Calcium binding of arterial tropomyosin: involvement in the thin filament regulation of smooth muscle

The implication of part of the C-terminal of actin (within the 285-375 sequence) in the interaction of serum gelsolin was investigated by the use of specific antibodies. These antibodies were directed against two or three discrete epitopes, one of which was specific for skeletal-muscle actin. Some of these epitopes were found to be near the serum gelsolin-actin interface. Thus it can be assumed that part of the C-terminal of actin is exposed at the barbed end of the actin filament. The interaction between tropomyosin and actin was also studied.

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“…purified by the procedure of Cavadore et al (1985b). Serum gelsolin was purified as described by Soua et al (1985).…”

Section: Materials and Methods Actins Abp And Derivativesmentioning

confidence: 99%

Antigenic probes locate a serum-gelsolin-interaction site on the C-terminal part of actin

Boyer

Feinberg

Hüe

et al. 1987

Biochemical Journal

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Evolution of tropomyosin functional domains: Differential splicing and genomic constraints

et al. 1988

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We have cloned and determined the nucleotide sequence of a complementary DNA (cDNA) encoded by a newly isolated human tropomyosin gene and expressed in liver. Using the least-square method of Fitch and Margoliash, we investigated the nucleotide divergences of this sequence and those published in the literature, which allowed us to clarify the classification and evolution of the tropomyosin genes expressed in vertebrates. Tropomyosin undergoes alternative splicing on three of its nine exons. Analysis of the exons not involved in differential splicing showed that the four human tropomyosin genes resulted from a duplication that probably occurred early, at the time of the amphibian radiation. The study of the sequences obtained from rat and chicken allowed a classification of these genes as one of the types identified for humans. The divergence of exons 6 and 9 indicates that functional pressure was exerted on these sequences, probably by an interaction with proteins in skeletal muscle and perhaps also in smooth muscle; such a constraint was not detected in the sequences obtained from nonmuscle cells. These results have led us to postulate the existence of a protein in smooth muscle that may be the counterpart of skeletal muscle troponin. We show that different kinds of functional pressure were exerted on a single gene, resulting in different evolutionary rates and different convergences in some regions of the same molecule. Codon usage analysis indicates that there is no strict relationship between tissue types (and hence the tRNA precursor pool) and codon usage. G + C content is characteristic of a gene and does not change significantly during evolution.(ABSTRACT TRUNCATED AT 250 WORDS)

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Polyacrylamide gel electrophoretic methods in the separation of structural muscle proteins

Bárány¹,

Bárány²,

Giometti³

1995

Journal of Chromatography A

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Calcium binding of arterial tropomyosin: involvement in the thin filament regulation of smooth muscle

Cited by 7 publications

References 41 publications

Antigenic probes locate a serum-gelsolin-interaction site on the C-terminal part of actin

Antigenic probes locate a serum-gelsolin-interaction site on the C-terminal part of actin

Evolution of tropomyosin functional domains: Differential splicing and genomic constraints

Polyacrylamide gel electrophoretic methods in the separation of structural muscle proteins

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