Identification of Ribosomal Proteins Specific to Higher Eukaryotic Organisms

Abstract

This report describes the identification of a novel protein named PS1D (Genbank TM accession number AJ272345), which is composed of an S1-like RNA-binding domain, a (cysteine)؋3-(histidine) CCCH-zinc finger, and a very basic carboxyl domain. PS1D is expressed as two isoforms, probably resulting from the alternative splicing of mRNA. The long PS1D isoform differs from the short one by the presence of 48 additional amino acids at its amino-terminal extremity. Analysis of PS1D subcellular distribution by cell fractionation reveals that this protein belongs to the core of the eukaryotic 60S ribosomal subunit. Interestingly, PS1D protein is a highly conserved protein among mammalians as murine, human, and simian PS1D homologues share more than 95% identity. In contrast, no homologous protein is found in lower eukaryotes such as yeast and Caenorhabditis elegans. These observations indicate that PS1D is the first eukaryotic ribosomal protein that is specific to higher eukaryotes.

Identification and expression analysis of genes associated with the early berry development in the seedless grapevine (Vitis vinifera L.) cultivar Sultanine

“…It codes for a putative S1-like ribosomal protein that, in conjunction with rRNA molecules, make up ribosomal subunits involved in the cellular process of translation. They are also described to be responsible for the stabilization of highly compact rRNA structures by filling the gaps between RNA domains [31]. Our observations that VvFS41 and VvUBP1 are mostly expressed during DS0 and DS2 (Fig.…”

ZCCHC17 is a master regulator of synaptic gene expression in Alzheimer’s disease

“…Pre-mRNA synthesis and splicing are increasingly recognized as occurring in tandem (Saldi et al, 2016), and a possible coordinating role for ZCCHC17 could lead to disruptions in both processes. In addition to ZCCHC17's nuclear role, early work also found that cytoplasmic ZCCHC17 cofractionates with ribosomes (Gueydan et al, 2002). This led some to initially propose that ZCCHC17 was part of the ribosome complex (Gueydan et al, 2002).…”

“…ZCCHC17 is a poorly understood protein that has been shown to interact with transcription factors (Chang et al, 2003;Joo et al, 2010) as well as splicing factors (Lin et al, 2017;Ouyang, 2009). ZCCHC17 contains a zinc-finger (CCHC) domain and a nuclear localization signal, and microscopy has localized ZCCHC17 to the nucleus and nucleolus (Chang et al, 2003;Gueydan et al, 2002;Lin et al, 2017;Ouyang, 2009). Although there is no published experimental study of ZCCHC17 protein in brain tissue, a recent metaanalysis of RNA expression data from six previous gene expression studies of AD brain tissue included ZCCHC17 as one of the top 30 most reliably downregulated genes in AD (Li et al, 2015).…”

SRrp37, a novel splicing regulator located in the nuclear speckles and nucleoli, interacts with SC35 and modulates alternative pre‐mRNA splicing in vivo

“…4k) when pNO40 was overexpressed in CV1 cells. Upon overexpression, pNO40, a core component of 60S ribosome subunit [Gueydan et al, 2002;Chang et al, 2003], was concentrated in nucleoli ( Fig. 4j) and induced marked SRrp37 nucleolar co-localization (arrows in Fig.…”

“…In general, no specific NoLSs have been described, but likely, a long array of basic amino acid flanked by basic amino acids, RXXR motifs (in which the X is preferably an arginine or leucine), or RGG motifs, may act as NoLS [Quaye et al, 1996;Liu et al, 1997;Das et al, 1998]. Many ribosomal proteins that transit to the nucleolus to be assembled with rRNA contain such a signal for nucleolar localization [Gueydan et al, 2002], and it should be noted that SRrp37 NoLS contains two such motifs (Fig. 2B) that might mediate SRrp37 nucleolar translocation.…”