Abstract
The Gram-negative bacterium Myxococcus xanthus has a complex life cycle1 during which large amounts of a protein of relative molecular mass (Mr) 19,000, known as protein S, are assembled into a spore surface coat by a process that specifically requires calcium ions2,3. The gene for protein S has been cloned and the DNA sequence shows that the gene product is composed of four internally repeated homologous sequences, each 40 amino acids long4. Although protein S resembles calmodulin both in its internally duplicated structure and its ability to bind calcium4, it apparently has a β-sheet secondary structure5 rather than the helix–loop–helix motifs that characterize the calmodulin family6–8. We now show that protein S has a striking homology with the β- and γ-crystallins of the vertebrate eye lens9–11 which are β-sheet proteins with internally duplicated structures. This implies that the β- and γ-crystallins evolved from already existing proteins, whose ancestors occurred in the prokaryotes. The biological function of protein S, as a closely packed, stable protein in a relatively dehydrated environment, has implications for the functions of crystalline, which are found closely packed in the lens fibre cells, where their stability is essential for maintenance of transparency.
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References
Kaiser, D., Manoil, C. & Dworken, M. A. Rev. Microbiol. 33, 595–639 (1979).
Inouye, M., Inouye, S. & Zusman, D. R. Devl Biol. 68, 579–591 (1979).
Inouye, M., Inouye, S. & Zusman, D. R. Proc. natn. Acad. Sci. U.S.A. 76, 209–213 (1979).
Inouye, S., Franceschini, T. & Inouye, M. Proc. natn. Acad. Sci. U.S.A. 80, 6829–6833 (1983).
Inouye, S., Harada, W., Zusman, D. & Inouye, M. J. Bact. 148, 678–683 (1981).
Kretsinger, R. H. & Nockolds, C. E. J. biol. Chem. 248, 3313–3326 (1973).
Szebenyi, D. M. E., Obendorf, S. K. & Moffat, K. Nature 294, 327–332 (1981).
Kretsinger, R. H. CRC crit. Rev. Biochem. 8, 119–174 (1980).
Blundell, T. L. et al. Nature 289, 771–7777 (1981).
Wistow, G. et al. J. molec. Biol. 170, 173–202 (1983).
Summers, L. et al. Peptide and Protein Reviews Vol. 3 (ed. Hearn, M. T. W.) 147–168 (Dekker, New York, 1984).
Bhat, S. P. & Spector, A. DNA 3, 287–296 (1984).
Moormann, R. J. M., Den Dunnen, J. T., Bloemendal, H. & Schoenmakers, J. G. G. Proc. natn. Acad. Sci. U.S.A. 79, 6876–6880 (1982).
Tomarev, S. F., Krayev, A. S., Skryabin, K. G., Gause, G. G. & Bayev, A. A. Dokl. Akad. Nauk SSSR 263, 1489–1492 (1982).
Tomarev, S. F., Krayev, A. S., Skryabin, K. G., Bayev, A. & Gause, G. G. FEBS Lett. 146, 315–318 (1982).
Lok, S. et al. Nucleic Acids Res. 12, 4517–4529 (1984).
Driessen, H. P. C., Herbrink, P., Bloemendal, H. & de Jong, W. W. FEBS Lett. 161, 225–229 (1981).
Inana, G., Piatigorsky, J., Norman, B., Slingsby, C. & Blundell, T. L. Nature 302, 310–315 (1983).
Schoenmakers, J. G. G. et al. Ciba Fdn Symp. 106, 208–218 (1984).
Lesk, A. & Chothia, C. J. molec. Biol. 160, 325–342 (1982).
Inouye, S., Inouye, M., McKeever, B. & Sarma, R. J. biol. Chem. 255, 3713–3714 (1980).
Inouye, S., Ike, Y. & Inouye, M. J. biol. Chem. 258, 38–40 (1983).
Giblin, F. J., Hightower, K. R., Ragatzki, P. A. & Readdy, V. N. Expl Eye Res. 39, 9–17 (1984).
Harding, J. J. & Dilley, K. J. Expl Eye Res. 22, 1–73 (1976).
Jones, T. A. J. appl. Crystallogr. 11, 268–272 (1978).
Wistow, G. et al. FEBS Lett. 133, 9–16 (1981).
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Wistow, G., Summers, L. & Blundell, T. Myxococcus xanthus spore coat protein S may have a similar structure to vertebrate lens βγ-crystallins. Nature 315, 771–773 (1985). https://doi.org/10.1038/315771a0
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DOI: https://doi.org/10.1038/315771a0
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