Abstract
The advent of techniques for cloning and rapidly sequencing DNA has produced an explosive increase of sequence information for nucleic acids and their inferred proteins. Careful study of this large store of data might give us new insights into the relations between the linear sequences of genes and their functions embodied in the three-dimensional structure of proteins, and also illuminate the origin and evolution of the structural complexity of present-day proteins. Here I argue from such a study that the active site sequences of enzymes that have analogous essential serine residues lie in fact on two lines of descent from an ancient ancestral enzyme which had a cysteine instead of serine in its active site. This is based on the assumption that the two codon types which define the separate lines of descent and which have different bases in two positions could not interconvert by single mutations.
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
Miller, J., McLachlan, A. D. & Klug, A. EMBO J. 4, 1609–1614 (1985).
Kretsinger, R. H. & Nockholds, C. E. J. biol. Chem. 248, 3313–3326 (1973).
Tso, J. Y., Van Den Berg, D. J. & Korn, L. J. Nucleic Acids Res. 14, 2187–2200 (1986).
Emori, Y., Ohno, S., Tobita, M. & Suzuki, K. FEBS Lett. 194, 249–252 (1986).
Sigal, I. S., Harwood, B. G. & Arentzen, R. Proc. natn. Acad. Sci. U.S.A. 79, 7157–7160 (1982).
Dalbadie-McFarland, C., Neitzel, J. J. & Richards, J. H. Biochemistry 25, 332–338 (1986).
Neet, K. E. & Koshland, D. E. Jr Proc. natn. Acad. Sci. U.S.A. 56, 1060–1611 (1966).
Lockridge, O. et al. J. biol. Chem. 262, 549–557 (1987).
Coulson, A. F. W., Collins, J. F. & Lyall, A. Computer J. 30, 420–424 (1987).
Toyoda, H. et al. Cell 45, 761–770 (1986).
Argos, P., Kamer, G., Nicklin, M. J. H. & Wimmer, E. Nucleic Acids Res. 12, 7251–7276 (1984).
Weng, M., Makaroff, C. A. & Zalkin, H. J. biol. Chem. 261, 5568–5574 (1985).
Cohn, D. H. et al. J. biol. Chem. 260, 6139–6146 (1985).
Taparowsky, E., Shimuzu, K., Goldfarb, M. & Wigler, M. Cell 34, 581–586 (1983).
Powers, S. et al. Cell 36, 607–612 (1984).
Nagata, S. et al. EMBO J. 3, 1825–1830 (1984).
An, G. & Friesen, J. D. Gene 12, 33–39 (1980).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Brenner, S. The molecular evolution of genes and proteins: a tale of two serines. Nature 334, 528–530 (1988). https://doi.org/10.1038/334528a0
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1038/334528a0
This article is cited by
-
Recent advances in the production, properties and applications of haloextremozymes protease and lipase from haloarchaea
World Journal of Microbiology and Biotechnology (2023)
-
Molecular, structural and biochemical characterization of a novel recombinant chlorophyllase from cyanobacterium Oscillatoria acuminata PCC 6304
Microbial Cell Factories (2021)
-
Biodegradable properties of organophosphorus insecticides by the potential probiotic Lactobacillus plantarum WCP931 with a degrading gene (opdC)
Applied Biological Chemistry (2021)
-
Characterisation of a lysophospholipase from Lactobacillus mucosae
Biotechnology Letters (2020)
-
Biochemical Characterization of a Lipolytic Enzyme From Aspergillus oryzae That Hydrolyzes Triacylglycerol and Sterol Esters
Applied Biochemistry and Biotechnology (2020)
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.
