Abstract
BackgroundThe ribosomal protein SA (RPSA), previously named 37-kDa laminin receptor precursor/67-kDa laminin receptor (LRP/LR) is a multifunctional protein that plays a role in a number of pathological processes, such as cancer and prion diseases. In all investigated species, RPSA is a member of a multicopy gene family consisting of one full length functional gene and several pseudogenes. Therefore, for studies on RPSA related pathways/pathologies, it is important to characterize the whole family and to address the possible function of the other RPSA family members. The present work aims at deciphering the RPSA family in sheep.ResultsIn addition to the full length functional ovine RPSA gene, 11 other members of this multicopy gene family, all processed pseudogenes, were identified. Comparison between the RPSA transcript and these pseudogenes shows a large variety in sequence identities ranging from 99% to 74%. Only one of the 11 pseudogenes, i.e. RPSAP7, shares the same open reading frame (ORF) of 295 amino acids with the RPSA gene, differing in only one amino acid. All members of the RPSA family were annotated by comparative mapping and fluorescence in situ hybridization (FISH) localization. Transcription was investigated in the cerebrum, cerebellum, spleen, muscle, lymph node, duodenum and blood, and transcripts were detected for 6 of the 11 pseudogenes in some of these tissues.ConclusionsIn the present work we have characterized the ovine RPSA family. Our results have revealed the existence of 11 ovine RPSA pseudogenes and provide new data on their structure and sequence. Such information will facilitate molecular studies of the functional RPSA gene taking into account the existence of these pseudogenes in the design of experiments. It remains to be investigated if the transcribed members are functional as regulatory non-coding RNA or as functional proteins.
Highlights
The ribosomal protein SA (RPSA), previously named 37-kDa laminin receptor precursor/67-kDa laminin receptor (LRP/LR) is a multifunctional protein that plays a role in a number of pathological processes, such as cancer and prion diseases
bacterial artificial chromosome (BAC) screening and sequence tagged site (STS) content mapping Eight different primer pairs were designed in conserved ovine RPSA regions identified by aligning previously described mRNA and expressed sequence tag (EST) sequences, representing each exon at least once
By sequence tagged site (STS) content mapping, performed with 54 unique STS primer pairs that were designed from the 68 BAC end sequences (BES) [GenBank:GS375851-GS375918], 6 mini-contigs could be constructed and another 6 single BAC clones could be identified, each containing a different family member of the ovine RPSA family (Figure 1 and 2; Additional file 2)
Summary
The ribosomal protein SA (RPSA), previously named 37-kDa laminin receptor precursor/67-kDa laminin receptor (LRP/LR) is a multifunctional protein that plays a role in a number of pathological processes, such as cancer and prion diseases. The ribosomal protein SA (RPSA), previously named 37-kDa laminin receptor precursor/67-kDa laminin receptor (LRP/LR) is a multifunctional protein In the nucleus it binds to DNA via the histones H2A, H2B and H4 [1], in the cytoplasm it is associated with the 40S ribosomal subunit [2], and at the cell surface it acts as a receptor for a number of components i.e. laminin, elastin, the green tea catechin epigallocatechin-3-gallate (EGCG), carbohydrates, the prion protein, different viruses like Dengue virus, Sindbis virus, Venezuelean Equine Encephalitis virus and Adeno-associated-viruses. Several therapeutic approaches based on down-regulation (e.g. via RNA interference) and/or blocking (e.g. with specific antibodies or transdominant negative mutants) of the receptor result in reduced adhesion, migration and invasion of tumour cells [4,5,6,7], and reduced accumulation of the pathogenic isoform of the prion protein in many organs involved in the pathogenesis of transmissible spongiform encephalopathies [8,9,10,11,12], leading to a significant prolongation of the pre-clinical phase or survival time after the occurrence of the first symptoms [10,11,12].
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