Effect of Ca2+ binding to 5,5'-dithiobis(2-nitrobenzoic acid) light chains on conformational changes of F-actin caused by myosin subfragment-1.
The fluorescent ADP analogue, 1:N6-ethenoadenosine 5'-diphosphate, was incorporated into F-actin in a myosin-free ghost single fibre. Polarized fluorescence measurements of tryptophan residues and 1:N6-ethenoadenosine 5'-diphosphate were performed under a microspectrophotometer to investigate the conformation of F-actin and the changes induced in it by myosin subfragment-1 with 5,5'-dithiobis(2-nitrobenzoic acid) light chains and without them. A relation was found between the conformational state of F-actin and the presence of 5,5'-dithiobis(2-nitrobenzoic acid) light chains. The conformational changes were shown to be controlled by Ca2+ in the presence of 5,5'-dithiobis(2-nitrobenzoic acid) light chains.
D000199:Actins / Q000378:metabolism*; D000244:Adenosine Diphosphate / Q000031:analogs & derivatives; D000818:Animals; D002118:Calcium / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D004228:Dithionitrobenzoic Acid / Q000378:metabolism*; D009218:Myosins / Q000032:analysis*; D009579:Nitrobenzoates / Q000378:metabolism*; D010446:Peptide Fragments; D011485:Protein Binding; D011487:Protein Conformation; D011817:Rabbits; D013050:Spectrometry, Fluorescence
D000199:Actins; D009579:Nitrobenzoates; D010446:Peptide Fragments; C015195:1,N(6)-ethenoadenosine diphosphate; D000244:Adenosine Diphosphate; D004228:Dithionitrobenzoic Acid; D009218:Myosins; D002118:Calcium