ArticleBiophysical journal2000
Actin and temperature effects on the cross-linking of the SH1-SH2 helix in myosin subfragment 1.
Article in Biophysical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 11 citations in OpenAlex.
- Electrostatic interactions in the force-generating region of the human cardiac myosin modulate ADP dissociation from actomyosin.Biochemical and biophysical research communications · 2019Article
- Effect of temperature on tether extraction, surface protrusion, and cortical tension of human neutrophils.Biophysical journal · 2007Article
- Engineering lysine reactivity as a conformational sensor in the Dictyostelium myosin II motor domain.Journal of muscle research and cell motility · 2004Article
- Conformational dynamics of the SH1-SH2 helix in the transition states of myosin subfragment-1.Biophysical journal · 2002Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Past biochemical work on myosin subfragment 1 (S1) has shown that the bent alpha-helix containing the reactive thiols SH1 (Cys(707)) and SH2 (Cys(697)) changes upon nucleotide and actin binding. In this study, we investigated the conformational dynamics of the SH1-SH2 helix in two actin-bound states of myosin and examined the effect of temperature on this helix, using five cross-linking reagents that are 5-15 A in length. Actin inhibited the cross-linking of SH1 to SH2 on both S1 and S1.MgADP for all of the reagents. Because the rate of SH2 modification was not altered by actin, the inhibition of cross-linking must result from a strong stabilization of the SH1-SH2 helix in the actin-bound states of S1. The dynamics of the helix is also influenced by temperature. At 25 degrees C, the rate constants for cross-linking in S1 alone are low, with values of approximately 0.010 min(-1) for all of the reagents. At 4 degrees C, the rate constants, except for the shortest reagent, range between 0.030 and 0.070 min(-1). The rate constants for SH2 modification in SH1-modified S1 show the opposite trend; they increase with the increases in temperature. The greater cross-linking at the lower temperature indicates destabilization of the SH1-SH2 helix at 4 degrees C. These results are discussed in terms of conformational dynamics of the SH1-SH2 helix.
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