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Methylation of the ribosyl moiety at position 34 of selenocysteine tRNA([Ser]Sec) is governed by both primary and tertiary structure

 Lark Kyun Kim  ;  Tamiko Matsufuji  ;  Senya Matsufuji  ;  Bradley A. Carlson  ;  Sukwon S. Kim  ;  Dolph L. Hatfield  ;  Byeong Jae Lee 
 RNA, Vol.6(9) : 1306-1315, 2000 
Journal Title
Issue Date
Animals ; Female ; Humans ; Methylation ; Mutation ; Nucleic Acid Conformation ; Oocytes ; RNA, Transfer, Amino Acyl/chemistry* ; RNA, Transfer, Amino Acyl/genetics ; RNA, Transfer, Amino Acyl/metabolism ; Ribose/metabolism ; Transfection ; Xenopus laevis
1-methyladenine ; 29-O-ribose methylation ; 5-methylcarboxymethyluridine ; 5-methylcarboxymethyluridine-29-O-methylribose ; N6-isopentenyladenosine ; pseudouridine ; selenocysteine ; tRNA modification
The selenocysteine (Sec) tRNA[Ser]Sec population in higher vertebrates consists of two major isoacceptors that differ from each other by a single nucleoside modification in the wobble position of the anticodon (position 34). One isoacceptor contains 5-methylcarboxymethyluridine (mcmU) in this position, whereas the other contains 5-methylcarboxymethyluridine-2'-O-methylribose (mcmUm). The other modifications in these tRNAs are N6-isopentenyladenosine (i6A), pseudouridine (psi), and 1-methyladenosine (m1A) at positions 37, 55, and 58, respectively. As methylation of the ribose at position 34 is influenced by the intracellular selenium status and the presence of this methyl group dramatically alters tertiary structure, we investigated the effect of the modifications at other positions as well as tertiary structure on its formation. Mutations were introduced within a synthetic gene encoded in an expression vector, transcripts generated and microinjected into Xenopus oocytes, and the resulting tRNA products analyzed for the presence of modified bases. The results suggest that efficient methylation of mcmU to yield mcmUm requires the prior formation of each modified base and an intact tertiary structure, whereas formation of modified bases at other positions, including mcmU, is not as stringently connected to precise primary and tertiary structure. These results, along with the observations that methylation of mcmU is enhanced in the presence of selenium and that this methyl group affects tertiary structure, further suggest that the mcmUm isoacceptor must have a role in selenoprotein synthesis different from that of the mcmU isoacceptor.
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1. College of Medicine (의과대학) > BioMedical Science Institute (의생명과학부) > 1. Journal Papers
Yonsei Authors
Kim, Lark Kyun(김락균) ORCID logo https://orcid.org/0000-0001-5983-4470
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