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. and Landthaler, M. and 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
ISSN:	0022-2836
Publisher:	Elsevier
Volume:	342
Number:	1
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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