ArticleBiophysical journal2003
Solution properties of tetramethylrhodamine-modified G-actin.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Partitioning and Enhanced Self-Assembly of Actin in Polypeptide Coacervates.Biophysical journal · 2018Article
- ATP and ADP actin states.Biopolymers · 2013Article
- Glutamyl phosphate is an activated intermediate in actin crosslinking by actin crosslinking domain (ACD) toxin.PloS one · 2012Article
- Subdomain location of mutations in cardiac actin correlate with type of functional change.PloS one · 2012Article
- A nucleotide state-sensing region on actin.The Journal of biological chemistry · 2010Article
- Functional effects of nemaline myopathy mutations on human skeletal alpha-actin.The Journal of biological chemistry · 2008Article
- Characterization of the enzymatic activity of the actin cross-linking domain from the Vibrio cholerae MARTX Vc toxin.The Journal of biological chemistry · 2008Article
- Nucleotide effects on the structure and dynamics of actin.Biophysical journal · 2007Article
- The Actin cross-linking domain of the Vibrio cholerae RTX toxin directly catalyzes the covalent cross-linking of actin.The Journal of biological chemistry · 2006Article
- The open nucleotide pocket of the profilin/actin x-ray structure is unstable and closes in the absence of profilin.Biophysical journal · 2006Article
- Actin-destabilizing factors disrupt filaments by means of a time reversal of polymerization.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Formation and destabilization of actin filaments with tetramethylrhodamine-modified actin.Biophysical journal · 2004Article
- Solution properties of TMR-actin: when biochemical and crystal data agree.Biophysical journal · 2003Article
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Authors and funding
2 authors.
Funding
Abstract
In the recently solved structure of TMR-modified ADP-G-actin, the nucleotide cleft is in a closed state conformation, and the D-loop contains an alpha-helix (L. R. Otterbein, P. Graceffa, and R. Dominguez, 2001, Science, 293:708-711). Subsequently, questions were raised regarding the possible role of the TMR label on Cys(374) in determining these aspects of G-actin structure. We show here that the susceptibility of D-loop on G-actin to subtilisin cleavage, and ATP/ADP-dependent changes in this cleavage, are not affected by TMR-labeling of actin. The TMR modification inhibits nucleotide exchange, but has no effect on DNase I binding and the fast phase of tryptic digestion of actin. These results show an absence of allosteric effects of TMR on subdomain 2, while confirming ATP/ADP-dependent changes in D-loop structure. In conjunction with similar results obtained on actin-gelsolin segment 1 complex, this works reveals the limitations of solution methods in probing the putative open and closed nucleotide cleft states of G-actin.
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