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Molecular interactions of human Exo1 with DNA
Byung-in Lee, Lam H. Nguyen, Daniel Barsky, Mike Fernandes, and David M. Wilson III
- Figure S1 Amino acid sequence alignment of the Rad2 domain of Exo1 and Fen1 from selected organisms. Included are the E. coli 5' to 3' exonuclease domain of DNA polymerase I and bacteriophage T5 5' to 3' exonuclease. The human Exo1 N-terminal fragment (Hs_Nterm) is Hex1-N2 (391 residues in length). The "*" indicates the invariant residues, ":" indicates positions that are "strongly" conserved and "." positions that are "weakly" conserved. The "0" marks the invariant residues examined by site-directed mutagenesis here. The running histogram in grey is a visual guide to the level of conservation, and the amino acid numbering of each protein is indicated at the end of each row. This alignment and representation was generated with ClustalX (v. 1.81) [Thompson, JD, Gibson, TJ, Plewniak, F, Jeanmougin, F and Higgins, DG (1997) The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Research, 24: 4876-4882] with the default parameters (Gap opening=10, gap ext.= 0.2, Gonnet weight matrices, etc.).
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