期刊
NUCLEIC ACIDS RESEARCH
卷 35, 期 5, 页码 1589-1600出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkl1170
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资金
- NIGMS NIH HHS [GM44844, R01 GM044844, R01 GM039422, GM39422, R37 GM039422] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM039422, R37GM039422] Funding Source: NIH RePORTER
Homing endonucleases are unusual enzymes, capable of recognizing lengthy DNA sequences and cleaving site-specifically within genomes. Many homing endonucleases are encoded within group I introns, and such enzymes promote the mobility reactions of these introns. Phage T4 has three group I introns, within the td, nr-dB and nrdD genes. The td and nrdD introns are mobile, whereas the nrdB intron is not. Phage RB3 is a close relative of T4 and has a lengthier nrdB intron. Here, we describe I-Tevill, the H-N-H endonuclease encoded by the RB3 nrdB intron. In contrast to previous reports, we demonstrate that this intron is mobile, and that this mobility is dependent on I-TevIII, which generates 2-nt 3 ' extensions. The enzyme has a distinct catalytic domain, which contains the H-N-H motif, and DNA-binding domain, which contains two zinc fingers required for interaction with the DNA substrate. Most importantly, I-Tevill, unlike the H-N-H endonucleases described so far, makes a double-strand break on the DNA homing site by acting as a dimer. Through deletion analysis, the dimerization interface was mapped to the DNA-binding domain. The unusual propensity of I-Tevill to dimerize to achieve cleavage of both DNA strands underscores the versatility of the H-N-H enzyme family.
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