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Protein Science, Vol 6, Issue 12 2677-2680, Copyright © 1997 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

Crystallization and preliminary X-ray studies of I-PpoI: A nuclear, intron-encoded homing endonuclease from Physarum polycephalum

K. E. FLICK, D. McHUGH, J. D. HEATH, K. M. STEPHENS, R. J. MONNAT-JR. and B. L. STODDARD
Fred Hutchinson Cancer Research Center, 1124 Columbia St. A3-023, Seattle, Washington 98104

The homing endonuclease I-PpoI is encoded by an optional third intron, Pp LSU 3, found in nuclear, extrachromosomal copies of the Physarum polycephalum 26S rRNA gene. This endonuclease promotes the lateral transfer or ``homing'' of its encoding intron by recognizing and cleaving a partially symmetric, 15 bp homing site in 26S rDNA alleles that lack the Pp LSU 3 intron. The open reading frame encoding I-PpoI has been subcloned, and the endonuclease has been overproduced in E. coli. Purified recombinant I-PpoI has been co-crystallized with a 21 bp homing site DNA duplex. The crystals belong to space group P3(1)21, with unit cell dimensions a = b = 114 A, c = 89 A. The results of initial X-ray diffraction experiments indicate that the asymmetric unit contains an enzyme homodimer and one duplex DNA molecule, and that the unit cell has a specific volume of 3.4 A(3)/dalton. These experiments also provide strong evidence that I-PpoI contains several bound zinc ions as part of its structure.
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