title: A covariant change of the two highly conserved bases in the GTPase-associated center of 28 S rRNA in silkworms and other moths.
abstract: The GTPase-associated center in 23/28 S rRNA is one of the most conserved functional domains throughout all organisms. We detected a unique sequence of this domain in Bombyx mori species in which the bases at positions 1094 and 1098 (numbering from Escherichia coli 23 S rRNA) are C and G instead of the otherwise universally conserved bases U and A, respectively. These changes were also observed in four other species of moths, but not in organisms other than the moths. Characteristics of the B. mori rRNA domain were investigated by native polyacrylamide gel electrophoresis using RNA fragments containing residues 1030-1128. Although two bands of protein-free RNA appeared on gel, they shifted to a single band when bound to Bombyx ribosomal proteins Bm-L12 and Bm-P complex, equivalent to E. coli L11 and L8, respectively. Bombyx RNA showed lower binding capacity than rat RNA for the ribosomal proteins and anti-28 S autoantibody, specific for a folded structure of the eukaryotic GTPase-associated domain. When the C(1094)/G(1098) bases in Bombyx RNA were replaced by the conserved U/A bases, the protein-free RNA migrated as a single band, and the complex formation with Bm-L12, Bm-P complex, and anti-28 S autoantibody was comparable to that of rat RNA. The results suggest that the GTPase-associated domain of moth-type insects has a labile structural feature that is caused by an unusual covariant change of the U(1094)/A(1098) bases to C/G.
authors.affiliation: Institute of High Polymer Research and the Department of Applied Biological Science, Faculty of Textile Science and Technology, Shinshu University, Ueda 386-8567, Japan. uchimi@giptc.shinshu-u.ac.jp
authors.forename: T
authors.initials: T
authors.lastname: Uchiumi
authors.forename: T
authors.initials: T
authors.lastname: Nomura
authors.forename: T
authors.initials: T
authors.lastname: Shimizu
authors.forename: Y
authors.initials: Y
authors.lastname: Katakai
authors.forename: K
authors.initials: K
authors.lastname: Mita
authors.forename: Y
authors.initials: Y
authors.lastname: Koike
authors.forename: M
authors.initials: M
authors.lastname: Nakagaki
authors.forename: H
authors.initials: H
authors.lastname: Taira
authors.forename: A
authors.initials: A
authors.lastname: Hachimori
mesh_terms: D000818:Animals; D001323:Autoantibodies / Q000378:metabolism; D001483:Base Sequence; D012831:Bombyx; D017124:Conserved Sequence; D018076:DNA, Complementary / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism; D020558:GTP Phosphohydrolases / Q000737:chemistry / Q000378:metabolism*; D015723:Gene Library; D007313:Insecta; D008969:Molecular Sequence Data; D009036:Moths; D009690:Nucleic Acid Conformation; D010957:Plasmids / Q000378:metabolism; D012339:RNA, Ribosomal, 28S / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D051381:Rats; D012270:Ribosomes / Q000378:metabolism; D017422:Sequence Analysis, DNA
chemical_list: D001323:Autoantibodies; D018076:DNA, Complementary; D012339:RNA, Ribosomal, 28S; D020558:GTP Phosphohydrolases