1887

Abstract

A group of prokaryotic actin-related proteins (PARP) with an of 43000 was detected in . These proteins were enriched by a depolymerization/polymerization cycle, under similar conditions to those used to polymerize muscle actin, and purified by affinity chromatography on a DNase I-Sepharose column. Three isoforms of PARP (-PARP) with pI values of 58, 615 and 62 were detected. -PARP were recognized by four different anti-actin antibodies (one anti-muscle and three anti-cytoplasmic isoforms). -PARP were also recognized by antibodies against PARP (-PARP) and against actin-binding proteins such as α-actinin and spectrin, and also by a monoclonal antibody against heat-shock cognate protein 70 (Hsc70). Specific binding of phalloidin to -PARP was detected both in permeabilized cells and . Purified -PARP can polymerize under similar conditions to those required for skeletal muscle actin polymerization and the filaments formed appear to be decorated with myosin subfragment-1 (S1) as observed by transmission electron microscopy. The amino acid composition of -PARP revealed more similarities to muscle γ-actin and the cytoplasmic β-actin isoform than to eukaryotic actin-related proteins.

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1999-11-01
2021-08-04
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