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(Received for publication, March 12, 1997)
From New England Biolabs, Inc., Beverly, Massachusetts 01915
The protein splicing element (intein) of the
vacuolar ATPase subunit (VMA) of Saccharomyces cerevisiae
catalyzes both protein splicing and site-specific DNA cleavage. It has
been demonstrated that the conserved splice junction residues are
directly involved in protein splicing and the central dodecapeptide
motifs are required for DNA cleavage. To examine whether the splicing
activity of the intein can be structurally separated from the
endonuclease motifs, we made large in-frame deletions at the central
region of the intein. We demonstrate for the first time that protein splicing can proceed efficiently after the removal of the central region of the intein including the endonuclease motifs. Our results suggest that the N- and C-terminal regions of the Sce VMA
intein may form a separate domain that is not only catalytically
sufficient for protein splicing but also structurally independent from
the endonuclease domain.
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