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A repeated decapeptide motif in the C‐terminal domain of the ribosomal RNA methyltransferase from the erythromycin producer Saccharopolyspora erythraea
Author(s) -
Dhillon Namrita,
Leadlay Peter F.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80186-m
Subject(s) - nucleolin , ribosome biogenesis , methyltransferase , ribosomal rna , biology , biochemistry , ribosomal protein , rna , ribosome , genetics , chemistry , microbiology and biotechnology , methylation , nucleolus , dna , gene , cytoplasm
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.