Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Letter
  • Published:

11-cis vitamin A in dark-adapted rod outer segments is a probable source of prosthetic groups for rhodopsin biosynthesis

Abstract

THROUGHOUT life, the outer segments of rod photoreceptors (ROS) are renewed continually1, a process that entails assembly of new disk membranes at the base of the ROS. Biosynthesis of the apoprotein of rhodopsin, the major membrane protein of the ROS disks, is known to occur in several stages in the inner segment2–5. Bok has found, however, that completion of the rhodopsin molecule by combination with its retinaldehyde prosthetic group does not take place until after the apoprotein has been transported to the ROS6, perhaps just before its insertion in to the membrane. The process continues unimpaired in darkness7,8, so that in these conditions a pool of 11-cis vitamin A should be readily available close to the site of synthesis.

This is a preview of subscription content, access via your institution

Access options

Buy this article

Prices may be subject to local taxes which are calculated during checkout

Similar content being viewed by others

References

  1. Young, R. W., J. Cell Biol., 33, 61–72 (1967).

    Article  CAS  Google Scholar 

  2. Bok, D., Basinger, S. F., and Hall, M. O., Expl Eye Res., 18, 225–240 (1974).

    Article  CAS  Google Scholar 

  3. O'Brien, P. J., and Muellenberg, C. G., Expl Eye Res., 18, 241–252 (1974).

    Article  CAS  Google Scholar 

  4. Hall, M. O., Bok, D., and Bacharach, A. D. E., J. molec. Biol., 45, 397–406 (1969).

    Article  CAS  Google Scholar 

  5. Papermaster, D. S., Converse, C. A., and Siu, J., Biochemistry, 14, 1343–1352 (1975).

    Article  CAS  Google Scholar 

  6. Bok, D., Abstr. Ass. Res. Vision Ophthal. Sarasota, USA, No. 5, 32 (1975).

  7. Bridges, C. D. B., and Yoshikami, S., Nature, 221, 275–276 (1969).

    Article  ADS  CAS  Google Scholar 

  8. Hall, M. O., and Bok, D., Expl Eye Res., 18, 105–117 (1974).

    Article  ADS  CAS  Google Scholar 

  9. Papermaster, D. S., and Dreyer, W. J., Biochemistry, 13, 2438–2444 (1974).

    Article  CAS  Google Scholar 

  10. Bridges, C. D. B., Vision Res., 15, 1311–1323 (1975).

    Article  CAS  Google Scholar 

  11. Hubbard, R., Brown, P. K., and Bownds, D., in Methods in Enzymology, 18, (edit. by McCormick, D. B., and Wright, L. D.), 615–653 (Academic, New York, 1971).

    Google Scholar 

  12. Wald, G., J. gen. Physiol, 19, 351–371 (1935).

    Article  CAS  Google Scholar 

  13. Hubbard, R., and Dowling, J. E., Nature, 193, 341–343 (1962).

    Article  ADS  CAS  Google Scholar 

  14. Bridges, C. D. B., Expl Eye Res. (in the press).

  15. Andrews, J. S., and Futterman, S., J. biol. Chem., 239, 4073–4076 (1964).

    CAS  PubMed  Google Scholar 

  16. Futterman, S., and Andrews, J. S., J. biol. Chem., 239, 81–84 (1964).

    CAS  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

BRIDGES, C. 11-cis vitamin A in dark-adapted rod outer segments is a probable source of prosthetic groups for rhodopsin biosynthesis. Nature 259, 247–248 (1976). https://doi.org/10.1038/259247a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/259247a0

This article is cited by

Comments

By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.

Search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing