A repeated decapeptide motif in the C‐terminal domain of the ribosomal RNA methyltransferase from the erythromycin producer Saccharopolyspora erythraea

FEBS Letters

Dhillon, Namrita¹  Leadlay, Peter F.¹ 

[1] Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 IQW, England

关键词: Erythromycin;    RNA-binding motif;    Nucleolin;    rRNA methyltransferase;    Resistance gene;   

DOI  :  10.1016/0014-5793(90)80186-M

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Re-analysis of the primary structure of the ribosomal RNA N-methyltransferase that confers self-resistance on the erythromycin-producing bacterium Saccharopolyspora erythraea has confirmed the presence of a C-terminal domain containing extensive repeat sequences. Nine tandem repeats can be discerned, with a decapeptide consensus sequence GGRx(H/R)GDRRT, although no single residue is wholly invariant. This highly polar, potentially flexible domain, which is predicted to adopt either a random coil or a structure with β turns, has a counterpart in the erythromycin methyltransferase of an erythromycin-producing species of Arthrobacter. It also significantly resembles a portion of the C-tenninal region of the eukaryotic protein nucleolin, which is unusually rich in dimethylarginine and glycine, and which is also predicted to behave as a random coil in solution. This resemblance, despite the very different roles of these proteins in ribosome biogenesis, strengthens the idea that in both rRNA methyltransferases and nucleolin these C-tenninal sequences might contribute to rRNA binding.

【 授权许可】

Unknown