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Ribonucleoprotein

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Ribonucleoprotein (RNP) is a nucleoprotein that contains RNA, i.e. it is an association that combines a ribonucleic acid and an RNA-binding protein together. Such a combination can also be referred to as a protein-RNA complex. These complexes play an integral part in a number of important biological functions that include DNA replication, regulating gene expression[1] and regulating the metabolism of RNA.[2] A few examples of RNPs include the ribosome, the enzyme telomerase, vault ribonucleoproteins, RNase P, hnRNP and small nuclear RNPs (snRNPs), which have been implicated in pre-mRNA splicing (spliceosome) and are among the main components of the nucleolus.[3]

A representative live cell imaging and tracking of cytoplasmic progeny vRNP signals of the influenza A virus. Results of the experiment suggest that the progeny vRNP uses Rab11-dependent RE machinery for apical plasma membrane trafficking. [4]

Currently, over 2000 RNPs can be found in the RCSB Protein Data Bank (PDB)[5]. Furthermore, the Protein-RNA Interface Data Base (PRIDB) possesses a collection of information on RNA-protein interfaces based on data drawn from the PDB.[6] Common features of protein-RNA interface were deduced based on known structures. For example, RNP in snRNPs have an RNA-binding motif in its RNA-binding protein. Aromatic amino acid residues in this motif result in stacking interactions with RNA. Lysine residues in the helical portion of RNA-binding proteins help to stabilize interactions with nucleic acids. This nucleic acid binding is strengthened by electrostatic attraction between the positive lysine side chains and the negative nucleic acid phosphate backbones. Additionally, it is possible to model RNPs computationally.[7] Although computational methods of deducing RNP structures are less accurate than experimental methods, they provide a rough model of the structure which allows for predictions of the identity of significant amino acids and nucleotide residues. Such information helps in understanding the overall function the RNP.

'RNP' can also refer to ribonucleoprotein particles. Ribonucleoprotein particles are distinct intracellular foci for post-transcriptional regulation. These particles play an important role in influenza A virus replication[8]. The influenza viral genome is composed of eight ribonucleoprotein particles formed by a complex of negative-sense RNA bound to a viral nucleoprotein. Each RNP carries with it an RNA polymerase complex. When the nucleoprotein binds to the viral RNA, it is able to expose the bases which allow the viral polymerase to transcribe RNA. At this point, once the virus enters a host cell it will be prepared to begin the process of replication.

Ribonucleoprotein (RNP) is a nucleoprotein that contains RNA, i.e. it is an association that combines ribonucleic acid and protein together (referred also as protein-RNA complexes).

Possibly add a source here?

Currently, over 2000 RNPs can be found in PDB database. Include link to PDB database.

During the replication stage of Kaposi’s sarcoma-associated herpesvirus (KSHV), mRNAs in the cytoplasm are often cleaved and broken down by the viral nuclease SOX. Some mRNAs are able to avoid degradation through the protection of a group of proteins that associates with a sequence element on the IL-6 mRNA. This protection is illustrated here as an RNP complex protects the Interleukin 6 mRNA. [9]

Link to PDB? (http://www.rcsb.org/pdb/results/results.do?tabtoshow=Current&qrid=F7A00833)

Additionally, it is possible to model RNPs computationally.

New paragraph, explain how RNPS can be modeled computationally.

RNPs among many can play an important role in influenza A virus replication.

Among many what?

'RNP' can also refer to ribonucleoprotein particles, distinct intracellular foci for post-transcriptional regulation.

Seems random. Jumped between three different topics. Possibly improve organization, expand on single sentence paragraphs/topics and improve on the flow of the article a little bit.

MAYBE expand on their role in mixed connective tissue disease.

Definitely expand list of ribonucleoproteins.

  1. ^ Hogan, Daniel J; Riordan, Daniel P; Gerber, André P; Herschlag, Daniel; Brown, Patrick O (2016-11-06). "Diverse RNA-Binding Proteins Interact with Functionally Related Sets of RNAs, Suggesting an Extensive Regulatory System". PLoS Biology. 6 (10). doi:10.1371/journal.pbio.0060255. ISSN 1544-9173. PMC 2573929. PMID 18959479.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  2. ^ Lukong, Kiven E.; Chang, Kai-wei; Khandjian, Edouard W.; Richard, Stéphane (2008-08-01). "RNA-binding proteins in human genetic disease". Trends in genetics: TIG. 24 (8): 416–425. doi:10.1016/j.tig.2008.05.004. ISSN 0168-9525. PMID 18597886.
  3. ^ "Ribonucleoprotein". www.uniprot.org. Retrieved 2016-11-06.
  4. ^ Momose, Fumitaka; Sekimoto, Tetsuya; Ohkura, Takashi; Jo, Shuichi; Kawaguchi, Atsushi; Nagata, Kyosuke; Morikawa, Yuko (2011-06-22). "Apical Transport of Influenza A Virus Ribonucleoprotein Requires Rab11-positive Recycling Endosome". PLoS ONE. 6 (6). doi:10.1371/journal.pone.0021123. ISSN 1932-6203. PMC 3120830. PMID 21731653.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  5. ^ Bank, RCSB Protein Data. "RCSB Protein Data Bank - RCSB PDB". {{cite journal}}: Cite journal requires |journal= (help)
  6. ^ Lewis, Benjamin A.; Walia, Rasna R.; Terribilini, Michael; Ferguson, Jeff; Zheng, Charles; Honavar, Vasant; Dobbs, Drena (2016-11-06). "PRIDB: a protein–RNA interface database". Nucleic Acids Research. 39 (Database issue): D277–D282. doi:10.1093/nar/gkq1108. ISSN 0305-1048. PMC 3013700. PMID 21071426.
  7. ^ Tuszynska, Irina; Matelska, Dorota; Magnus, Marcin; Chojnowski, Grzegorz; Kasprzak, Joanna M.; Kozlowski, Lukasz P.; Dunin-Horkawicz, Stanislaw; Bujnicki, Janusz M. (2014-02-01). "Computational modeling of protein-RNA complex structures". Methods (San Diego, Calif.). 65 (3): 310–319. doi:10.1016/j.ymeth.2013.09.014. ISSN 1095-9130. PMID 24083976.
  8. ^ Baudin, F; Bach, C; Cusack, S; Ruigrok, R W (1994-07-01). "Structure of influenza virus RNP. I. Influenza virus nucleoprotein melts secondary structure in panhandle RNA and exposes the bases to the solvent". The EMBO Journal. 13 (13): 3158–3165. ISSN 0261-4189. PMC 395207. PMID 8039508.
  9. ^ Muller, Mandy; Hutin, Stephanie; Marigold, Oliver; Li, Kathy H.; Burlingame, Al; Glaunsinger, Britt A. (2015-05-12). "A Ribonucleoprotein Complex Protects the Interleukin-6 mRNA from Degradation by Distinct Herpesviral Endonucleases". PLoS Pathogens. 11 (5). doi:10.1371/journal.ppat.1004899. ISSN 1553-7366. PMC 4428876. PMID 25965334.{{cite journal}}: CS1 maint: unflagged free DOI (link)
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