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
- 25 September 1988
- journal article
- research article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 16 (18) , 9017-9026
- https://doi.org/10.1093/nar/16.18.9017
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.This publication has 11 references indexed in Scilit:
- Evolutionary conservation among biotin enzymes.Journal of Biological Chemistry, 1988
- Evolutionary relationships among the malate dehydrogenasesTrends in Biochemical Sciences, 1988
- Evidence from Cassette Mutagenesis for a Structure-Function Motif in a Protein of Unknown StructureScience, 1988
- CLONING AND CHARACTERIZATION OF A CDNA-ENCODING HUMAN GALACTOSE-1-PHOSPHATE URIDYL TRANSFERASE1988
- Detecting homology of distantly related proteins with consensus sequencesJournal of Molecular Biology, 1987
- Homology probing: identification of cDNA clones encoding members of the protein-serine kinase family.Proceedings of the National Academy of Sciences, 1987
- Isolation and characterization of expressible cDNA clones encoding the M1 and M2 subunits of mouse ribonucleotide reductase.Molecular and Cellular Biology, 1986
- Human red cell galactose 1-phosphate uridylyltransferase: Effects of site-specific reagents on catalytic activityArchives of Biochemistry and Biophysics, 1981
- Sequence and structure of D-glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilusNature, 1977
- Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence dataNature, 1975