Crystallization of native striated‐muscle actin

@article{Oriol1977CrystallizationON,
  title={Crystallization of native striated‐muscle actin},
  author={C Oriol and C Dubord and F Landon},
  journal={FEBS Letters},
  year={1977},
  volume={73}
}

Structure of crystalline actin sheets

It is demonstrated that actin is an elongated globular molecule with a pronounced asymmetric shape in and perpendicular to the plane of the sheet, and the results indicate that these crystalline actin sheets might be suitable for three-dimensional structure determination by low-dose electron microscopy of unstained specimens12,13 to at least 10 Å resolution.

Actin binding proteins: regulation of cytoskeletal microfilaments.

Several ABPs that regulate actin-driven assembly, i.e., movement that is independent of motor proteins, are selected that represent a family of related proteins in nature and are widely distributed in nature.

Polyamine-induced actin polymerization.

Muscle actin has been found to polymerize reversibly upon addition of low concentrations of polyamines. This polymerization, studied by centrifugation, has shown a linear relationship between the

The interaction of bovine pancreatic deoxyribonuclease I and skeletal muscle actin.

The rate of exchange of actin-bound nucleotide is decreased by a factor of about 20 when actin is complexed with DNAase I without affecting the binding constant of calcium for actin. Binding

Isolation and characterization of secretory actin . DNAase I complex from rat pancreatic juice.

It is demonstrated that a protein fraction from bile is able to activate the DNAase I enzymatic activity of the rat secretory actin .

Regulation of the cytoskeleton assembly: a role for a ternary complex of actin with two actin-binding proteins.

This chapter poses the question: does cofilin act alone in controlling actin filament assembly or is the binding of coFilin to actin modulated by other ABPs?

References

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Complete amino-acid sequence of actin of rabbit skeletal muscle.

This study represents the first complete determination of the aminoacid sequence of a myofibrillar protein and indicates that the sequence of actin is highly conserved.

The role of actin in the temperature-dependent gelation and contraction of extracts of Acanthamoeba

Data suggest that Acanthamoeba contractile proteins have a dual role in the cell; they may generate the forces for cellular movements and also act as cytoskeletal elements by controlling the consistency of the cytoplasm.

Selective carbethoxylation of the histidine residues of actin by diethylpyrocarbonate.

The analysis of these fractions showed that one of the four fast-reacting histidines of G-actin plays an essential role in polymerization.

The selective blocking of the polymerization reaction of striated muscle actin leading to a derivative suitable for crystallization. Modification of Tyr-53 by 5-diazonium-(1H)tetrazole.

The polymerization reaction of rabbit muscle actin was completely inhibited by reaction of one amino acid side chain per protein monomer with 5-diazonium-(1H)[14C]tetrazole. A tryptic peptide

Cytobiologie, in the press

  • 1976

Cold Spring Harbor Symp

  • Quant. Biol
  • 1972