Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-18500
RNA 1996 Mar 01;23:264-73.
Show Gene links Show Anatomy links

The interactions with Ro60 and La differentially affect nuclear export of hY1 RNA.

Simons FH , Rutjes SA , van Venrooij WJ , Pruijn GJ .


???displayArticle.abstract???
Ro RNPs are evolutionarily conserved ribonucleoprotein particles that consist of a small RNA, known as Y RNA, associated with several proteins, such as La, Ro60, and Ro52. The Y RNAs (Y1-Y5), which are transcribed by RNA polymerase III, have been shown to reside almost exclusively in the cytoplasm as Ro RNPs. To obtain more insight into the nuclear export pathway of Y RNAs, hY1 RNA export was studied in Xenopus laevis oocytes. Injection of various hY1 RNA mutants showed that an intact Ro60 binding site is a prerequisite for nuclear export, whereas the presence of an intact La binding site resulted in strong nuclear retention of hY1 RNA. Competition studies with various classes of RNAs indicated that, in addition to Ro60, another titratable factor was necessary for nuclear export of hY1 RNA. This factor appears also to be involved in nuclear export of tRNA. Because export of hY1 RNA could not be blocked by a synthetic peptide containing the recently identified nuclear export signal of the HIV-1 Rev protein, nuclear export of hY1 RNA does not seem to be dependent on a Rev-like nuclear export signal.

???displayArticle.pubmedLink??? 8608450
???displayArticle.pmcLink??? PMC1369369
???displayArticle.link??? RNA


Species referenced: Xenopus laevis
Genes referenced: mt-tr ro60 trna

References [+] :
Boelens, Nuclear retention of RNA as a mechanism for localization. 1995, Pubmed, Xenbase