Disease relevance of RNPC3

• The RNP and Sm antigens recognized by lupus erythematosus antibodies are located on discrete particles containing single small nuclear RNA's complexed with proteins [1].
• The small RNA's in ribonucleoproteins with Ro are discrete, like those associated with RNP and Sm; in contrast, ribonucleoproteins with La contain a striking highly banded spectrum of small RNA's from uninfected cells as well as virus-associated RNA from adenovirus-infected cells [1].
• 49 individuals, most of whom had systemic lupus erythematosus or Sjögren's syndrome, possessed antibodies that precipitated the previously identified RNP, Sm, Ro, and La antigens either singly or in combinations [2].
• The physical grouping of the common proteins (Sm epitopes) and the specific proteins (RNP epitopes) could result in one or the other being presented to the immune system as is the case in patients suffering from SLE or MCTD, respectively [3].
• Mechanistically, the block in virus propagation appeared to be due to retention of the viral RNP complexes in the nucleus, preventing formation of progeny virus particles [4].

Psychiatry related information on RNPC3

• RT-6, which binds H1 and Sm/RNP, expresses essentially a private Id [5].

High impact information on RNPC3

• We used antibody to the nuclear cap binding protein CBP80 or its cytoplasmic counterpart eIF4E to immunopurify RNP containing nonsense-free or nonsense-containing transcripts [6].
• Adenine recognition is primarily mediated by contacts with conserved residues found in the RNP motifs of the two RRMs [7].
• A look at messenger RNP moving through the nuclear pore [8].
• Eukaryotic nuclear telomeres: molecular fossils of the RNP world [9]?
• Endogenous protein kinase activity in nuclear RNP particles from HeLa cells [10].

Chemical compound and disease context of RNPC3

• Heterogenous nuclear RNP C1 and C2 core proteins are targets for an autoantibody found in the serum of a patient with systemic sclerosis and psoriatic arthritis [11].
• Formation of an RNP complex with poliovirus RNA was severely impaired by substitution of a lysine, highly conserved among vertebrates, with glutamine in the RNA recognition motif (RRM) of recombinant hnRNP C1, suggesting that the binding is mediated by the RRM in the protein [12].
• Sera samples of 168 patients with familial Mediterranean fever (FMF) and their 184 first degree relatives were analyzed for the presence of autoantibodies to ssDNA, dsDNA, poly (I), poly (G), cardiolipin, histones, RNP and Ro(SSA), using an enzyme linked immunosorbent assay (ELISA) [13].
• Other 'auto-immune' phenomena such as Sjogren's-like syndrome and polyarthritis were present in association with antibodies to RNP, low C4 and a null allele was demonstrated at the C4B locus [14].
• We have studied 44 sera of patients with uveitis, and controls for the presence of ANF and other antinuclear antibodies (ss-DNA, ds-DNA, Poly (I), Poly (G), RNP, Sm, histones) and for the presence of a common anti-DNA idiotype (16/6 Id) employing the ELISA method [15].

Biological context of RNPC3

• The wide variety of components that concentrate within these subdomains makes them a likely interface for multiple cellular processes, including transcription, RNA processing, transport, RNP assembly, protein modification, apoptosis and cell-cycle control [16].
• Recent insights into RNA transport have come from studies of kinetic control mechanisms and the preconditions for translocation that include processing, RNP assembly, and a targeting function for 5' caps [17].
• RNP searches the bound DNA before undergoing a conformational change that is associated with identification of its specific binding site [18].
• RNA editing in trypanosomatids is catalyzed by a high molecular mass RNP complex, which is only partially characterized [19].
• Along with previous studies on RNA-binding proteins such as Sm, RNP, Ro, and La, the present findings suggest that nucleic acid-binding proteins, as a class, may be particularly frequent targets of autoimmunity in SLE and related disorders [20].

Anatomical context of RNPC3

• The GFP location of the RNPC3 gene product shows that this protein is located in the cell nucleus [21].
• Analyses of spliceosome assembly with this substrate showed that it formed large RNP complexes that did not migrate like mature spliceosomes on native gels [22].
• Methods of extraction also caused some differences which was especially true for the rabbit thymus extract widely used for Sm and RNP studies [23].
• The discovery of DNA-binding motifs in ribosomal proteins has led to the conjecture that the transition of the ribosome from an RNA to an RNP machine occurred by adding pre-existing proteins [24].
• Careful study of the viability and permeability of irradiated keratinocytes by several techniques showed that this apparent cell membrane expression of extractable nuclear antigens (SSA/Ro, RNP, and Sm) following irradiation was seen on injured keratinocytes whose cell membranes were intact, but not on dead cells [25].

Associations of RNPC3 with chemical compounds

• Further evidence for a U4/U6 RNP particle is obtained by sedimentation studies with purified snRNPs in sucrose gradients [26].
• All of the proteins described here contain two amino-terminal RNP consensus sequence RNA-binding domains and a carboxyl-terminal glycine-rich domain [27].
• To this end, we have developed a tobramycin affinity-selection method that is generally applicable for the purification of native RNP complexes [28].
• The presence of aFIB was essential for methylation; mutant proteins having amino acid replacements in the SAM-binding motif of aFIB were able to assemble into an RNP complex, but the resulting complexes were defective in methylation activity [29].
• Sera containing other antibody specificities (i.e., anti-native DNA, cardiolipin, Sm, and nuclear RNP) failed to stain the neonatal cardiac tissue or produced alterations in membrane repolarization [30].

Analytical, diagnostic and therapeutic context of RNPC3

• Sequential immunoprecipitation with and without prior SDS treatment provided further evidence for these specificities and suggested that two classes of particles exist in different tissues, one containing proteins immunoreactive with the Sn and RNP antisera and the other containing proteins immunoreactive only with the Sm antisera [23].
• To study the structure of this particularly dynamic RNP machine that undergoes many changes in composition and conformation, single-particle cryo-electron microscopy (cryo-EM) is currently the method of choice [31].
• When tested by immunoblotting, these sera recognized up to four different protein antigens in purified mixtures of U1-U6 RNP particles [32].
• The transport of Balbiani ring (BR) premessenger RNP particles in the larval salivary gland cells of the dipteran Chironomus tentans can be followed using electron microscopy [33].
• Immunoprecipitations of nuclear extracts demonstrated the presence of the protein in heterogeneous nuclear (hn) RNP particles, but not in small nuclear RNPs, explaining the chromosomal localization of the protein [34].

References