Molecular cloning of a plant N-acetylserotonin methyltransferase and its expression characteristics in rice.

Abstract:

:N-acetylserotonin methyltransferase (ASMT), the last enzyme in the synthesis of melatonin, catalyzes N-acetylserotonin into melatonin. For the first time, we cloned ASMT from rice through the analysis of recombinant Escherichia coli harboring putative rice O-methyltransferase (OMT) cDNAs. In total, 18 full-length cDNAs, which show homology to wheat caffeic acid 3-O-methyltransferase, were expressed in E. coli and induced in the presence of N-acetylserotonin; we then analyzed the production of melatonin. Only recombinant E. coli line 15 showed melatonin synthesis; no other recombinant lines produced melatonin with the addition of N-acetylserotonin in E. coli culture. Line 15 clearly exhibited in vitro ASMT enzyme activity with 0.27 pkat/mg protein. ASMT enzyme activity was inhibited by various related compounds such as N-acetyltryptamine and N-acetyltyrosine. The open reading frame of ASMT consists of 364 amino acids possessing well-conserved motifs found in plant OMT such as S-adenosyl-L-methionine-binding and catalytic sites. Induction patterns of ASMT mRNA were well matched with the production of melatonin in rice leaves during senescence, as well as several stressors.

journal_name

J Pineal Res

authors

Kang K,Kong K,Park S,Natsagdorj U,Kim YS,Back K

doi

10.1111/j.1600-079X.2010.00841.x

subject

Has Abstract

pub_date

2011-04-01 00:00:00

pages

304-9

issue

3

eissn

0742-3098

issn

1600-079X

journal_volume

50

pub_type

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