Structural analysis of plant ribosomal 5S RNAs. Visualisation of novel tertiary interactions by cleavage of lupin and wheat 5SrRNAs with ribonuclease H

• Published in: Biochimica et biophysica acta Vol. 1087; no. 1; pp. 68 - 72
• Main Authors: Barciszewska, Mirosława Z., Lorenz, Siegfried, Erdmann, Volker A., Barciszewski, Jan
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 10.09.1990
• Subjects: Base Sequence; Endoribonucleases; Fabaceae - genetics; Hydrogen Bonding; interactions; Lupin; lupins; Models, Molecular; Molecular Sequence Data; Nucleic Acid Conformation; Oligonucleotides; Plants, Medicinal; protein tertiary structure; Ribonuclease H; ribonucleases; ribosomes; RNA; RNA structure; RNA, Ribosomal; RNA, Ribosomal, 5S; rRNA, 5S; Seeds - genetics; Synthetic oligodeoxyribonucleotide; Triticum - genetics; Wheat germ; Ribonuclease H; Lupin; Wheat germ; rRNA, 5S; Synthetic oligodeoxyribonucleotide; RNA structure
• ISSN: 0167-4781; 0006-3002; 1879-2634
• DOI: 10.1016/0167-4781(90)90122-I

A model for the tertiary structure of plant 5S rRNA, previously proposed by our laboratory (Joachimiak, A. et al. (1990) Int. J. Biol. Macromol., in press) was tested by specific cleavage of the plant 5S rRNA in the presence of synthetic oligodeoxynucleotides. The hexanucleotides used in this study were complementary to different portions of loops C, D and E, the nucleotides of which have recently been proposed to be involved in tertiary hydrogen bonds. The results obtained strongly support the interaction of loops C and D by nucelotides C34, C35, C36, A37 and G85, G86, G87, U88, respectively. Digestion pattern of loop E (domain gamma, nucleotides 66–110) suggests a possible different arrangement of this part of the plant 5S rRNA molecule, when compared with other eukaryotes.