ArticleBiophysical journal1999
Divalent cation-, nucleotide-, and polymerization-dependent changes in the conformation of subdomain 2 of actin.
Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 47 citations in OpenAlex.
- Myopathy-Sensitive G-Actin Segment 227-235 Is Involved in Salt-Induced Stabilization of Contacts within the Actin Filament.International journal of molecular sciences · 2021Article
- Nucleotide-dependent conformational changes in the actin filament: Subtler than expected.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Mechanism of actin polymerization revealed by cryo-EM structures of actin filaments with three different bound nucleotides.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Binding of Red Clover Isoflavones to Actin as A Potential Mechanism of Anti-Metastatic Activity Restricting the Migration of Cancer Cells.Molecules (Basel, Switzerland) · 2018Article
- Mechanisms of nuclear actin in chromatin-remodeling complexes.Trends in cell biology · 2014Review
- Structural states and dynamics of the D-loop in actin.Biophysical journal · 2012Article
- Flavonoids affect actin functions in cytoplasm and nucleus.Biophysical journal · 2007Article
- Role of actin DNase-I-binding loop in myosin subfragment 1-induced polymerization of G-actin: implications for the mechanism of polymerization.Biophysical journal · 2005Article
- The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Actin-ATP hydrolysis is a major energy drain for neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003Article
- Role of the DNase-I-binding loop in dynamic properties of actin filament.Biophysical journal · 2002Article
- Thermodynamics and kinetics of actin filament nucleation.Biophysical journal · 2001Article
- Distinct structural changes detected by X-ray fiber diffraction in stabilization of F-actin by lowering pH and increasing ionic strength.Biophysical journal · 2001Article
- The oxidation produced by hydrogen peroxide on Ca-ATP-G-actin.Protein science : a publication of the Protein Society · 2000Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Conformational changes in subdomain 2 of actin were investigated using fluorescence probes dansyl cadaverine (DC) or dansyl ethylenediamine (DED) covalently attached to Gln41. Examination of changes in the fluorescence emission spectra as a function of time during Ca2+/Mg2+ and ATP/ADP exchange at the high-affinity site for divalent cation-nucleotide complex in G-actin confirmed a profound influence of the type of nucleotide but failed to detect a significant cation-dependent difference in the environment of Gln41. No significant difference between Ca- and Mg-actin was also seen in the magnitude of the fluorescence changes resulting from the polymerization of these two actin forms. Evidence is presented that earlier reported cation-dependent differences in the conformation of the loop 38-52 may be related to time-dependent changes in the conformation of subdomain 2 in DED- or DC-labeled G-actin, accelerated by substitution of Mg2+ for Ca2+ in CaATP-G-actin and, in particular, by conversion of MgATP- into MgADP-G-actin. These spontaneous changes are associated with a denaturation-driven release of the bound nucleotide that is promoted by two effects of DED or DC labeling: lowered affinity of actin for nucleotide and acceleration of ATP hydrolysis on MgATP-G-actin that converts it into a less stable MgADP form. Evidence is presented that the changes in the environment of Gln41 accompanying actin polymerization result in part from the release of Pi after the hydrolysis of ATP on the polymer. A similarity of this change to that accompanying replacement of the bound ATP with ADP in G-actin is discussed.
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