Comparative study of invertebrate actins: Antigenic cross-reactivity versus sequence variability

Hüe, H.; Benyamin, Yves; Roustan, Claude

doi:10.1007/bf01739969

Cited by 9 publications

(4 citation statements)

References 30 publications

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“…Mejean et al (1987), using a second antibody population directed against the 18-28 segment, characterized a major contact area for S-1 in the hydrophilic constant 18-28 sequence (Hue et al, 1989). 1H n.m.r.…”

Section: Introductionmentioning

confidence: 99%

Characterization of an actin-myosin head interface in the 40–113 region of actin using specific antibodies as probes

Labbé

Méjean

Benyamin

et al. 1990

Biochemical Journal

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Evidence for the participation of the 1-7 and 18-28 N-terminal sequences of actin at different steps of actin-myosin interaction process is well documented in the literature. Cross-linking of the rigor complex between filamentous actin and skeletal-muscle myosin subfragment 1 was accomplished by the carboxy-group-directed zero-length protein cross-linker, 1-ethyl-3-[3-(dimethylamino)propyl]carbodi-imide. After chaotropic depolymerization and thrombin digestion, which cleaves only actin, the covalent complex with Mr 100,000 was characterized by PAGE. The linkage was identified as being between myosin subfragment 1 (S-1) heavy chain and actin-(1-28)-peptide. The purified complex retained in toto its ability to combine reversibly with fresh filamentous actin, but showed a decrease in the Vmax. of actin-dependent Mg2(+)-ATPase. By using e.l.i.s.a., S-1 was observed to bind to coated monomeric actin or its 1-226 N-terminal peptide. This interaction strongly interfered with the binding of antibodies directed against the 95-113 actin sequence. Moreover, S-1 was able to bind with coated purified actin-(40-113)-peptide. Finally, antibodies directed against the 18-28 and 95-113 actin sequence, which strongly interfered with S1 binding, were unable to compete with each other. These results suggest that two topologically independent regions are involved in the actin-myosin interface: one located in the conserved 18-28 sequence and the other near residues 95-113, including the variable residue at position 89. Other experiments support the 'multisite interface model', where the two actin sites could modulate each other during S-1 interaction.

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Section: Introductionmentioning

confidence: 99%

Characterization of an actin-myosin head interface in the 40–113 region of actin using specific antibodies as probes

Labbé

Méjean

Benyamin

et al. 1990

Biochemical Journal

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“…Double-labeling co-immunofluorescence further revealed the location of PDCP-1 together with the actin on the shell surface and confirmed the interaction of PDCP-1 with the actin at the nacre and the myostracum layer. The PDZ/actin interaction may be important for shell formation and the attachment between adductor muscle-myostracum, considering that abundant actin was identified from Mytilus shell ( Gao et al, 2015 ; Liao et al, 2015 ), and the actin is also the main component of adductor muscle ( Hue et al, 1989 ).…”

Section: Discussionmentioning

confidence: 99%

Molecular Characterization of a Novel Shell Matrix Protein With PDZ Domain From Mytilus coruscus

et al. 2020

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Mollusk shells are products of biomineralization and possess excellent mechanical properties, and shell matrix proteins (SMPs) have important functions in shell formation. A novel SMP with a PDZ domain (PDZ-domain-containing-protein-1, PDCP-1) was identified from the shell matrices of Mytilus coruscus. In this study, the gene expression, function, and location of PDCP-1 were analyzed. PDCP-1 was characterized as an ∼70 kDa protein with a PDZ (postsynaptic density/discs large/zonula occludes) domain and a ZM (ZASP-like motif) domain. The PDCP-1 gene has a high expression level and specific location in the foot, mantle and adductor muscle. Recombinantly expressed PDCP-1 (rPDCP-1) altered the morphology of calcite crystals, the polymorph of calcite crystals, binding with both calcite and aragonite crystals, and inhibition of the crystallization rate of calcite crystals. In addition, anti-rPDCP-1 antibody was prepared, and immunohistochemistry and immunofluorescence analyses revealed the specific location of PDCP-1 in the mantle, the adductor muscle, and the aragonite (nacre and myostracum) layer of the shell, suggesting multiple functions of PDCP-1 in biomineralization, muscle-shell attachment, and muscle attraction. Furthermore, pull-down analysis revealed 19 protein partners of PDCP-1 from the shell matrices, which accordingly provided a possible interaction network of PDCP-1 in the shell. These results expand the understanding of the functions of PDZ-domain-containing proteins (PDCPs) in biomineralization and the supramolecular chemistry that contributes to shell formation.

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“…These antibodies were specific to three epitopes in skeletal-muscle actin, including residues Met-305, Met-325 and Met-355. The different antibody populations were selectively purified by affinity chromatography using scallop actin, which differs from rabbit actin by a mutation at position 306 (Boyer et al, 1987;Hue et al, 1989), immobilized on Sepharose 4B. Anti-[actin-(285-375)] antibodies were first purified on a rabbit S-carboxymethylated skeletal-muscle actin column.…”

Section: Immunological Techniquesmentioning

confidence: 99%

Interaction of skeletal-muscle myosin subfragment-1 with the actin-(338-348) peptide.

Labbé

Lelievre

Boyer

et al. 1994

Biochemical Journal

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Comparative study of invertebrate actins: Antigenic cross-reactivity versus sequence variability

Cited by 9 publications

References 30 publications

Characterization of an actin-myosin head interface in the 40–113 region of actin using specific antibodies as probes

Characterization of an actin-myosin head interface in the 40–113 region of actin using specific antibodies as probes

Molecular Characterization of a Novel Shell Matrix Protein With PDZ Domain From Mytilus coruscus

Interaction of skeletal-muscle myosin subfragment-1 with the actin-(338-348) peptide.

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