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Biochemical characterization of tektins from sperm flagellar doublet microtubules.
Linck RW
,
Stephens RE
.
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Tektins, protein components of stable protofilaments from sea urchin sperm flagellar outer doublet microtubules (Linck, R. W., and G. L. Langevin, 1982, J. Cell Sci., 58:1-22), are separable by preparative SDS PAGE into 47-, 51-, and 55-kD equimolar components. High resolution two-dimensional tryptic peptide mapping reveals 63-67% coincidence among peptides of the 51-kD tektin chain and its 47- and 55-kD counterparts, greater than 70% coincidence between the 47- and 55-kD tektins, but little obvious similarity to either alpha- or beta-tubulin. With reverse-phase HPLC on a C18 column, using 6 M guanidine-HCl solubilization and a 0.1% trifluoroacetic acid/CH3CN gradient system (Stephens, R. E., 1984, J. Cell Biol. 90:37a [Abstr.]), the relatively less hydrophobic 51-kD tektin elutes at greater than 45% CH3CN, immediately followed by the 55-kD chain. The 47-kD tektin is substantially more hydrophobic, eluting between the two tubulins. The amino acid compositions of the tektins are very similar to each other but totally distinct from tubulin chains, being characterized by a greater than 50% higher arginine plus lysine content (in good agreement with the number of tryptic peptides) and about half the content of glycine, histidine, proline, and tyrosine. The proline content correlates well with the fact that tektin filaments have twice as much alpha-helical content as tubulin. Total hydrophobic amino acid content correlates with HPLC elution times for the tektins but not tubulins. The average amino acid composition of the tektins indicates that they resemble intermediate filament proteins, as originally postulated from structural, solubility, and electrophoretic properties. Tektins have higher cysteine and tryptophan contents than desmin and vimentin, which characteristically have only one residue of each, more closely resembling certain keratins in these amino acids.
Amos,
Proteins closely similar to flagellar tektins are detected in cilia but not in cytoplasmic microtubules.
1985, Pubmed,
Echinobase
Amos,
Proteins closely similar to flagellar tektins are detected in cilia but not in cytoplasmic microtubules.
1985,
Pubmed
,
Echinobase
Amos,
Studies of tektin filaments from flagellar microtubules by immunoelectron microscopy.
1987,
Pubmed
,
Echinobase
BEAVEN,
Ultraviolet absorption spectra of proteins and amino acids.
2004,
Pubmed
Bryan,
Biochemical properties of microtubules.
1974,
Pubmed
,
Echinobase
Edelhoch,
Spectroscopic determination of tryptophan and tyrosine in proteins.
1967,
Pubmed
Fairbanks,
Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane.
1971,
Pubmed
Gibbons,
Some properties of bound and soluble dynein from sea urchin sperm flagella.
1972,
Pubmed
,
Echinobase
Heinrikson,
Amino acid analysis by reverse-phase high-performance liquid chromatography: precolumn derivatization with phenylisothiocyanate.
1984,
Pubmed
LOWRY,
Protein measurement with the Folin phenol reagent.
2004,
Pubmed
Laemmli,
Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
1970,
Pubmed
Linck,
The structure of microtubules.
1982,
Pubmed
Linck,
Localization of tektin filaments in microtubules of sea urchin sperm flagella by immunoelectron microscopy.
1985,
Pubmed
,
Echinobase
Linck,
Flagellar doublet microtubules: fractionation of minor components and alpha-tubulin from specific regions of the A-tubule.
1976,
Pubmed
,
Echinobase
Linck,
Reassembly of flagellar B (alpha beta) tubulin into singlet microtubules: consequences for cytoplasmic microtubule structure and assembly.
1981,
Pubmed
,
Echinobase
Linck,
Structure and chemical composition of insoluble filamentous components of sperm flagellar microtubules.
1983,
Pubmed
,
Echinobase
Meza,
Chemical heterogeneity of protofilaments forming the outer doublets from sea urchin flagella.
1973,
Pubmed
,
Echinobase
Steinert,
The molecular biology of intermediate filaments.
1985,
Pubmed
Stephens,
Fluorescent thin-layer peptide mapping for protein identification and comparison in the subnanomole range.
1978,
Pubmed
Stephens,
Primary structural differences among tubulin subunits from flagella, cilia, and the cytoplasm.
1978,
Pubmed
,
Echinobase
Stephens,
Reconstitution of ciliary membranes containing tubulin.
1983,
Pubmed
Stephens,
High-resolution preparative SDS-polyacrylamide gel electrophoresis: fluorescent visualization and electrophoretic elution-concentration of protein bands.
1975,
Pubmed
Stephens,
Thermal fractionation of outer fiber doublet microtubules into A- and B-subfiber components. A- and B-tubulin.
1970,
Pubmed
Stephens,
Differential protein synthesis and utilization during cilia formation in sea urchin embryos.
1978,
Pubmed
,
Echinobase
Weber,
Intermediate filaments: structural conservation and divergence.
1986,
Pubmed
Weeds,
Substructure of the myosin molecule. II. The light chains of myosin.
1972,
Pubmed
Witman,
Chlamydomonas flagella. I. Isolation and electrophoretic analysis of microtubules, matrix, membranes, and mastigonemes.
1972,
Pubmed
Witman,
Chlamydomonas flagella. II. The distribution of tubulins 1 and 2 in the outer doublet microtubules.
1972,
Pubmed
Zweidler,
Resolution of histones by polyacrylamide gel electrophoresis in presence of nonionic detergents.
1978,
Pubmed
