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Phylogenetic analysis and amino acid sequences comparison of HO endonucleases. Phylogenetic analysis and amino acid sequences comparison of HO endonucleases.

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Presentation on theme: "Phylogenetic analysis and amino acid sequences comparison of HO endonucleases. Phylogenetic analysis and amino acid sequences comparison of HO endonucleases."— Presentation transcript:

1 Phylogenetic analysis and amino acid sequences comparison of HO endonucleases.
Phylogenetic analysis and amino acid sequences comparison of HO endonucleases. (A) Neighbor-joining (NJ) phylogeny as inferred from HO sequences depicting evolutionary relationships between Z. sapae and other hemiascomycetes. Numbers on branches indicate bootstrap support (1000 pseudoreplicates) from NJ. The Red branch indicates clusters, including ZrHO and ZsHO sequences, and the dark triangle indicates pre-WGD species. (B) Functional domains in PI-SceI and HO endonucleases. Primary amino acid alignment of S. cerevisiae PI-SceI (Sc-PI-SceI; GenBank: AA98762) and HO cloned in S. cerevisiae (Sc-HO; GenBank: CAA98806) and Z. sapae (ZsHO copy 1, GenBank: HG931720; ZsHO copy 2, GenBank: HG931721). Protein splicing domain with Hint motifs: A, Na, B, F, and G. Endonuclease domains C, D, E, and H. The DNA recognition region (DDR) and C-X2-C amino acid repeats (zinc) of putative zinc finger motifs at Sc-HO carboxyl-terminal are also shown (Bakhrat et al. 2004). In black shading are amino acid positions that are inferred to be critical for Sc-HO activity by analyzing naturally occurred or artificially induced HO mutants or by homology modeling with PI-SceI (Meiron et al. 1995; Ekino et al. 1999; Bakhrat et al. 2004; Ezov et al. 2010). In light gray, divergent positions between HO copies 1 and 2 in Z. sapae are shown. Amino acid identities are reported below the alignment following ClustalW rules: *, identity; :, conservative substitution; ., semiconservative substitution. Lisa Solieri et al. G3 2014;4: ©2014 by Genetics Society of America


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