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      Cajal bodies and snRNPs - friends with benefits

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      Publication date (Electronic):
      Journal: RNA Biology
      Publisher: Taylor & Francis

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          ABSTRACT

          Spliceosomal snRNPs are complex particles that proceed through a fascinating maturation pathway. Several steps of this pathway are closely linked to nuclear non-membrane structures called Cajal bodies. In this review, I summarize the last 20 y of research in this field. I primarily focus on snRNP biogenesis, specifically on the steps that involve Cajal bodies. I also evaluate the contribution of the Cajal body in snRNP quality control and discuss the role of snRNPs in Cajal body formation.

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          Integrator, a multiprotein mediator of small nuclear RNA processing, associates with the C-terminal repeat of RNA polymerase II.

          Ramin Shiekhattar, Anders Näär, Neil Cooch … (2005)
          The C-terminal domain (CTD) of RNA polymerase II (RNAPII) is an essential component of transcriptional regulation and RNA processing of protein-coding genes. A large body of data also implicates the CTD in the transcription and processing of RNAPII-mediated small nuclear RNAs (snRNAs). However, the identity of the complex (or complexes) that associates with the CTD and mediates the processing of snRNAs has remained elusive. Here, we describe an RNA polymerase II complex that contains at least 12 novel subunits, termed the Integrator, in addition to core RNAPII subunits. Two of the Integrator subunits display similarities to the subunits of the cleavage and polyadenylation specificity factor (CPSF) complex. We show that Integrator is recruited to the U1 and U2 snRNA genes and mediates the snRNAs' 3' end processing. The Integrator complex is evolutionarily conserved in metazoans and directly interacts with the C-terminal domain of the RNA polymerase II largest subunit.
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            Cajal body-specific small nuclear RNAs: a novel class of 2'-O-methylation and pseudouridylation guide RNAs.

            Maria Kiss, Céline Verheggen, Tamás Kiss … (2002)
            Cajal (coiled) bodies are conserved subnuclear organelles that are present in the nucleoplasm of both animal and plant cells. Although Cajal bodies were first described nearly 100 years ago, their function has remained largely speculative. Here, we describe a novel class of human small nuclear RNAs that localize specifically to Cajal bodies. The small Cajal body-specific RNAs (scaRNAs) are predicted or have already been demonstrated to function as guide RNAs in site-specific synthesis of 2'-O-ribose-methylated nucleotides and pseudouridines in the RNA polymerase II-transcribed U1, U2, U4 and U5 spliceosomal small nuclear RNAs (snRNAs). Our results provide strong support for the idea that the Cajal body, this mysterious nuclear organelle, provides the cellular locale for post-transcriptional modification of spliceosomal snRNAs.
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              The evolutionarily conserved core design of the catalytic activation step of the yeast spliceosome.

              Patrizia Fabrizio, Julia Dannenberg, Prakash Dube … (2009)
              Metazoan spliceosomes exhibit an elaborate protein composition required for canonical and alternative splicing. Thus, the minimal set of proteins essential for activation and catalysis remains elusive. We therefore purified in vitro assembled, precatalytic spliceosomal complex B, activated B(act), and step 1 complex C from the simple eukaryote Saccharomyces cerevisiae. Mass spectrometry revealed that yeast spliceosomes contain fewer proteins than metazoans and that each functional stage is very homogeneous. Dramatic compositional changes convert B to B(act), which is composed of approximately 40 evolutionarily conserved proteins that organize the catalytic core. Additional remodeling occurs concomitant with step 1, during which nine proteins are recruited to form complex C. The moderate number of proteins recruited to complex C will allow investigations of the chemical reactions in a fully defined system. Electron microscopy reveals high-quality images of yeast spliceosomes at defined functional stages, indicating that they are well-suited for three-dimensional structure analyses.
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                Author and article information

                Journal
                Journal ID (nlm-ta): RNA Biol
                Journal ID (iso-abbrev): RNA Biol
                Journal ID (publisher-id): KRNB
                Journal ID (publisher-id): krnb20
                Title: RNA Biology
                Publisher: Taylor & Francis
                ISSN (Print): 1547-6286
                ISSN (Electronic): 1555-8584
                Publication date Collection: 2017
                Publication date (Electronic): 14 September 2016
                Publication date PMC-release: 14 September 2016
                Volume: 14
                Issue: 6 , Cajal Bodies Guest Editor: Karla M. Neugebauer
                Pages: 671-679
                Affiliations
                Institute of Molecular Genetics, Czech Academy of Sciences , Prague, Czech Republic
                Author notes
                CONTACT David Staněk stanek@ 123456img.cas.cz Institute of Molecular Genetics CAS , Videnska 1083, 142 20 Prague, Czech Republic
                Author information
                https://orcid.org/0000-0002-5865-175X
                Article
                Publisher ID: 1231359
                DOI: 10.1080/15476286.2016.1231359
                PMC ID: 5519240
                PubMed ID: 27627834
                SO-VID: ed6f23a1-431c-463b-96f8-fd69708751bd
                Copyright © © 2017 The Author(s). Published with license by Taylor & Francis Group, LLC
                License:

                This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License ( http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.

                History
                Date received : 8 July 2016
                Date revision received : 24 August 2016
                Date accepted : 29 August 2016
                Page count
                Figures: 2, Tables: 0, References: 114, Pages: 9
                Categories
                Subject: Review

                ScienceOpen disciplines: Molecular biology
                Data availability:
                ScienceOpen disciplines: Molecular biology

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