title: Changes in actin lysine reactivities during polymerization detected using a competitive labeling method.
abstract: We have studied the structure of actin by measuring the relative reactivities of lysines with acetic anhydride using a competitive labeling procedure comparing monomeric globular actin. monomeric actin in the presence of salt, and filamentous actin polymerized in 100 mM NaCl and 100 mM NaCl, 2 mM MgCl2. We have identified 12 of the 19 lysines: 18, 50, 61, 68, 113, 191, 237, 290, 315, 325, 327, and 358. In all conditions, Lys (325, 327) is the most reactive. In globular actin, Lys 18, 191, 290, 314. and 358 are less than 20% as reactive as Lys (325, 327); the remaining have intermediate reactivities. On polymerization in the presence of NaCl and Mg2+, lysines 50, 61, 68, 113, and 290 become less reactive relative to Lys (325, 327). The changes in Lys 50, 61, and 113 are due largely to the polymerization event whereas those in Lys 68 and 290 appear to be an effect of Mg2+. Lys 18, 191, and 358 increase in relative reactivity when cation is added to the monomer and then become less reactive in the polymer, showing no large overall change in reactivity relative to the monomer in the absence of salt. Lysines that are reduced in reactivity upon polymerization indicate possible contact regions between actin monomers in the filament in the NH2-terminal third of the protein.
mesh_terms: D000089:Acetic Anhydrides / Q000494:pharmacology; D000199:Actins / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002250:Carbon Radioisotopes; D002918:Chymotrypsin; D008239:Lysine; D046911:Macromolecular Substances; D009132:Muscles / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis; D011817:Rabbits; D014357:Trypsin
chemical_list: D000089:Acetic Anhydrides; D000199:Actins; D000596:Amino Acids; D002250:Carbon Radioisotopes; D046911:Macromolecular Substances; D010446:Peptide Fragments; C031800:acetic anhydride; D002918:Chymotrypsin; D014357:Trypsin; D008239:Lysine