Molecular evolution of patristacin genes in teleosts based on the genome survey

Author:

Nakano Yuko12,Nagasawa Tatsuki3,Okazawa Yohei1,Mashiko Naoya1,Yasumasu Shigeki1,Kawaguchi Mari1ORCID

Affiliation:

1. Department of Materials and Life Sciences, Faculty of Science and Technology Sophia University Tokyo Japan

2. Department of Biochemistry and Molecular Biology Thomas Jefferson University Philadelphia Pennsylvania USA

3. Department of Life Science and Technology Tokyo Institute of Technology Tokyo Japan

Abstract

AbstractDuring the evolution of astacin metalloprotease family genes, gene duplication occurred, especially in the lineage of teleosts, in which several types of astacins containing six conserved cysteines (c6ast) emerged. One of them is patristacin, originally found in syngnathid fishes, such as pipefishes and seahorses. Patristacin is expressed in the brood pouch and is present on the same chromosome as other c6ast (pactacin and nephrosin) genes. We first surveyed all the genes from 33 teleost species using a genome database, and characterized the genes by phylogenetic analysis. Pactacin and nephrosin gene homologs were found from all the examined species with only few exceptions, while patristacin gene homologs were found from only several lineages. The patristacin gene homologs were found as multicopy genes in most species of Percomorpha, one of the diverged groups in teleosts. Further diversification of the gene occurred during the evolution of Atherinomorphae, one of the groups in Percomorpha. Fishes of Atherinomorphae possess two types of patristacin, belonging to subclades 1 and 2. Among the Atherinomorpha, we chose the southern platyfish to examine the patristacin gene expression. Platyfish possess eight patristacin gene homologs, called XmPastn1, 2, 3, 4, 5, 7, 10, and 11. Of these genes, only XmPastn2 belongs to subclade 1, while the other seven belong to subclade 2. Only XmPastn2 showed strong expression in several organs of adult platyfish, as observed in reverse‐transcription polymerase chain reaction of RNA extracts. Cells expressing XmPastn2 were predominantly mucus‐secreting cells found in epidermis around the jaw, as revealed by in‐situ hybridization. This result suggests that XmPastn2 is secreted and may contribute to mucus formation or secretion.

Publisher

Wiley

Subject

Developmental Biology,Genetics,Animal Science and Zoology,Molecular Medicine,Ecology, Evolution, Behavior and Systematics

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