Actin interaction with purified dystrophin from electric organ of Torpedo marmorata: possible resemblance with filamin-actin interface. 1995

M C Lebart, and D Casanova, and Y Benyamin
Centre de Recherche de Biochimie Macromoléculaire, U. 249 Institut National de la Santé et de la Recherche Médicale, Laboratoire de Recherche sur la Motilité Cellulaire, Ecole Pratique des Hautes Etudes, Université de Montpellier I, BP 5051, France.

We have purified dystrophin from Torpedo marmorata electric tissue by means of alkaline extraction in conjunction with an affinity chromatography column using anti-peptide antibodies. Using solution (cosedimentation) and solid phase experiments (sedimentation with Sepharose filamentous actin and ELISA), we have demonstrated that purified dystrophin is able to bind filamentous and monomeric actin. Using ELISA coupled with biotin labelled peptides and taking advantage of strong affinity binding of streptavidin-biotin complex, we have identified two exposed sequences of the actin molecule implicated in dystrophin binding: fragment 40-113, further restricted to peptide 75-106 and peptide 360-372. In a previous study, we have shown that fragment 40-113 displays binding site(s) for filamin but probably not for alpha-actinin. Moreover, we have recently reported that alpha-actinin and filamin display divergent behaviours towards conformational changes of actin. In this study, we have demonstrated that, similarly to filamin, dystrophin binding is insensitive to the locking of actin in a monomeric conformation. Taken together, these results lead us to favour the idea that dystrophin could share properties in common with filamin in its binding of actin.

UI MeSH Term Description Entries
D008840 Microfilament Proteins Monomeric subunits of primarily globular ACTIN and found in the cytoplasmic matrix of almost all cells. They are often associated with microtubules and may play a role in cytoskeletal function and/or mediate movement of the cell or the organelles within the cell. Actin Binding Protein,Actin-Binding Protein,Actin-Binding Proteins,Microfilament Protein,Actin Binding Proteins,Binding Protein, Actin,Protein, Actin Binding,Protein, Actin-Binding,Protein, Microfilament,Proteins, Actin-Binding,Proteins, Microfilament
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010455 Peptides Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS. Peptide,Polypeptide,Polypeptides
D002352 Carrier Proteins Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes. Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D003285 Contractile Proteins Proteins which participate in contractile processes. They include MUSCLE PROTEINS as well as those found in other cells and tissues. In the latter, these proteins participate in localized contractile events in the cytoplasm, in motile activity, and in cell aggregation phenomena. Contractile Protein,Protein, Contractile,Proteins, Contractile
D004557 Electric Organ In about 250 species of electric fishes, modified muscle fibers forming disklike multinucleate plates arranged in stacks like batteries in series and embedded in a gelatinous matrix. A large torpedo ray may have half a million plates. Muscles in different parts of the body may be modified, i.e., the trunk and tail in the electric eel, the hyobranchial apparatus in the electric ray, and extrinsic eye muscles in the stargazers. Powerful electric organs emit pulses in brief bursts several times a second. They serve to stun prey and ward off predators. A large torpedo ray can produce of shock of more than 200 volts, capable of stunning a human. (Storer et al., General Zoology, 6th ed, p672) Electric Organs,Organ, Electric,Organs, Electric
D000185 Actinin A protein factor that regulates the length of R-actin. It is chemically similar, but immunochemically distinguishable from actin. alpha-Actinin,Eu-Actinin,beta-Actinin,Eu Actinin,alpha Actinin,beta Actinin
D000199 Actins Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle. F-Actin,G-Actin,Actin,Isoactin,N-Actin,alpha-Actin,alpha-Isoactin,beta-Actin,gamma-Actin,F Actin,G Actin,N Actin,alpha Actin,alpha Isoactin,beta Actin,gamma Actin
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

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