021/bi981240i. Biochemistry. 1998. PMID: 9772181
-
Polymerization, three-dimensional structure and mechanical properties of Ddictyostelium versus rabbit muscle actin filaments.J Mol Biol. 2000 Oct 20;303(2):171-84. doi: 10.1006/jmbi.2000.4129. J Mol Biol. 2000. PMID: 11023784
-
Troponin is a potential regulator for actomyosin interactions.J Biochem. 2006 Feb;139(2):289-93. doi: 10.1093/jb/mvj030. J Biochem. 2006. PMID: 16452317
-
Thermal unfolding and aggregation of actin.FEBS J. 2008 Sep;275(17):4280-95. doi: 10.1111/j.1742-4658.2008.06569.x. Epub 2008 Jul 14. FEBS J. 2008. PMID: 18637820 Review.
-
Physical chemistry of actin: past, present and future.Biophys Chem. 1993 Aug;47(2):101-11. doi: 10.1016/0301-4622(93)85028-g. Biophys Chem. 1993. PMID: 8400016 Review.
Cited by
-
Depletion plays a pivotal role in self-incompatibility, revealing a link between cellular energy status, cytosolic acidification and actin remodelling in pollen tubes.New Phytol. 2022 Dec;236(5):1691-1707. doi: 10.1111/nph.18350. Epub 2022 Jul 23. New Phytol. 2022. PMID: 35775998 Free PMC article.
-
Hydrodynamic and Polyelectrolyte Properties of Actin Filaments: Theory and Experiments.Polymers (Basel). 2022 Jun 16;14(12):2438. doi: 10.3390/polym14122438. Polymers (Basel). 2022. PMID: 35746014 Free PMC article.
-
Controlling the Rigidity of Kinesin-Propelled Microtubules in an In Vitro Gliding Assay Using the Deep-Sea Osmolyte Trimethylamine N-Oxide.ACS Omega. 2022 Jan 24;7(4):3796-3803. doi: 10.1021/acsomega.1c06699. eCollection 2022 Feb 1. ACS Omega. 2022. PMID: 35128287 Free PMC article.
-
Generation of stable microtubule superstructures by binding of peptide-fused tetrameric proteins to inside and outside.Sci Adv. 2022 Sep 9;8(36):eabq3817. doi: 10.1126/sciadv.abq3817. Epub 2022 Sep 7. Sci Adv. 2022. PMID: 36070375 Free PMC article.
-
Analysis of flexural rigidity of actin filaments propelled by surface adsorbed myosin motors.Cytoskeleton (Hoboken). 2013 Nov;70(11):718-28. doi: 10.1002/cm.21138. Epub 2013 Oct 4. Cytoskeleton (Hoboken). 2013. PMID: 24039103 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Miscellaneous