Ro ribonucleoprotein assembly in vitro

Slobbe, Rob; Pluk, W.; Venrooij, Walther J. van; Pruijn, Ger J. M.

doi:10.1016/0022-2836(92)90890-v

Cited by 93 publications

(10 citation statements)

References 31 publications

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“…In humans, the Ro60 gene is approximately 32 kb in size, located on chromosome 19, while the Ro52 gene is 8.8 kb in size, located on chromosome 11. Although the Ro52 protein was initially suggested to be part of the Ro-hY-RNA complex with Ro60 [49, 52, 53], subsequent studies failed to confirm a direct interaction of the proteins [54, 55]. Recent studies provided evidence that Ro52 and Ro60 are localized to different cell compartments and that anti-Ro52 and anti-Ro60 antibodies have different clinical associations [15].…”

Section: Two Autoantigens To Ssa Autoantibodies Ro52 and Ro60mentioning

confidence: 99%

Clinical and Pathological Roles of Ro/SSA Autoantibody System

Yoshimi

Ueda

Ozato³

et al. 2012

Clinical and Developmental Immunology

114

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Anti-Ro/SSA antibodies are among the most frequently detected autoantibodies against extractable nuclear antigens and have been associated with systemic lupus erythematosus (SLE) and Sjögren's syndrome (SS). Although the presence of these autoantibodies is one of the criteria for the diagnosis and classification of SS, they are also sometimes seen in other systemic autoimmune diseases. In the last few decades, the knowledge of the prevalence of anti-Ro/SSA antibodies in various autoimmune diseases and symptoms has been expanded, and the clinical importance of these antibodies is increasing. Nonetheless, the pathological role of the antibodies is still poorly understood. In this paper, we summarize the milestones of the anti-Ro/SSA autoantibody system and provide new insights into the association between the autoantibodies and the pathogenesis of autoimmune diseases.

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Section: Two Autoantigens To Ssa Autoantibodies Ro52 and Ro60mentioning

confidence: 99%

Clinical and Pathological Roles of Ro/SSA Autoantibody System

Yoshimi

Ueda

Ozato³

et al. 2012

Clinical and Developmental Immunology

114

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“…Presently, it is unclear whether Par-2 and other proteins with the conserved cysteine-rich motifbind to nucleic acids. Evidence on individual members of this class has led to predictions of DNA binding (23,25), RNA binding (24,31), and proteinprotein interactions (30,32 (27); RAD18 (25); consensus sequence (27) …”

mentioning

confidence: 99%

par-2, a gene required for blastomere asymmetry in Caenorhabditis elegans, encodes zinc-finger and ATP-binding motifs.

Levitan

Boyd

Mello

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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The par-2 gene of Caenorhabditi elgans functions in early embryogenesis to ensure an amme first cleavage and the segregation of cytoplasmic factors. Both processes appear to be required to generate daughter blastomeres with distinct developmental potential. We isolated an allele of par-2 by using a screen for maternal-effect lethal mutations in a strain known for its high frequency of transposition events. A transposable lement was found to be linked to this allele. Sequences lanig the site oftransposon insertion were cloned and found to rescue the par-2 mutant phenotype. DNA In the par-2 region hybridized to a 2.3-kb germ-liueenriched mRNA. The cDNA corresponding to this germ-lineenriched message was cloned, sequenced, and used to identify the molecular lesions associated with three par-2 alleles. Sequence analysis of the par-2 cDNA revealed that the predicted protein contained two distinct motifs found in other known proteins: an ATP-binding site and a cystelue-rich motif which identifies thepar-2 gene product as a member of a growing class of putative zinc-binding proteins.A class of genes has been identified that is required for the generation of asymmetry in the early embryo and whose mutant phenotype resembles the cytochalasin D-treated embryos described above (6). Mutations in any one of the five par genes (for partitioning-defective) result in embryos with defects in the pition of the first cleavage furrow, altered orientation of the spindle at the second cleavage, synchronous early cleavages, defects in P-granule localization, and altered expression of intestinal cell differentiation markers. All mutations in these five genes result in strict maternaleffect lethality; therefore maternal expression of the par genes is required during oogenesis in order to produce viable embryos.To gain further insight into the role of the par genes in cytoplasmic partitioning, molecular analysis ofthese genes is essential. As a step toward an understanding of the generation of asymmetry and cytoplasmic localization in the C. elegans embryo at the molecular level, we have isolated and sequenced the par-2 gene. 1 1 Early embryogenesis in the nematode Caenorhabditis elegans is characterized by a series of asymmetric cleavages. The initial asymmetry of the early embryo becomes apparent during the first cell cycle, at which time cytoplasmic factors thought to be required for the specification of cell fate are segregated. The first cleavage produces a larger, anterior cell (AB) and a smaller, posterior cell (P1) which differ from each other in many respects including the orientation of subsequent cleavage planes, the timing ofcell cycles, and the kinds of differentiated cell types they ultimately produce (1). For instance, germ-line-specific P granules are uniformly dispersed in one-cell embryos but become localized to the posterior cortex midway through the first cell cycle (2). At first cleavage, nearly all of the P granules are partitioned to the P1 blastomere. Furthermore, studies of gut development (3) have shown ...

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“…The Y RNAs, which are transcribed by RNA polymerase III (13), are characterized by a conserved stem structure formed by extensive base pairing between the evolutionarily conserved 5Ј-and 3Ј-ends. In addition to Y RNAs, Ro RNPs contain at least two different proteins: the La protein and the 60-kDa Ro protein (Ro60), whereas the association of a third protein, the 52-kDa Ro protein (Ro52), is still a matter of debate (17)(18)(19)(20). The La protein binds to the oligouridylate stretch at the 3Ј-end of the Y RNAs, whereas Ro60 interacts with the most highly conserved part of the stem structure (21,22).…”

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confidence: 99%

Rapid Nucleolytic Degradation of the Small Cytoplasmic Y RNAs during Apoptosis

Rutjes¹,

Heijden²,

Utz³

et al. 1999

Journal of Biological Chemistry

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We have investigated the fate of the RNA components of small ribonucleoprotein particles in apoptotic cells. We show that the cytoplasmic Ro ribonucleoprotein-associated Y RNAs are specifically and rapidly degraded during apoptosis via a caspase-dependent mechanism. This is the first study describing the selective degradation of a specific class of small structural RNA molecules in apoptotic cells. Cleavage and subsequent truncation of Y RNAs was observed upon exposure of cells to a variety of apoptotic stimuli and were found to be inhibited by Bcl-2, zinc, and several caspase inhibitors. These results indicate that apoptotic degradation of Y RNAs is dependent on caspase activation, which suggests that the nucleolytic activity responsible for hY RNA degradation is activated downstream of the caspase cascade. The Y RNA degradation products remain bound by the Ro60 protein and in part also by the La protein, the only two proteins known to be stably associated with intact Ro ribonucleoprotein particles. The size of the Y RNA degradation products is consistent with the protection from degradation of the most highly conserved region of the Y RNAs by the bound Ro60 and La proteins. Our results indicate that the rapid abrogation of the yet unknown function of Y RNAs might be an early step in the systemic deactivation of the dying cell.Apoptosis is a form of cell death characterized by distinct morphological and biochemical alterations. Morphologically, apoptotic cells are characterized by chromatin condensation, cell shrinkage, fragmentation of the nucleus, and partition of cytoplasm and nucleus into membrane bound-vesicles (apoptotic bodies) (1). During the last 5 years, many of the molecules that participate in the biochemical pathway mediating apoptosis have been identified. A major role in this pathway is played by caspases, cysteine proteases with aspartic acid substrate specificity (2). Proteins cleaved by caspases appear to be structural proteins essential for maintaining nuclear and cytoplasmic architecture and enzymes essential for repair of damaged cell components (reviewed in Ref.3). A prominent nuclear event during apoptosis is internucleosomal cleavage of DNA, recognized as a "DNA ladder" on conventional agarose gel electrophoresis (4). The endonuclease activity responsible for apoptotic degradation of chromosomal DNA has recently been identified (5). The activity depends on two interacting proteins, one of which contains the endonuclease activity (caspase-activated deoxyribonuclease (CAD) 1 ), which is retained in the cytoplasm in an inactive form due to its association with the second protein (inhibitor of CAD). Caspase activation in apoptotic cells leads to cleavage of the inhibitor of CAD, thereby releasing active CAD resulting in DNA fragmentation in the nuclei (5, 6).Much less is known about cleavage and degradation of RNA in apoptotic cells. An increased rate of mRNA turnover has been suggested (7, 8) as well as mitochondrial 16 S ribosomal RNA degradation (9), but no nuclease associated with specif...

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Ro ribonucleoprotein assembly in vitro

Cited by 93 publications

References 31 publications

Clinical and Pathological Roles of Ro/SSA Autoantibody System

Clinical and Pathological Roles of Ro/SSA Autoantibody System

par-2, a gene required for blastomere asymmetry in Caenorhabditis elegans, encodes zinc-finger and ATP-binding motifs.

Rapid Nucleolytic Degradation of the Small Cytoplasmic Y RNAs during Apoptosis

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