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

Important note: Information in this article was accurate in 1996. The state of the art may have changed since the publication date.

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

RNA. 1996 Mar;2(3):264-73. Unique Identifier : AIDSLINE MED/96196014
Simons FH; Rutjes SA; van Venrooij WJ; Pruijn GJ; Department of Biochemistry, University of Nijmegen, The; Netherlands.

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.

Keywords: Animal Autoantigens/GENETICS/*PHYSIOLOGY Base Sequence Binding Sites Binding, Competitive Biological Transport Cell Nucleus/*METABOLISM Gene Products, rev/PHYSIOLOGY HIV-1 Molecular Sequence Data Mutation Nucleic Acid Conformation Oocytes Ribonucleoproteins/GENETICS/*PHYSIOLOGY RNA/CHEMISTRY/*METABOLISM RNA, Small Nuclear/METABOLISM RNA, Transfer, Met/METABOLISM Signal Peptides Support, Non-U.S. Gov't Xenopus laevis JOURNAL ARTICLE
960830
M9681216

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