Non-participation of opal suppressor phosphoseryl-transfer ribonucleic acid(tRNA) in phosphoserine aminotransferase catalysis.

Mizutani, Takaharu; Kanbe, K; Kimura, Yukiko; Tachibana, Yoshio; Hitaka, Teruaki

doi:10.1248/cpb.36.824

Cited by 6 publications

(1 citation statement)

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“…The peak of phosphoseryl-tRNA was collected by ethanol precipitation and hydrolyzed with 0.1 M NH40H. The hydrolyzate was mixed with authentic phosphoserine and then analyzed on an AC-1 column according to Mizutani et al [14]. 47-49.…”

Section: Methodsmentioning

confidence: 99%

The detection of natural opal suppressor seryl‐tRNA in Escherichia coli by the dot blot hybridization and its phosphorylation by a tRNA kinase

et al. 1989

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It was believed that there was no natural suppressor tRNA in Escherichiu coli, however, it has been suggested that selC', relating to the synthesis of formate dehydrogenase of a selenoprotein [(1988) Nature 331, 723-7251, codes for tRNA, even though the presence of tRNA has not yet been demonstrated. We detected the product of se/C in the tRNA preparation of the E. cofi MC 4100 strain by the dot blot hybridization method with a DNA probe (ACCGCTGGCGGC) corresponding to the extra arm of sefC tRNA. Two hybridization peaks were found in the chromatographic pattern from Sephadex ASO. The amount of tRNA was estimated to be about 0.03% of the total tRNA. The suppressor PH]seryl-tRNA was phosphorylated by a tRNA kinase in E. co/i B. These results suggest that the opal suppressor seryl-tRNA in E. coli should be converted to selenocysteyl-tRNA through phosphoseryl-tRNA, and occurs in vertebrates as a general phenomenon Suppressor tRNA; Formate dehydrogenase; Selenocysteine; Opal termination codon; tRNA, phosphoseryl-

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Section: Methodsmentioning

confidence: 99%