Two Novel Classes of Small Ribonucleoproteins Detected by Antibodies Associated with Lupus Erythematosus

Lerner, Michael R.; Boyle, John A.; Hardin, John A.; Steitz, Joan A.

doi:10.1126/science.6164096

Cited by 522 publications

(297 citation statements)

References 29 publications

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“…The antigen precipitated by anti-RNP serum is similar to that described by others [9,15]. A major difference, however, is in the polypeptides associated with snRNP antigen.…”

Section: The M U W E Ofthe Antigensupporting

confidence: 60%

“…Complementarity between portions of the U1 RNA and concensus splice junction sequences has led to speculation that U 1 RNA might serve to align the splice joints [14]. Since one type of systemic lupus erythematosus serum, characterized as 'anti-RNP', precipitates particles containing only U1 RNA [15], introduction of such a serum might neutralize its antigen and Abbreviation. snRNP, small (10-S) nuclear ribonucleoprotein comEnzyme.…”

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confidence: 99%

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Expression of Two Late Adenovirus Genes Is Altered by Introducing Antibodies against Ribonucleoprotein into Living HeLa Cells

1982

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These experiments describe the effect on adenovirus gene expression of tranfusing liposome-encapsulated antibodies directed against a 10-S ribonucleoprotein complex into infected Hela cells. Immunoprecipitation studies demonstrate that this particular serum contains antibodies directed against particles containing U1 RNA and five polypeptides in the molecular weight range of 45 000 -60000. The procedure of fusing liposomes successfully treats nearly all the cells in culture, and the transfused material has access throughout the cell. The IgG fraction from this serum is introduced into adenovirus-infected cells shortly before the transition from the early to the late stage of the lytic cycle; 19 h after fusion the accumulated effects of the antibodies on late virus expression are examined by pulse-labeling cells with radioactive methionine and observing the synthesized proteins. While most late viral genes are expressed normally in treated cells, fiber synthesis is reduced to a very low level and hexon synthesis is reduced twofold. That most viral genes are expressed normally demonstrates that many cell activities (transcription, transport, processing and translation) are minimally affected. The effects on these two genes can be distinguished by varying the concentration of antibody transfused : interference with hexon synthesis occurs at a lower dosage than fiber. A simple interpretation of these results is that the antibody has bound to its antigen and prevented the latter from participating in its role in message processing.

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“…The antigen precipitated by anti-RNP serum is similar to that described by others [9,15]. A major difference, however, is in the polypeptides associated with snRNP antigen.…”

Section: The M U W E Ofthe Antigensupporting

confidence: 60%

mentioning

confidence: 99%

Expression of Two Late Adenovirus Genes Is Altered by Introducing Antibodies against Ribonucleoprotein into Living HeLa Cells

1982

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“…Although their sequence is diversified, their structure and association with Ro60 are conserved (Sim and Wolin 2011). In mammals, four Y RNAs (Y1, Y3, Y4, and Y5) and isoforms (e.g., the Y3-derived Y3 * * ) have been identified (Hendrick et al 1981;Lerner et al 1981;Wolin and Steitz 1983). Notably, Muroidea (mouse-like rodents) express only Y1 and Y3 but not Y3 * * (Wolin and Steitz 1983;Pruijn et al 1993).…”

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confidence: 99%

The Y3** ncRNA promotes the 3′ end processing of histone mRNAs

et al. 2015

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We demonstrate that the Y3/Y3 * * noncoding RNAs (ncRNAs) bind to the CPSF (cleavage and polyadenylation specificity factor) and that Y3 * * associates with the 3 ′ untranslated region (UTR) of histone pre-mRNAs. The depletion of Y3 * * impairs the 3 ′ end processing of histone premRNAs as well as the formation and protein dynamics of histone locus bodies (HLBs), the site of histone mRNA synthesis and processing. HLB morphology is also disturbed by knockdown of the CPSF but not the U7-snRNP components. In conclusion, we propose that the Y3 * * ncRNA promotes the 3 ′ end processing of histone pre-mRNAs by enhancing the recruitment of the CPSF to histone pre-mRNAs at HLBs.

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“…8 -10). The La protein is implicated in several aspects of the RNA metabolism, including processing of precursors of tRNAs, U3 snoRNA, U1 RNA, U6 snRNA (11)(12)(13)(14)(15)(16)(17)(18)(19)(20), and stabilization of viral (21-23) as well as cellular RNAs (24). In the cytoplasm, La has been implicated in the translational control of viral (25-27) and cellular RNAs (28 -30).…”

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confidence: 99%

Nuclear Trafficking of La Protein Depends on a Newly Identified Nucleolar Localization Signal and the Ability to Bind RNA

Horke

Reumann

Schweizer

et al. 2004

Journal of Biological Chemistry

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Here we provide evidence for an interaction-dependent subnuclear trafficking of the human La (hLa) protein, known as transient interaction partner of a variety of RNAs. Among these, precursor transcripts of certain RNAs are located in the nucleoplasm or nucleolus. Here we examined which functional domains of hLa are involved in its nuclear trafficking. By using green fluorescent-hLa fusion proteins, we discovered a nucleolar localization signal and demonstrated its functionality in a heterologous context. In addition, we revealed that the RRM2 motif of hLa is essential both for its RNA binding competence in vitro and in vivo and its exit from the nucleolus. Our data imply that hLa traffics between different subnuclear compartments, which depend decisively on a functional nucleolar localization signal as well as on RNA binding. Directed trafficking of hLa is fully consistent with its function in the maturation of precursor RNAs located in different subnuclear compartments.The human La protein (hLa) 1 is a 47-kDa phosphoprotein predominantly localized in the nucleus. It was first discovered as an autoantigen recognized by antibodies present in the sera of patients suffering from systemic lupus erythematosus and Sjogren's syndrome (1, 2). The La protein is a member of a large group of RNA-binding proteins containing RNA recognition motifs (RRMs) (3-7) and interacts with a variety of small RNAs (for reviews see Refs. 8 -10). The La protein is implicated in several aspects of the RNA metabolism, including processing of precursors of tRNAs, U3 snoRNA, U1 RNA, U6 snRNA (11)(12)(13)(14)(15)(16)(17)(18)(19)(20), and stabilization of viral (21-23) as well as cellular RNAs (24). In the cytoplasm, La has been implicated in the translational control of viral (25-27) and cellular RNAs (28 -30).The human La protein contains a nuclear localization sequence at the very C-terminal end, and the staining for endogenous La as well as the distribution of GFP-tagged La reveal a predominantly diffuse nuclear staining, although this may appear different under certain conditions or treatments (31-33). Subcellular distribution of human and yeast La was assumed to be independent of phosphorylation (34, 35); however, recent studies (36, 37) revealed that phosphorylation at Ser-366 may well influence subcellular localization of La. A regulated, nonhomogeneous nuclear distribution of La may also be predicted from the distinct nuclear distribution of its various RNA interaction partners. For instance, pre-tRNAs are most likely synthesized in the nucleoplasm (38) but are processed, at least in part, in the nucleolus (39, 40), whereas in yeast the La-associated precursor of U3 snoRNA is probably processed in the nucleolar body and nucleolus (20). Nevertheless, interactions with precursor RNAs in different nuclear compartments implicate a highly dynamic and regulated nuclear distribution of La. Although a nucleolar localization of La has been reported (for review see Ref. 9), the hLa protein was not identified among the recently resolved protein ...

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Two Novel Classes of Small Ribonucleoproteins Detected by Antibodies Associated with Lupus Erythematosus

Cited by 522 publications

References 29 publications

Expression of Two Late Adenovirus Genes Is Altered by Introducing Antibodies against Ribonucleoprotein into Living HeLa Cells

Expression of Two Late Adenovirus Genes Is Altered by Introducing Antibodies against Ribonucleoprotein into Living HeLa Cells

The Y3** ncRNA promotes the 3′ end processing of histone mRNAs

Nuclear Trafficking of La Protein Depends on a Newly Identified Nucleolar Localization Signal and the Ability to Bind RNA

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