Abstract
In bacteriophage λ, genes C and Nu3, two of the four cistrons which are essential for normal prohead formation, have overlapping nucleotide sequences. These genes are translated in the same reading frame so that the Nu3 protein is identical to the COOH-terminal one-third of the C protein. This structural relationship may provide for the functional interaction of the C and Nu3 proteins through their regions of structural homology during prohead assembly. The in-phase overlapping organisation of genes may constitute a general strategy to facilitate the mutual interaction of a pair of proteins through their common structural domains.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Campbell, A. Virology 14, 22–32 (1961).
Parkinson, J. S. Genetics 59, 311–325 (1968).
Boklage, E. E., Wong, E. C. & Bode, V. C. Genetics 75, 221–230 (1973).
Jara, L. & Murialdo, H. Virology 64, 264–268 (1975).
Murialdo, H. & Siminovitch, L. Virology 48, 824–835 (1972).
Murialdo, H. & Becker, A. Microbiol. Rev. 42, 529–576 (1978).
Hohn, T. & Katsura, I. Curr. Topics Microbiol. Immun. 78, 69–110 (1977).
Hohn, B. & Hohn, T. Proc. natn. Acad. Sci. U.S.A. 71, 2372–2376 (1974).
Hohn, B., Wurtz, M., Klein, B., Lustig, A. & Hohn, T. J. supramolec. Struct. 2, 302–317 (1974).
Kaiser, A. D., Syvanen, M. & Masuda, T. J. supramolec. Struct. 2, 318–328 (1974); J. molec. Biol 91, 175–186 (1975).
Becker, A., Murialdo, H. & Gold, M. Virology 78, 277–290 (1977).
Murialdo, H. & Becker, A. Proc. natn. Acad. Sci. U.S.A. 74, 906–910 (1977).
Murialdo, H. & Becker, A. J. molec. Biol. 125, 57–74 (1978).
Hohn, T., Flick, H. & Hohn, B. J. molec. Biol. 98, 107–120 (1975).
Hendrix, R. W. & Casjens, S. R. J. molec. Biol. 91, 187–199 (1975).
Zachary, A., Simon, L. D. & Litwin, S. Virology 72, 429–442 (1976).
Ray, P. N. & Murialdo, H. Virology 64, 247–263 (1975).
Hendrix, R. W. & Casjens, S. R. Proc. natn. Acad. Sci. U.S.A. 71, 1451–1455 (1974); J. supramolec. Struct. 2, 329–336 (1974).
Murialdo, H. & Ray, P. N. Nature 257, 815–817 (1975).
Murialdo, H. & Siminovitch, L. Virology 48, 785–823 (1972).
O'Farrell, P. H. J. biol. Chem. 250, 4007–4021 (1975).
Shaw, J. E., Bingham, H., Fuerst, C. R. & Pearson, M. L. Virology 83, 180–194 (1977).
Hunter, T. & Gibson, W. J. Virol. 28, 240–253 (1978).
Siddell, S. G. & Smith, A. E. J. Virol 27, 427–431 (1978).
Linney, E. & Hayashi, M. Nature 249, 345–348 (1974).
Ray, P. N. & Pearson, M. L. J. molec. Biol 85, 163–175 (1974).
Herskowitz, I. & Signer, E. R. J. molec. Biol. 47, 545–556 (1970).
Ray, P. N. & Pearson, M. L. Nature 253, 647–650 (1975).
Platt, T. & Yanofsky, C. Proc. natn. Acad. Sci. U.S.A 72, 2399–2403 (1975).
Rechler, M. M. & Martin, R. G. Nature 226, 908–911 (1970).
Yourno, J., Kohno, T. & Roth, J. R. Nature 228, 820–824 (1970).
Barrell, B. G., Air, G. M. & Hutchison, C. A. III Nature 264, 34–41 (1976).
Linney, E. A., Hayashi, M. N. & Hayashi, M. Virology 50, 381–387 (1972).
Linney, E. & Hayashi, M. Nature new Biol. 245, 6–8 (1973).
Sanger, F. et al. Nature 265, 687–695 (1977).
Godson, G. N., Barrell, B. G., Staden, R. & Fiddes, J. C. Nature 276, 236–247 (1978).
Shaw, D. C. et al. Nature 272, 510–515 (1978).
Moore, C. H., Farron, F., Bohnert, D. & Weissmann, C. Nature new Biol. 234, 204–206 (1971).
Weiner, A. M. & Weber, K. Nature new Biol. 234, 206–209 (1971).
Horiuchi, K., Webster, K. E. & Matsuhashi, S. Virology 45, 429–439 (1971).
Reddy, V. E., Dhar, R. & Weissman, S. M. J. biol. Chem. 253, 621–630 (1978).
Rozenblatt, S., Mulligan, R. C., Gorecki, M., Roberts, B. E. & Rich, A. Proc. natn. Acad. Sci. U.S.A. 73, 2747–2751 (1976).
Gibson, W., Hunter, T., Cogen, B. & Eckhart, W. Virology 80, 21–41 (1977).
Hofstetter, H., Monstein, J.-J. & Weissmann, C. Biochim. biophys. Acta. 374, 238–251 (1974).
Brady, J. N., Winston, V. D. & Consigli, R. A. J. Virol. 27, 193–204 (1978).
Moir, D. & Paulus, H. J. biol Chem. 252, 4655–4661 (1977).
Campbell, A. Genetics 48, 409–421 (1963).
Ptashne, M. Proc. natn. Acad. Sci. U.S.A. 57, 306–313 (1967).
Pirotta, V. & Ptashne, M. Nature 222, 541–544 (1969).
Shaw, J. E., Jones, B. & Pearson, M. L. Proc. natn. Acad. Sci. U.S.A. 75, 2225–2229 (1978).
Epp, C. & Pearson, M. L. in RNA Polymerase (eds Losick, R. & Chamberlain, M.) 667–691 (Cold Spring Harbor Laboratory, New York, 1976).
Laemmli, U. K. Nature 227, 680–685 (1970).
Studier, F. W. J. molec. Biol. 79, 237–248 (1973).
Bonner, W. M. & Laskey, R. A. Eur. J. Biochem. 46, 83–88 (1974).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Shaw, J., Murialdo, H. Morphogenetic genes C and Nu3 overlap in bacteriophage λ. Nature 283, 30–35 (1980). https://doi.org/10.1038/283030a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/283030a0
This article is cited by
-
Overlapping genes in bacterial and phage genomes
Molecular Biology (2000)
-
Plasmid RP4 encodes two forms of a DNA primase
Molecular and General Genetics MGG (1984)
-
Regulation and structure of aspartokinase in the genusBacillus
Journal of Biosciences (1984)
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.