Changes of lysine reactivities of actin in complex with DNAase I.
The reactivities of lysines of actin in the actin-DNAase I complex were measured by the method of reductive methylation. The reactivities of lysines in the amino-terminal part, lysines 18, 50, 61 and 68, decreased 50%, while those of lysines 237, 283 and 290 increased about 30%, in comparison with those in G-actin, when actin was bound to DNAase I. These results are consistent with the view that the amino-terminal region of actin is the binding site for DNAase I. In conjunction with our earlier work on the reactivities of lysines in F-actin (Lu, R.C. and Szilagyi, L. (1981) Biochemistry 20, 5914-5919), these results are also consistent with the view that DNAase I binds to actin at one of the regions that is involved in polymerization.
D000199:Actins / Q000378:metabolism*; D003850:Deoxyribonuclease I / Q000037:antagonists & inhibitors / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D008239:Lysine / Q000378:metabolism*; D008745:Methylation; D010084:Oxidation-Reduction; D011485:Protein Binding
D000199:Actins; D003850:Deoxyribonuclease I; D008239:Lysine