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Nucleic Acids Research, 2001, Vol. 29, No. 21 4310-4318
© 2001 Oxford University Press

Identification of the first eubacterial endonuclease coded by an intein allele in the pps1 gene of mycobacteria

Isabelle Saves1,*, Fabrice Westrelin1, Mamadou Daffé1 and Jean-Michel Masson1,2

1Institut de Pharmacologie et Biologie Structurale (UMR5089), CNRS/Université Paul Sabatier Toulouse III, 205 Route de Narbonne, F-31077 Toulouse Cedex, France and 2Institut National des Sciences Appliquées, Complexe Scientifique de Rangueil, F-31077 Toulouse Cedex, France

A survey of a vast range of mycobacterial strains led us to discover a new Pps1 intein allele in Mycobacterium gastri which differs from those of Mycobacterium tuberculosis and Mycobacterium leprae in both its sequence and insertion site. While little is known about Pps1, except that it belongs to the YC24 family of ABC transporters, we show that, unlike the other inteins described so far from Eubacteria, the MgaPps1 intein possesses a specific endonuclease activity. The intein is the first eubacterial intein to be characterised as an endonuclease. Like other intein endonucleases, its minimal sequence for recognition and cleavage is quite large, with 22 bp spanning the Pps1-c site. The fact that an active endonuclease is found among the mycobacterial inteins supports the concept of a cyclical model of invasion by horizontal transfer of these genes, followed by degeneration and loss until a new invasion event, thus explaining their long-term persistence in closely related eubacterial species.

* To whom correspondence should be addressed. Tel: +33 561 175 471; Fax: +33 561 175 994; Email: saves{at}ipbs.fr


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