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J. Biol. Chem., Vol. 278, Issue 47, 46826-46831, November 21, 2003

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Four Inteins and Three Group II Introns Encoded in a Bacterial Ribonucleotide Reductase Gene^*

Xiang-Qin Liu, Jing Yang, and Qing Meng

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

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-amino acid 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 amino acids apart and next to key catalytic residues of the enzyme. Protein-splicing activities of all four inteins were demonstrated in Escherichia coli. The four inteins coexist with three group II introns encoded on the first half of the same gene, which suggests a breakdown of the presumed barrier against intron insertion in this bacterial conserved protein-coding gene.

Received for publication, August 28, 2003 , and in revised form, September 12, 2003.

^* This work was supported by research grants from the National Science and Engineering Research Council of Canada and the Canadian Institute of Health Research. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 902-494-1208; Fax: 902-494-1355; E-mail: pxqliu{at}dal.ca.

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