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논문 기본 정보

자료유형
학술저널
저자정보
Yoo Bin Yoon (Chung-Ang University) Sung-Jin Cho (Chungbuk National University) Soon Cheol Park (Chung-Ang University)
저널정보
한국유전학회 Genes & Genomics Genes & Genomics Vol.43 No.3
발행연도
2021.1
수록면
295 - 301 (7page)

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Background RNA editing is a widespread phenomenon in all metazoans. One of the common RNA editing event is the chemical conversion of adenosine to inosine (A-to-I) catalyzed by adenosine deaminases acting on tRNA (ADAT). During D. melanogaster development, the ADAT1 transcript was found to localize mainly to the central nervous system including brain and ventral nerve cord during brain development. Although an earthworm adenosine deaminases acting on mRNA (ADAR) has been identified and its possible implication in earthworm regeneration has been investigated, there is little accumulated information on ADAT and tRNA editing in the annelid including terrestrial earthworms. Objective This study aimed to investigate the molecular characteristics and the expression pattern of earthworm ADAT during tail regeneration to understand its physiological significance. Methods Nucleotide sequence of Ean-ADAT was retrieved from the genome assembly of Eisenia andrei via Basic Local Alignment Search Tool (BLAST). The genome assembly of Eisenia andrei was downloaded from National Genomics Data Center (http://bigd.big.ac.cn/gwh/). The alignment and phylogenetic relationship of the core deaminase domains of ADATs and ADARs were analyzed. Its temporal expression during early tail regeneration was measured using real-time PCR. Results The open reading frame of Ean-ADAT consists of 1719 nucleotides encoding 573 amino acids. Domain analysis indicates that Ean-ADAT has a deaminase domain composed of 498 amino acids and a predicted nuclear localization signal at the N-terminal. Its subcellular localization was predicted to be nuclear. The core deaminase region of Ean-ADAT encompasses the three active-site motifs, including zinc-chelating residues and a glutamate residue for catalytic activity. In addition, Ean-ADAT shares highly conserved RNA recognition region flanking the third cysteine of the deaminase motif with other ADAT1s even from the yeast. Multiple sequence alignment and phylogenetic analysis indicate that Ean-ADAT shows greater similarity to vertebrate ADARs than to yeast Tad1p. Ean-ADAT mRNA expression began to remarkably decrease before 12 h post-amputation, showing a tendency to gradual decrease until 7 dpa and then it slightly rebounded at 10 dpa. Conclusions Our results demonstrate that Ean-ADAT belongs to a class of ADAT1s and support the hypothesis of a common evolutionary origin for ADARs and ADATs. The temporal expression of Ean-ADAT could suggest that its activity is unrelated to the molecular mechanisms of dedifferentiation.
#Earthworm · Tail regeneration · Adenosine deaminase acting on tRNA · mRNA expression

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참고문헌 (16)

참고문헌 신청
Auxilien S / 1996 / Mechanism specifcity and general properties of the yeast enzyme catalysing the formation of inosine 34 in the anticodon of transfer RNA / J Mol Biol 262:437~458 google schola Gerber AP / 1999 / An adenosine deaminase that generates inosine at the wobble position of tRNAs / Science 286:1146~1149 google schola Gerber A / 1998 / Tad1p, a yeast tRNA-specifc adenosine deaminase, is related to the mammalian pre-mRNA editing enzymes ADAR1 and ADAR2 / EMBO J 17:4780~4789 google schola Grice LF / 2015 / The origin of the ADAR gene family and animal RNA editing / BMC Evol Biol 15:4 google schola Grosjean H / 1996 / Enzymatic conversion of adenosine to inosine and to Nl-methylinosine in transfer RNAs : a review / Biochimie 78:488~501 google schola

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