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A more recent version of this article appeared on November 21, 2003
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Papers In Press, published online ahead of print September 15, 2003
J. Biol. Chem, 10.1074/jbc.M309575200
Submitted on August 28, 2003
Revised on September 12, 2003
Accepted on September 15, 2003

Four inteins and three group II introns encoded in a bacterial ribonucleotide reductase gene

Xiang-Qin Liu, Jing Yang, and Qing Meng

Department of Biochemistry and Molecular Biology, Dalhousie University, Halifax, Nova Scotia B3H 4H7

Corresponding Author: pxqliu{at}dal.ca

A bacterial ribonucleotide reductase gene was found to encode four inteins and three group II introns in the oceanic N2-fixing cyanobacterium Trichodesmium erythraeum. The 13,650-bp ribonucleotide reductase gene is divided into eight extein- or exon-coding sequences that together encode a 768-aa mature ribonucleotide reductase protein, with 83% of the gene sequence encoding introns and inteins. The four inteins are encoded on the second half of the gene, and each has conserved sequence motifs for a protein splicing domain and an endonuclease domain. These four inteins, together with known inteins, define five intein insertion sites in ribonucleotide reductase homologues. Two of the insertion sites are 10 aa apart and next to key catalytic residues of the enzyme. Protein splicing activities of all four inteins were demonstrated in E. coli. The four inteins coexist with three group II introns encoded on the second half of the same gene, which suggests a breakdown of the presumed barrier against intron insertion in this bacterial conserved protein-coding gene.


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