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The Unusually Long Amino Acid Acceptor Stem of Escherichia Coli Selenocysteine TRNA Results from Abnormal Cleavage by RNase P

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Specialty Biochemistry
Date 1988 Dec 23
PMID 3062578
Citations 15
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Abstract

The nucleotide sequence of the gene encoding the Escherichia coli selenocysteine tRNA (tRNA(SeCys] predicts an unusually long acceptor stem of 8 base pairs (one more than other tRNAs). Here we show by in vivo experiments (Northern blots, primer extension analysis) and by in vitro RNA processing studies that E. coli tRNA(SeCys) does contain this additional basepair, and that its formation results from abnormal cleavage by RNase P.

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References
1.
Gardiner K, Marsh T, Pace N, Altman S . The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme. Cell. 1983; 35(3 Pt 2):849-57. DOI: 10.1016/0092-8674(83)90117-4. View

2.
Reich C, Gardiner K, Olsen G, Pace B, Marsh T, Pace N . The RNA component of the Bacillus subtilis RNase P. Sequence, activity, and partial secondary structure. J Biol Chem. 1986; 261(17):7888-93. View

3.
Krupp G, Cherayil B, Frendewey D, Nishikawa S, Soll D . Two RNA species co-purify with RNase P from the fission yeast Schizosaccharomyces pombe. EMBO J. 1986; 5(7):1697-703. PMC: 1166996. DOI: 10.1002/j.1460-2075.1986.tb04413.x. View

4.
Orellana O, Cooley L, Soll D . The additional guanylate at the 5' terminus of Escherichia coli tRNAHis is the result of unusual processing by RNase P. Mol Cell Biol. 1986; 6(2):525-9. PMC: 367542. DOI: 10.1128/mcb.6.2.525-529.1986. View

5.
Zinoni F, Birkmann A, Leinfelder W, Bock A . Cotranslational insertion of selenocysteine into formate dehydrogenase from Escherichia coli directed by a UGA codon. Proc Natl Acad Sci U S A. 1987; 84(10):3156-60. PMC: 304827. DOI: 10.1073/pnas.84.10.3156. View