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Phosphorylation loops in synthetic peptides of the human neurofilament protein middle-sized subunit

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Abstract

Peptides containing 13 and 39 amino acid residues and serine-side-chain-phosphorylated (P) analogues thereof, corresponding to human neurofilament protein middle-sized subunit (NF-M), have been synthesized in order to localize the phosphorylation site of this protein. The secondary structure of the nonphosphorylated peptides, determined by circular dichroism (CD) measurements, predicted secondary structural calculations and energy conformational calculations, was suggested to be a series of alternating type I (III) β-turns and 310 or α-helices. By contrast, the phosphorylated peptides exhibit a unique conformation, probably due to salt bridges between the phosphoserine and the lysine residues. This has provided the first clear evidence that phosphorylation induces conformational changes among these synthetic peptides and presumably, in NF proteins as well. These phosphorylation loops might be the major recognition sites of the neurofilament protein-directed kinases.

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References

  • Bandekar, F., Evans, D. F., Krimm, S., Leach, S. F., Lee, S. McQuie, F. R., Minasian, E., Nemethy, A., Pottle, M. S., Scheraga, H. A., Stimson, E. R., and Woody, R. W. (1982).Int. J. Peptide Protein Res. 19, 187–201.

    Article  CAS  Google Scholar 

  • Chang, C. T., Wu, C.-S. C., and Yang, J. T. (1978).Anal. Biochem. 91, 13–31.

    Article  CAS  PubMed  Google Scholar 

  • Chen, Y.-H., Yang, J. T., and Chau, K. H. (1974).Biochemistry 13, 3350–3359.

    Article  CAS  PubMed  Google Scholar 

  • Chou, P. Y., and Fasman, G. D. (1978).Adv. Enzymology 47, 45–148.

    CAS  Google Scholar 

  • Fasman, G. D., Hollosi, M., and Perczel, A. (1988). Manuscript in preparation.

  • Ferrel, R. E., Olcott, H. S., and Fraenkel-Conrat, H. J. (1948).J. Am. Chem. Soc. 70, 2101–2107.

    Article  CAS  PubMed  Google Scholar 

  • Francis, A. K., Iqbal, M., Balaram, P., and Vijayan, M. (1983).FEBS Lett. 155, 230–232.

    Article  CAS  Google Scholar 

  • Frank, A. N. (1984).CRC Crit. Rev. Biochem. 16(1), 51–101.

    Article  CAS  PubMed  Google Scholar 

  • Gierasch, L. M., Deber, C. M., Madison, V., Niu, C.-H., and Blout, E. R. (1981).Biochemistry 20, 4730–4738.

    Article  CAS  PubMed  Google Scholar 

  • Glazer, A. N., DeLange, R. J., and Sigman, D. S. (1975). InLaboratory Techniques in Biochemistry and Molecular Biology (Work, T. S., and Work, E., eds.), American Elsevier-North-Holland, New York, pp. 51–52.

    Google Scholar 

  • Greenfield, N., and Fasman, G. D. (1969).Biochemistry 8, 4108–4116.

    Article  CAS  PubMed  Google Scholar 

  • Hider, R. C., Ragnarsson, U., and Zetterquist, O. (1985).J. Biochem. 229, 485–489.

    Article  CAS  Google Scholar 

  • Hollosi, M., Kawai, M., and Fasman, G. D. (1985).Biopolymers 24, 211–242.

    Article  CAS  PubMed  Google Scholar 

  • Hollosi, M., Kover, K. E., Holly, S., Radics, L., and Fasman, G. D. (1987).Biopolymers 26, 1555–1572.

    Article  CAS  PubMed  Google Scholar 

  • Kaplan, L. I., Bauer, R., Morrison, E., Langan, T. A., and Fasman, G. D. (1984).J. Biol. Chem. 259, 8777–8785.

    Article  CAS  PubMed  Google Scholar 

  • Lee, Virginia M.-Y., Otvos, L., Jr., Carden, M. J., Hollosi, M., Dietzschold, B., and Lazzarini, R. A. (1988).Proc. Natl. Acad. Sci. U.S.A. 85, 1998–2002.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • McClare, C. W. I. (1971).Anal. Biochem. 39, 527–530.

    Article  CAS  PubMed  Google Scholar 

  • Myers, M. M., Lazzarini, R. A., Lee, V. M.-Y., Schaepfer, W. W., and Nelson, D. (1987).EMBO J. 6, 1617–1626.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Nussbaum, S. R., Beaudette, N. V., Fasman, G. D., Potts, J. T., and Rosenblatt, M. (1985).J. Protein Chem. 4, 391–406.

    Article  CAS  Google Scholar 

  • Otvos, L., Jr., Dietzschold, B., and Kisfaludy, L. (1987).Int. J. Peptide Protein Res. 30, 511–514.

    Article  CAS  Google Scholar 

  • Savin, V. K., Kent, S. B. H., Tam, J. P., and Merrifield, R. B. (1981).Anal. Biochem. 117, 147–157.

    Article  Google Scholar 

  • Schlesinger, D. H., Buku, A., Wyssbrod, H. R., and Hay, D. I. (1987).Int. J. Peptide Protein Res. 30, 257–262.

    Article  CAS  Google Scholar 

  • Smith, F. A., and Pease, L. G. (1980).CRC Crit. Rev. Biochem. 8, 315–399.

    Article  CAS  PubMed  Google Scholar 

  • Sudha, T. S., Vijayakumar, E. U. S., and Balaram, P. (1983)Int. J. Peptide Protein Res. 22, 464–468.

    Article  CAS  Google Scholar 

  • Venkatachalam, C. M. (1968).Biopolymers 6, 1425–1436.

    Article  CAS  PubMed  Google Scholar 

  • Woody, R. W. (1974). InPeptides, Polypeptides and Proteins (Blout, E. R., Bovey, F. A., Goodman, M., and Lotan, M., eds.), Wiley, New York, pp. 338–360.

    Google Scholar 

  • Woody, R. W. (1985). inThe Peptides. Vol. 7 (Hruby, V. J., ed.), Academic Press, Orlando, Florida, pp. 15–114.

    Google Scholar 

  • Yang, J. T., Wu, C.-S., and Hugo, M. (1986).Methods Enzymol. 130, 208–269.

    Article  CAS  PubMed  Google Scholar 

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Otvos, L., Hollosi, M., Perczel, A. et al. Phosphorylation loops in synthetic peptides of the human neurofilament protein middle-sized subunit. J Protein Chem 7, 365–376 (1988). https://doi.org/10.1007/BF01024886

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