Interaction of ADP‐ribosylated actin with actin binding proteins

[摘要]

Actin ADP-ribosylated at Arg177 was previously shown not to polymerise after increasing the ionic strength, but to cap the barbed ends of filaments. Here we confirm that the polymerisation of ADP-ribosylated actin is inhibited, however, under specific conditions the modified actin copolymerises with native actin, indicating that its ability to take part in normal subunit interactions within filaments is not fully eliminated. We also show that ADP-ribosylated actin forms antiparallel but not parallel dimers: the former are not able to form filaments. ADP-ribosylated actin interacts with deoxyribonuclease I, vitamin D binding protein, thymosin β₄, cofilin and gelsolin segment 1 like native actin. Interaction with myosin subfragment 1 revealed that the potential of the modified actin to aggregate into oligomers or short filaments is not fully eliminated.

[学科分类] 生物化学/生物物理

[关键词] Actin binding protein;ADP-ribosylated actin;DbP;vitamin D binding protein;DNase I;deoxyribonuclease I (EC 3.1.21.1.);EDC;1-ethyl-3[3(dimethylamino)propyl] carbodiimide;FFD;1;5-difluoro-2;4-dinitrobenzene;LD;lower dimer of actin;1;4-PBM;1;4-phenylene-bismaleimide;NAD;nicotinamide adenindinucleotide;Tβ4;thymosin β4