Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 60, Issue 10, Pages 2219-2227Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00018-003-3235-0
Keywords
RNA export; KH protein; KH domain; RNA transport; polyribosomes; microsome
Categories
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available