PMID: 11904226Mar 21, 2002Paper

Changes at the interface of the N- and C-terminal parts of the heavy chain of myosin subfragment 1

Biochimica Et Biophysica Acta
B Pliszka, Emilia Karczewska

Abstract

It has been previously shown that in the M-MgADP-P(i) state, where the myosin head adopts a pre-power stroke conformation, treatment of trypsin-split subfragment 1 of skeletal muscle myosin with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) results in cross-linking of the C-terminal fragment of the heavy chain of S1 -- most probably its converter region -- to the N-terminal S1 heavy-chain fragment, generating a product of 44 kDa [Biochim. Biophys. Acta 1481 (2000) 55]. The results described here show that this product is neither generated in the absence of nucleotide nor in the presence of MgADP or MgPP(i). The 44 kDa cross-linking product can be formed when S1 treated with EDC is complexed with MgADP-AlF(4) or MgADP-V(i) (MgADP-P(i) analogs) and with MgADP-BeF(x), MgATP gamma S or MgAMPPNP (MgATP analogs). The results suggest structural differences between MgATP- or MgADP-P(i)-bound S1, and MgADP-bound or nucleotide-free S1, in spatially close regions of their N- and C-terminal heavy-chain fragments.

References

Jun 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·C C Goodno
Feb 29, 2000·Biophysical Journal·K PolosukhinaS Highsmith
Jun 3, 2000·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·K C Holmes, M A Geeves
Aug 24, 2000·The Journal of Biological Chemistry·C B BauerI Rayment
Aug 30, 2000·Biochimica Et Biophysica Acta·B PliszkaB Wawro
Oct 4, 2000·Proceedings of the National Academy of Sciences of the United States of America·A HoudusseC Cohen

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