Three functional luciferase domains in a single polypeptide chain
AUTOR(ES)
Li, Liming
FONTE
The National Academy of Sciences of the USA
RESUMO
We report a unique case of a gene containing three homologous and contiguous repeat sequences, each of which, after excision, cloning, and expression in Escherichia coli, is shown to code for a peptide catalyzing the same reaction as the native protein, Gonyaulax polyedra luciferase (Mr = 137). This enzyme, which catalyzes the light-emitting oxidation of a linear tetrapyrrole (dinoflagellate luciferin), exhibits no sequence similarities to other luciferases in databases. Sequence analysis also reveals an unusual evolutionary feature of this gene: synonymous substitutions are strongly constrained in the central regions of each of the repeated coding sequences.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=22980Documentos Relacionados
- Molecular evolution of dinoflagellate luciferases, enzymes with three catalytic domains in a single polypeptide
- Functional three-domain single-chain T-cell receptors.
- Is there a single pathway for the folding of a polypeptide chain?
- Functional domains are specified to single-cell resolution in a Drosophila epithelium
- EVIDENCE FOR MULTIPLE GENE CONTROL OF A SINGLE POLYPEPTIDE CHAIN: THE HEAVY CHAIN OF RABBIT IMMUNOGLOBULIN