BMC Evolutionary Biology

official impact factor 3.70

Open Access Research article

Intron-loss evolution of hatching enzyme genes in Teleostei

Mari Kawaguchi1,2, Junya Hiroi3, Masaki Miya4, Mutsumi Nishida1, Ichiro Iuchi5 and Shigeki Yasumasu5*

Author Affiliations

1 Atmosphere and Ocean Research Institute, The University of Tokyo, 5-1-5 Kashiwanoha, Kashiwa, Chiba 277-8564, Japan

2 Research Fellow of the Japan Society for the Promotion of Science (JSPS), Japan

3 Department of Anatomy, St. Marianna University School of Medicine, 2-16-1 Sugao, Miyamae-ku, Kawasaki 216-8511, Japan

4 Department of Zoology, Natural History Museum & Institute, Chiba, 955-2 Aoba-cho, Chuo-ku, Chiba 260-8682, Japan

5 Department of Materials and Life Sciences, Faculty of Science and Technology, Sophia University, 7-1 Kioi-cho, Chiyoda-ku, Tokyo 102-8554, Japan

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BMC Evolutionary Biology 2010, 10:260 doi:10.1186/1471-2148-10-260

Published: 27 August 2010

Additional files

Additional file 1:

Teleostean species examined in this study and the names of hatching enzyme genes

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Additional file 2:

A multiple alignment of amino acid sequences deduced from teleostean hatching enzyme genes. All hatching enzymes were composed of a signal sequence (putative cleavage sites are shown as white triangle), a pro-sequence, and a mature enzyme sequence (the N-terminals are shown as black triangle). The mature enzyme portion possesses two active site consensus sequences for astacin family metallo-proteases, HExxHxxGFxHExxRxDR (Zn-binding site, indicated in dark gray) and SxMHY (methionine turn, indicated in light gray). In addition, six conserved cysteine residues are shaded in black. Red lines indicate the intron insertion sites. Identical residues are boxed. Dashes, asterisks and "X"s represent gaps, stop codons and unidentified amino acid residues, respectively. Arrows at the bottom indicate sites of primers designed for amplification of hatching enzyme gene fragments.

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