ArticleJournal of muscle research and cell motility2007
Nucleotide-induced and actin-induced structural changes in SH1-SH2-modified myosin subfragment 1.
Article in Journal of muscle research and cell motility, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- Article
- Thermal denaturation and aggregation of myosin subfragment 1 isoforms with different essential light chains.International journal of molecular sciences · 2010Article
- Effects of Myosin "essential" light chain A1 on the aggregation properties of the Myosin head.Acta naturae · 2010Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We compared the structural properties of myosin subfragment 1 (S1) modified at both reactive SH-groups, SH1 (Cys707) and SH2 (Cys697), with the properties of unmodified S1 and SH1-modified S1. It is shown using differential scanning calorimetry (DSC) that SH1 modification has no noticeable influence on the changes in S1 thermal unfolding induced by the formation of S1 ternary complexes with ADP and P(i) analogs (V(i), AlF(4)(-), and BeF(x)). These changes, however, normally expressed in a significant increase of S1 thermal stability, are almost fully prevented by modification of both SH1 and SH2. In contrast, SH2 modification had no effect on the changes induced by the formation of the ternary complexes S1-ADP-V(i), S1-ADP-AlF(4)(-), and S1-ADP-BeF(x) in EPR spectra of S1 spin-labeled at SH1 group. Interaction of S1 with F-actin substantially increased the thermal stability of S1; a similar effect was observed by DSC with both SH1- and SH1-SH2-modified S1. Overall, our results demonstrate that modification of both reactive SH-groups on S1 has no influence on the actin-induced changes of S1 and on the local nucleotide-induced conformational changes in the SH1 group region, but strongly prevents the global nucleotide-induced structural changes in the entire S1 molecule. The results suggest that modification of SH1 and SH2 impairs the spread of nucleotide-induced conformational changes from the ATPase site throughout the structure of the entire S1 molecule, thus disturbing a coupling between the motor and regulatory domains in the myosin head.
Indexed as
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Registered trials
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