Identification of the magnesium, europium and lead binding sites in E. coli and lupine tRNAPhe by specific metal ion‐induced cleavages

• Published in: FEBS letters 1989-01, Vol.243 (2), p.293-298
• Main Authors: Marciniec, Tadeusz, Ciesiołka, Jerzy, Wrzesinski, Jan, Krzyżosiak, Włodzimierz J.
• Format: Article
• Language: English
• Subjects: Base Sequence; Binding Sites - drug effects; Escherichia coli - metabolism; Europium - metabolism; Fabaceae - metabolism; Hydrolysis; Lead - metabolism; Magnesium - metabolism; Metal-binding site; Metals - metabolism; Metals - pharmacology; Molecular Sequence Data; ms2i6A, 2-methylthio-N 6-(Δ2-isopentenyl)adenosine; Nucleic Acid Conformation; o2yW, α-(carboxyamino)-4,9-dihydro-β-hydroperoxy-4,6-dimethyl-9-oxo-1H-imidazolo[1,2-α]purine-7-butyric acid dimethyl ester; Plants, Medicinal; RNA, Transfer, Amino Acid-Specific - metabolism; RNA, Transfer, Phe - metabolism; Saccharomyces cerevisiae - metabolism; tRNA cleavage; tRNAPhe; Y-base, α-(carboxyamino)-4,9-dihydro-4,6-dimethyl-9-oxo-1H-imidazolo[1,2-α]purine-7-butyric acid dimethyl ester
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(89)80148-6

The Pb, Eu and Mg‐induced cleavages in E. coli and lupine tRNAPhe have been characterized and compared with those found in yeast tRNAPhe. The pattern of lupine tRNAPhe hydrolysis closely resembles that of yeast tRNAPhe, while several major differences occur in the specificity and efficiency of the E. coli tRNAPhe hydrolysis. The latter tRNA is cleaved with much lower yield in the D‐loop, and interestingly, cleavage is also detected in the variable region, that is highly resistant to hydrolysis in eukaryotic tRNAs. The possible location of tight Pb, Eu and Mg binding sites in E. coli tRNAPhe is discussed on the basis of the specific hydrolysis data.