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The multi-KH protein vigilin associates with free and membrane-bound ribosomes.

Authors
  • Kruse, C
  • Willkomm, D
  • Gebken, J
  • Schuh, A
  • Stossberg, H
  • Vollbrandt, T
  • Müller, P K
Type
Published Article
Journal
Cellular and molecular life sciences : CMLS
Publication Date
Oct 01, 2003
Volume
60
Issue
10
Pages
2219–2227
Identifiers
PMID: 14618268
Source
Medline
License
Unknown

Abstract

The-multi-KH domain protein vigilin has been identified by ex vivo experiments as both a tRNA- and/or mRNA-binding protein. We show here that in vitro under conditions previously shown to allow tRNA binding, recombinant vigilin also binds to selected mRNA species and ribosomal RNA. An in vivo link of vigilin to mRNA and rRNA was elucidated by several approaches. (i) Coexpression/costimulation of vigilin was found with many other proteins independently of whether their mRNA was translated on free or membrane-bound ribosomes. (ii) A close codistribution of vigilin with free ribosomes was seen in the cytoplasm while nucleoli were a major organelle of vigilin accumulation in the nucleus. (iii) Furthermore, free and membrane-bound ribosomes can be enriched for vigilin which suggests that this binding does not depend on the class of mRNA translated. Therefore, we suggest that vigilin does not distinguish between free or membrane-bound ribosomes but is generally necessary for the localization of mRNAs to actively translating ribosomes.

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