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DNA binding and cleavage by the HNH homing endonuclease I-HmuI

Item Type:Article
Title:DNA binding and cleavage by the HNH homing endonuclease I-HmuI
Creators Name:Shen, B.W., Landthaler, M., Shub, D.A. and Stoddard, B.L.
Abstract:The structure of I-HmuI, which represents the last family of homing endonucleases without a defining crystallographic structure, has been determined in complex with its DNA target. A series of diverse protein structural domains and motifs, contacting sequential stretches of nucleotide bases, are distributed along the DNA target. I-HmuI contains an N-terminal domain with a DNA-binding surface found in the I-PpoI homing endonuclease and an associated HNH/N active site found in the bacterial colicins, and a C-terminal DNA-binding domain previously observed in the I-TevI homing endonuclease. The combination and exchange of these features between protein families indicates that the genetic mobility associated with homing endonucleases extends to the level of independent structural domains. I-HmuI provides an unambiguous structural connection between the His-Cys box endonucleases and the bacterial colicins, supporting the hypothesis that these enzymes diverged from a common ancestral nuclease.
Keywords:Homing Endonuclease, DNA-Binding Protein, Crystal Structure, Nuclease Mechanism
Source:Journal of Molecular Biology
Page Range:43-56
Date:3 September 2004
Official Publication:https://doi.org/10.1016/j.jmb.2004.07.032
PubMed:View item in PubMed

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