Topological assignment of the N-terminal extension of plasma gelsolin to the gelsolin surface.

The actin-binding protein gelsolin is highly conserved in vertebrates and exists in two isoforms, a cytoplasmic and an extracellular variant, generated by alternative splicing. In mammals, these isoforms differ only by an N-terminal extension in plasma gelsolin, a short sequence of up to 25 amino acids. Cells and tissues may contain both variants, as plasma gelsolin is secreted by many cell types.

Comparative biochemical analysis suggests that vinculin and metavinculin cooperate in muscular adhesion sites.

Metavinculin, the muscle-specific splice variant of the cell adhesion protein vinculin, is characterized by a 68-amino acid insert within the C-terminal tail domain. The findings that mutations within this region correlate with hereditary idiopathic dilated cardiomyopathy in man suggest a specific contribution of metavinculin to the molecular architecture of muscular actin-membrane attachment sites, the nature of which, however, is still unknown. In mice, metavinculin is expressed in smooth and skeletal muscle, where it co-localizes with vinculin in dense plaques and costameres, respectively, but is of conspicuously low abundance in the heart.

Nebulin is a thin filament protein of the cardiac muscle of the agnathans.

Nebulin is an integral protein of skeletal muscle thin filaments and probably acts as a ruler for the thin filament length. Cardiac muscles of higher vertebrates have been shown earlier to lack nebulin. Instead in human and chicken cardiac muscle the much smaller protein nebulette replaces nebulin.

Identification and localisation of nebulin as a thin filament component of invertebrate chordate muscles.

The giant actin-binding protein nebulin is regarded as a component of the thin filaments in vertebrate skeletal muscles, whereas the existence of nebulin in invertebrate muscles has not yet been demonstrated. Using the cross-reactivities of polyclonal antibodies raised against nebulin from muscles of trout and lamprey, we were able to identify nebulin in the myofibrils of the cephalochordate Branchiostoma lanceolatum (lancelet) by immunoblot and immunofluorescence techniques. The approximately 720-kDa protein is localised in the I-bands of the sarcomere, where vertebrate nebulin has previously also been shown to be localised.

Metabolism of Chlorotoluenes by Burkholderia sp. Strain PS12 and Toluene Dioxygenase of Pseudomonas putida F1: Evidence for Monooxygenation by Toluene and Chlorobenzene Dioxygenases.

The degradation of toluene by Pseudomonas putida F1 and of chlorobenzenes by Burkholderia sp. strain PS12 is initiated by incorporation of dioxygen into the aromatic nucleus to form cis-dihydrodihydroxybenzenes. Toluene-grown cells of P.