Skip to main content
PMC home page
Nucleic Acids Research logoLink to Nucleic Acids Research
. 1988 Sep 26;16(18):9017–9026. doi: 10.1093/nar/16.18.9017

Conservation of short patches of amino acid sequence amongst proteins with a common function but evolutionarily distinct origins: implications for cloning genes and for structure-function analysis.

J K Reichardt 1, P Berg 1
PMCID: PMC338649  PMID: 2845364

Abstract

Small patches of identical amino acid sequences commonly occur in proteins that have the same function but are derived from evolutionarily distant organisms. Reverse translation of such patches into degenerate pools of oligonucleotides provide useful hybridization probes for cloning the gene for the corresponding protein from other organisms. Since the conserved patches of identical amino acid sequence are probably important for the protein's biological function, they are preferred targets for reverse genetic studies aimed at defining structure-function relationships.

Full text

PDF

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Adams C. W., Fornwald J. A., Schmidt F. J., Rosenberg M., Brawner M. E. Gene organization and structure of the Streptomyces lividans gal operon. J Bacteriol. 1988 Jan;170(1):203–212. doi: 10.1128/jb.170.1.203-212.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Banner D. W., Bloomer A. C., Petsko G. A., Phillips D. C., Pogson C. I., Wilson I. A., Corran P. H., Furth A. J., Milman J. D., Offord R. E. Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5 angstrom resolution using amino acid sequence data. Nature. 1975 Jun 19;255(5510):609–614. doi: 10.1038/255609a0. [DOI] [PubMed] [Google Scholar]
  3. Biesecker G., Harris J. I., Thierry J. C., Walker J. E., Wonacott A. J. Sequence and structure of D-glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus. Nature. 1977 Mar 24;266(5600):328–333. doi: 10.1038/266328a0. [DOI] [PubMed] [Google Scholar]
  4. Clarke N. D., Lien D. C., Schimmel P. Evidence from cassette mutagenesis for a structure-function motif in a protein of unknown structure. Science. 1988 Apr 22;240(4851):521–523. doi: 10.1126/science.3282306. [DOI] [PubMed] [Google Scholar]
  5. Hanks S. K. Homology probing: identification of cDNA clones encoding members of the protein-serine kinase family. Proc Natl Acad Sci U S A. 1987 Jan;84(2):388–392. doi: 10.1073/pnas.84.2.388. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. McAlister-Henn L. Evolutionary relationships among the malate dehydrogenases. Trends Biochem Sci. 1988 May;13(5):178–181. doi: 10.1016/0968-0004(88)90146-6. [DOI] [PubMed] [Google Scholar]
  7. Patthy L. Detecting homology of distantly related proteins with consensus sequences. J Mol Biol. 1987 Dec 20;198(4):567–577. doi: 10.1016/0022-2836(87)90200-2. [DOI] [PubMed] [Google Scholar]
  8. Reichardt J. K., Berg P. Cloning and characterization of a cDNA encoding human galactose-1-phosphate uridyl transferase. Mol Biol Med. 1988 Apr;5(2):107–122. [PubMed] [Google Scholar]
  9. Samols D., Thornton C. G., Murtif V. L., Kumar G. K., Haase F. C., Wood H. G. Evolutionary conservation among biotin enzymes. J Biol Chem. 1988 May 15;263(14):6461–6464. [PubMed] [Google Scholar]
  10. Thelander L., Berg P. Isolation and characterization of expressible cDNA clones encoding the M1 and M2 subunits of mouse ribonucleotide reductase. Mol Cell Biol. 1986 Oct;6(10):3433–3442. doi: 10.1128/mcb.6.10.3433. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Williams V. P., Fried C., Popják G. Human red cell galactose 1-phosphate uridylyltransferase: effects of site-specific reagents on catalytic activity. Arch Biochem Biophys. 1981 Feb;206(2):353–361. doi: 10.1016/0003-9861(81)90102-8. [DOI] [PubMed] [Google Scholar]

Articles from Nucleic Acids Research are provided here courtesy of Oxford University Press

RESOURCES