Nucleic Acids Research, Vol 25, Issue 15 3088-3094, Copyright © 1997 by Oxford University Press
G Pont-Kingdon, E Chi, S Christensen and D Carroll
The Tx1L elements constitute a family of site-specific non-LTR
retrotransposons found in the genome of the frog Xenopus laevis . The
elements have two open reading frames (ORFs) with homology to proteins of
retroviruses and other retroelements. This study demonstrates an expected
activity of one of the element-encoded proteins. The RNA binding properties
of ORF1p, the product of the first ORF of Tx1L, were examined after
expression from RNA injected into Xenopus oocytes. Using sucrose gradient
sedimentation and non-denaturing gel electrophoresis, we show that ORF1p
associates with RNA in cytoplasmic ribonucleoprotein (RNP) particles.
Discrete RNPs are formed with well-defined mobilities. The ORF1p RNPs are
distinct from endogenous RNPs that contain stored oocyte mRNAs and two
specific endogenous mRNAs do not become associated with ORF1p. ORF1p
appears to be capable of associating with its own mRNA and with other
injected RNAs, independent of specific recognition sequences. Although
nuclear localization of ORF1p was anticipated, based both on the supposed
mechanism of transposition and on the presence of a potential nuclear
localization signal, no significant fraction of the protein was found in
the oocyte nucleus. Nonetheless, the RNA binding capability of ORF1p is
consistent with the proposed model for transposition of non-LTR
retrotransposons.
ARTICLES
Ribonucleoprotein formation by the ORF1 protein of the non-LTR retrotransposon Tx1L in Xenopus oocytes
Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84132, USA. genevieve.kingdon@genetics.utah.edu
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