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

Abstract：

: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 beta turns, has a counterpart in the erythromycin methyltransferase of an erythromycin-producing species of Arthrobacter. It also significantly resembles a portion of the C-terminal 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-terminal sequences might contribute to rRNA binding.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Dhillon N,Leadlay PF

doi

10.1016/0014-5793(90)80186-m

subject

Has Abstract

pub_date

1990-03-26 00:00:00

pages

189-93

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(90)80186-M

journal_volume

262

pub_type

杂志文章

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