U7 small nuclear RNA

Last updated
U7 small nuclear RNA
RF00066.jpg
Predicted secondary structure and sequence conservation of U7
Identifiers
SymbolU7
Rfam RF00066
Other data
RNA type Gene; snRNA
Domain(s) Eukaryota
SO SO:0000274
PDB structures PDBe

The U7 small nuclear RNA (U7 snRNA) is an RNA molecule and a component of the small nuclear ribonucleoprotein complex (U7 snRNP). The U7 snRNA is required for histone pre-mRNA processing.

Contents

The 5' end of the U7 snRNA binds the HDE (histone downstream element), a conserved purine-rich region, located 15 nucleotides downstream the histone mRNA cleavage site. [1] [2] The binding of the HDE region by the U7 snRNA, through complementary base-pairing, is an important step for the future recruitment of cleavage factors during histone pre-mRNA processing. [3]

See also

Related Research Articles

snRNPs, or small nuclear ribonucleoproteins, are RNA-protein complexes that combine with unmodified pre-mRNA and various other proteins to form a spliceosome, a large RNA-protein molecular complex upon which splicing of pre-mRNA occurs. The action of snRNPs is essential to the removal of introns from pre-mRNA, a critical aspect of post-transcriptional modification of RNA, occurring only in the nucleus of eukaryotic cells. Additionally, U7 snRNP is not involved in splicing at all, as U7 snRNP is responsible for processing the 3′ stem-loop of histone pre-mRNA.

Small nuclear RNA (snRNA) is a class of small RNA molecules that are found within the splicing speckles and Cajal bodies of the cell nucleus in eukaryotic cells. The length of an average snRNA is approximately 150 nucleotides. They are transcribed by either RNA polymerase II or RNA polymerase III. Their primary function is in the processing of pre-messenger RNA (hnRNA) in the nucleus. They have also been shown to aid in the regulation of transcription factors or RNA polymerase II, and maintaining the telomeres.

<span class="mw-page-title-main">LSm</span> Family of RNA-binding proteins

In molecular biology, LSm proteins are a family of RNA-binding proteins found in virtually every cellular organism. LSm is a contraction of 'like Sm', because the first identified members of the LSm protein family were the Sm proteins. LSm proteins are defined by a characteristic three-dimensional structure and their assembly into rings of six or seven individual LSm protein molecules, and play a large number of various roles in mRNA processing and regulation.

<span class="mw-page-title-main">Histone 3′ UTR stem-loop</span>

The histone 3′ UTR stem-loop is an RNA element involved in nucleocytoplasmic transport of the histone mRNAs, and in the regulation of stability and of translation efficiency in the cytoplasm. The mRNAs of metazoan histone genes lack polyadenylation and a poly-A tail, instead 3′ end processing occurs at a site between this highly conserved stem-loop and a purine rich region around 20 nucleotides downstream. The stem-loop is bound by a 31 kDa stem-loop binding protein. Together with U7 snRNA binding of the HDE, SLBP binding nucleates the formation of the processing complex.

<span class="mw-page-title-main">U4 spliceosomal RNA</span> Non-coding RNA component of the spliceosome

The U4 small nuclear Ribo-Nucleic Acid is a non-coding RNA component of the major or U2-dependent spliceosome – a eukaryotic molecular machine involved in the splicing of pre-messenger RNA (pre-mRNA). It forms a duplex with U6, and with each splicing round, it is displaced from the U6 snRNA in an ATP-dependent manner, allowing U6 to re-fold and create the active site for splicing catalysis. A recycling process involving protein Brr2 releases U4 from U6, while protein Prp24 re-anneals U4 and U6. The crystal structure of a 5′ stem-loop of U4 in complex with a binding protein has been solved.

<span class="mw-page-title-main">HNRPU</span> Protein-coding gene in the species Homo sapiens

Heterogeneous nuclear ribonucleoprotein U is a protein that in humans is encoded by the HNRNPU gene.

<span class="mw-page-title-main">HNRPD</span> Protein-coding gene in the species Homo sapiens

Heterogeneous nuclear ribonucleoprotein D0 (HNRNPD) also known as AU-rich element RNA-binding protein 1 (AUF1) is a protein that in humans is encoded by the HNRNPD gene. Alternative splicing of this gene results in four transcript variants.

<span class="mw-page-title-main">HNRNPC</span> Protein-coding gene in the species Homo sapiens

Heterogeneous nuclear ribonucleoproteins C1/C2 is a protein that in humans is encoded by the HNRNPC gene.

<span class="mw-page-title-main">SNRPB</span> Protein-coding gene in the species Homo sapiens

Small nuclear ribonucleoprotein-associated proteins B and B' is a protein that in humans is encoded by the SNRPB gene.

<span class="mw-page-title-main">U2 small nuclear RNA auxiliary factor 1</span> Protein-coding gene in the species Homo sapiens

Splicing factor U2AF 35 kDa subunit is a protein that in humans is encoded by the U2AF1 gene.

<span class="mw-page-title-main">SLBP</span> Protein-coding gene in humans

Histone RNA hairpin-binding protein or stem-loop binding protein (SLBP) is a protein that in humans is encoded by the SLBP gene.

<span class="mw-page-title-main">HNRNPL</span> Protein-coding gene in the species Homo sapiens

Heterogeneous nuclear ribonucleoprotein L is a protein that in humans is encoded by the HNRNPL gene.

<span class="mw-page-title-main">SF3B3</span> Protein-coding gene in the species Homo sapiens

Splicing factor 3B subunit 3 is a protein that in humans is encoded by the SF3B3 gene.

<span class="mw-page-title-main">PRPF6</span> Protein-coding gene in the species Homo sapiens

Pre-mRNA-processing factor 6 is a protein that in humans is encoded by the PRPF6 gene.

<span class="mw-page-title-main">SNRPB2</span> Protein-coding gene in the species Homo sapiens

U2 small nuclear ribonucleoprotein B is a protein that in humans is encoded by the SNRPB2 gene.

<span class="mw-page-title-main">SNRPG</span> Protein-coding gene in the species Homo sapiens

Small nuclear ribonucleoprotein G is a protein that in humans is encoded by the SNRPG gene.

<span class="mw-page-title-main">PRPF4</span> Protein-coding gene in the species Homo sapiens

U4/U6 small nuclear ribonucleoprotein Prp4 is a protein that in humans is encoded by the PRPF4 gene. The removal of introns from nuclear pre-mRNAs occurs on complexes called spliceosomes, which are made up of 4 small nuclear ribonucleoprotein (snRNP) particles and an undefined number of transiently associated splicing factors. PRPF4 is 1 of several proteins that associate with U4 and U6 snRNPs.[supplied by OMIM]

<span class="mw-page-title-main">LSM10</span> Protein-coding gene in the species Homo sapiens

U7 snRNA-associated Sm-like protein LSm10 is a protein that in humans is encoded by the LSM10 gene.

<span class="mw-page-title-main">HNRPDL</span> Mammalian protein found in Homo sapiens

Heterogeneous nuclear ribonucleoprotein D-like, also known as HNRPDL, is a protein which in humans is encoded by the HNRPDL gene.

<span class="mw-page-title-main">ZNF473</span> Protein-coding gene in the species Homo sapiens

Zinc finger protein 473 is a protein that in humans is encoded by the ZNF473 gene.

References

  1. ↑ Spycher C, Streit A, Stefanovic B, Albrecht D, Koning TH, Schümperli D (1994). "3' end processing of mouse histone pre-mRNA: evidence for additional base-pairing between U7 snRNA and pre-mRNA". Nucleic Acids Res. 22 (20): 4023–4030. doi:10.1093/nar/22.20.4023. PMC   331885 . PMID   7937126.
  2. ↑ Mowry KL, Steitz JA (1987). "Identification of the human U7 snRNP as one of several factors involved in the 3' end maturation of histone premessenger RNA's". Science. 238 (4834): 1682–1687. Bibcode:1987Sci...238.1682M. doi:10.1126/science.2825355. PMID   2825355.
  3. ↑ Marzluff, William F.; Wagner, Eric J.; Duronio, Robert J. (2008). "Metabolism and regulation of canonical histone mRNAs: life without a poly(A) tail". Nature Reviews Genetics. 9 (11): 843–854. doi:10.1038/nrg2438. PMC   2715827 . PMID   18927579.

Further reading

  1. ↑ Voigt T, Meyer K, Baum O, Schümperli D (2010). "Ultrastructural changes in diaphragm neuromuscular junctions in a severe mouse model for Spinal Muscular Atrophy and their prevention by bifunctional U7 snRNA correcting SMN2 splicing". Neuromuscul Disord. 20 (11): 744–752. doi:10.1016/j.nmd.2010.06.010. PMID   20832308. S2CID   11835561.
  2. ↑ Ruepp MD, Vivarelli S, Pillai RS, Kleinschmidt N, Azzouz TN, Barabino SM, Schümperli D (2010). "The 68 kDa subunit of mammalian cleavage factor I interacts with the U7 small nuclear ribonucleoprotein and participates in 3'-end processing of animal histone mRNAs". Nucleic Acids Res. 38 (21): 7637–7650. doi:10.1093/nar/gkq613. PMC   2995043 . PMID   20634199.
  3. ↑ Geib T, Hertel KJ (2009). Valcarcel, Juan (ed.). "Restoration of full-length SMN promoted by adenoviral vectors expressing RNA antisense oligonucleotides embedded in U7 snRNAs". PLOS ONE. 4 (12): e8204. Bibcode:2009PLoSO...4.8204G. doi: 10.1371/journal.pone.0008204 . PMC   2781471 . PMID   19997596.
  4. ↑ Godfrey AC, White AE, Tatomer DC, Marzluff WF, Duronio RJ (2009). "The Drosophila U7 snRNP proteins Lsm10 and Lsm11 are required for histone pre-mRNA processing and play an essential role in development". RNA. 15 (9): 1661–1672. doi:10.1261/rna.1518009. PMC   2743060 . PMID   19620235.
  5. ↑ Yang XC, Torres MP, Marzluff WF, Dominski Z (2009). "Three proteins of the U7-specific Sm ring function as the molecular ruler to determine the site of 3'-end processing in mammalian histone pre-mRNA". Mol Cell Biol. 29 (15): 4045–4056. doi:10.1128/MCB.00296-09. PMC   2715809 . PMID   19470752.
  6. ↑ Goyenvalle A, Babbs A, van Ommen GJ, Garcia L, Davies KE (2009). "Enhanced exon-skipping induced by U7 snRNA carrying a splicing silencer sequence: Promising tool for DMD therapy". Mol Ther. 17 (7): 1234–1240. doi:10.1038/mt.2009.113. PMC   2835201 . PMID   19455105.
  7. ↑ Meyer K, Marquis J, Trüb J, Nlend Nlend R, Verp S, Ruepp MD, Imboden H, Barde I, Trono D, Schümperli D (2009). "Rescue of a severe mouse model for spinal muscular atrophy by U7 snRNA-mediated splicing modulation". Hum Mol Genet. 18 (3): 546–555. doi: 10.1093/hmg/ddn382 . PMID   19010792.
  8. ↑ Marquis J, Kämpfer SS, Angehrn L, Schümperli D (2009). "Doxycycline-controlled splicing modulation by regulated antisense U7 snRNA expression cassettes". Gene Ther. 16 (1): 70–77. doi: 10.1038/gt.2008.138 . PMID   18701908.
  9. ↑ Marz M, Mosig A, Stadler BM, Stadler PF (2007). "U7 snRNAs: a computational survey". Genomics Proteomics Bioinformatics. 5 (3–4): 187–195. doi:10.1016/S1672-0229(08)60006-6. PMC   5054213 . PMID   18267300.
  10. ↑ Higuchi T, Anzai K, Kobayashi S (2008). "U7 snRNA acts as a transcriptional regulator interacting with an inverted CCAAT sequence-binding transcription factor NF-Y". Biochim Biophys Acta. 1780 (2): 274–281. doi:10.1016/j.bbagen.2007.11.005. PMID   18078822.
  11. ↑ Friend K, Lovejoy AF, Steitz JA (2007). "U2 snRNP binds intronless histone pre-mRNAs to facilitate U7-snRNP-dependent 3' end formation". Mol Cell. 28 (2): 240–252. doi:10.1016/j.molcel.2007.09.026. PMC   2149891 . PMID   17964263.
  12. ↑ Uchikawa H, Fujii K, Kohno Y, Katsumata N, Nagao K, Yamada M, Miyashita T (2007). "U7 snRNA-mediated correction of aberrant splicing caused by activation of cryptic splice sites". J Hum Genet. 52 (11): 891–897. doi: 10.1007/s10038-007-0192-8 . PMID   17851636.
  13. ↑ Marquis J, Meyer K, Angehrn L, Kämpfer SS, Rothen-Rutishauser B, Schümperli D (2007). "Spinal muscular atrophy: SMN2 pre-mRNA splicing corrected by a U7 snRNA derivative carrying a splicing enhancer sequence". Mol Ther. 15 (8): 1479–1486. doi: 10.1038/sj.mt.6300200 . PMID   17505471.
  14. ↑ Asparuhova MB, Marti G, Liu S, Serhan F, Trono D, Schümperli D (2007). "Inhibition of HIV-1 multiplication by a modified U7 snRNA inducing Tat and Rev exon skipping". J Gene Med. 9 (5): 323–334. doi:10.1002/jgm.1027. PMID   17474072. S2CID   26072168.
  15. ↑ Scheuerbrandt G (2006). "Exon skipping with U7 gene transfer". Acta Myol. 25 (1): 40–2. PMID   17039980.
  16. ↑ Jaeger S, Martin F, Rudinger-Thirion J, Giegé R, Eriani G (2006). "Binding of human SLBP on the 3'-UTR of histone precursor H4-12 mRNA induces structural rearrangements that enable U7 snRNA anchoring". Nucleic Acids Res. 34 (17): 4987–4995. doi:10.1093/nar/gkl666. PMC   1635294 . PMID   16982637.
  17. ↑ Wagner EJ, Marzluff WF (2006). "ZFP100, a component of the active U7 snRNP limiting for histone pre-mRNA processing, is required for entry into S phase". Mol Cell Biol. 26 (17): 6702–6712. doi:10.1128/MCB.00391-06. PMC   1592837 . PMID   16914750.
  18. ↑ Kolev NG, Steitz JA (2006). "In vivo assembly of functional U7 snRNP requires RNA backbone flexibility within the Sm-binding site". Nat Struct Mol Biol. 13 (4): 347–353. doi:10.1038/nsmb1075. PMID   16547514. S2CID   868532.
  19. ↑ Godfrey AC, Kupsco JM, Burch BD, Zimmerman RM, Dominski Z, Marzluff WF, Duronio RJ (2006). "U7 snRNA mutations in Drosophila block histone pre-mRNA processing and disrupt oogenesis". RNA. 12 (3): 396–409. doi:10.1261/rna.2270406. PMC   1383579 . PMID   16495235.
  20. ↑ Madocsai C, Lim SR, Geib T, Lam BJ, Hertel KJ (2005). "Correction of SMN2 Pre-mRNA splicing by antisense U7 small nuclear RNAs". Mol Ther. 12 (6): 1013–1022. doi: 10.1016/j.ymthe.2005.08.022 . PMID   16226920.
  21. ↑ Azzouz TN, Pillai RS, Däpp C, Chari A, Meister G, Kambach C, Fischer U, Schümperli D (2005). "Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm proteins with PRMT5 and SMN complexes". J Biol Chem. 280 (41): 34435–34440. doi: 10.1074/jbc.M505077200 . hdl: 21.11116/0000-0007-E5F1-6 . PMID   16087681.
  22. ↑ Azzouz TN, Gruber A, Schümperli D (2005). "U7 snRNP-specific Lsm11 protein: dual binding contacts with the 100 kDa zinc finger processing factor (ZFP100) and a ZFP100-independent function in histone RNA 3' end processing". Nucleic Acids Res. 33 (7): 2106–2117. doi:10.1093/nar/gki516. PMC   1075925 . PMID   15824063.
  23. ↑ Goyenvalle A, Vulin A, Fougerousse F, Leturcq F, Kaplan JC, Garcia L, Danos O (2004). "Rescue of dystrophic muscle through U7 snRNA-mediated exon skipping". Science. 306 (5702): 1796–1799. Bibcode:2004Sci...306.1796G. doi: 10.1126/science.1104297 . PMID   15528407. S2CID   9359783.
  24. ↑ Schümperli D, Pillai RS (2004). "The special Sm core structure of the U7 snRNP: far-reaching significance of a small nuclear ribonucleoprotein" (PDF). Cell Mol Life Sci. 61 (19–20): 2560–2570. doi:10.1007/s00018-004-4190-0. PMID   15526162. S2CID   5780814.
  25. ↑ Liu S, Asparuhova M, Brondani V, Ziekau I, Klimkait T, Schümperli D (2004). "Inhibition of HIV-1 multiplication by antisense U7 snRNAs and siRNAs targeting cyclophilin A". Nucleic Acids Res. 32 (12): 3752–3759. doi:10.1093/nar/gkh715. PMC   484190 . PMID   15254276.
  26. ↑ Azzouz TN, Schumperli D (2003). "Evolutionary conservation of the U7 small nuclear ribonucleoprotein in Drosophila melanogaster". RNA. 9 (12): 1532–1541. doi:10.1261/rna.5143303. PMC   1370506 . PMID   14624008.
  27. ↑ Pillai RS, Grimmler M, Meister G, Will CL, Lührmann R, Fischer U, Schümperli D (2003). "Unique Sm core structure of U7 snRNPs: assembly by a specialized SMN complex and the role of a new component, Lsm11, in histone RNA processing". Genes Dev. 17 (18): 2321–2333. doi:10.1101/gad.274403. PMC   196468 . PMID   12975319.
  28. ↑ Dominski Z, Yang XC, Purdy M, Marzluff WF (2003). "Cloning and characterization of the Drosophila U7 small nuclear RNA". Proc Natl Acad Sci U S A. 100 (16): 9422–9427. Bibcode:2003PNAS..100.9422D. doi: 10.1073/pnas.1533509100 . PMC   170934 . PMID   12872004.
  29. ↑ Brun C, Suter D, Pauli C, Dunant P, Lochmüller H, Burgunder JM, Schümperli D, Weis J (2003). "U7 snRNAs induce correction of mutated dystrophin pre-mRNA by exon skipping". Cell Mol Life Sci. 60 (3): 557–566. doi:10.1007/s000180300047. PMID   12737315. S2CID   42878523.
  30. ↑ Dominski Z, Erkmann JA, Yang X, Sànchez R, Marzluff WF (2002). "A novel zinc finger protein is associated with U7 snRNP and interacts with the stem-loop binding protein in the histone pre-mRNP to stimulate 3'-end processing". Genes Dev. 16 (1): 58–71. doi:10.1101/gad.932302. PMC   155312 . PMID   11782445.
  31. ↑ Pillai RS, Will CL, Lührmann R, Schümperli D, Müller B (2001). "Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like protein". EMBO J. 20 (19): 5470–5479. doi:10.1093/emboj/20.19.5470. PMC   125645 . PMID   11574479.
  32. ↑ Müller B, Link J, Smythe C (2000). "Assembly of U7 small nuclear ribonucleoprotein particle and histone RNA 3' processing in Xenopus egg extracts". J Biol Chem. 275 (32): 24284–24293. doi: 10.1074/jbc.M003253200 . PMID   10827192.
  33. ↑ Tuma RS, Roth MB (1999). "Induction of coiled body-like structures in Xenopus oocytes by U7 snRNA". Chromosoma. 108 (6): 337–344. doi:10.1007/s004120050385. PMID   10591993. S2CID   26083793.
  34. ↑ Suter D, Tomasini R, Reber U, Gorman L, Kole R, Schümperli D (1999). "Double-target antisense U7 snRNAs promote efficient skipping of an aberrant exon in three human beta-thalassemic mutations". Hum Mol Genet. 8 (13): 2415–2423. doi: 10.1093/hmg/8.13.2415 . PMID   10556289.
  35. ↑ Jacobs EY, Frey MR, Wu W, Ingledue TC, Gebuhr TC, Gao L, Marzluff WF, Matera AG (1999). "Coiled bodies preferentially associate with U4, U11, and U12 small nuclear RNA genes in interphase HeLa cells but not with U6 and U7 genes". Mol Biol Cell. 10 (5): 1653–63. doi:10.1091/mbc.10.5.1653. PMC   30488 . PMID   10233169.
  36. ↑ Dominski Z, Zheng LX, Sanchez R, Marzluff WF (1999). "Stem-loop binding protein facilitates 3'-end formation by stabilizing U7 snRNP binding to histone pre-mRNA". Mol Cell Biol. 19 (5): 3561–70. doi:10.1128/mcb.19.5.3561. PMC   84148 . PMID   10207079.
  37. ↑ Müller B, Schümperli D (1997). "The U7 snRNP and the hairpin binding protein: Key players in histone mRNA metabolism". Semin Cell Dev Biol. 8 (6): 567–576. doi:10.1006/scdb.1997.0182. PMID   9642171.
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  57. ↑ Melin L, Soldati D, Mital R, Streit A, Schümperli D (1992). "Biochemical demonstration of complex formation of histone pre-mRNA with U7 small nuclear ribonucleoprotein and hairpin binding factors". EMBO J. 11 (2): 691–7. doi:10.1002/j.1460-2075.1992.tb05101.x. PMC   556501 . PMID   1531633.
  58. ↑ Murray BA, Turner PC (1992). "Copy number of the U7 gene in some mammalian species". Biochem Soc Trans. 20 (1): 28S. doi:10.1042/bst020028s. PMID   1386043.
  59. ↑ Smith HO, Tabiti K, Schaffner G, Soldati D, Albrecht U, Birnstiel ML (1991). "Two-step affinity purification of U7 small nuclear ribonucleoprotein particles using complementary biotinylated 2'-O-methyl oligoribonucleotides". Proc Natl Acad Sci U S A. 88 (21): 9784–9788. Bibcode:1991PNAS...88.9784S. doi: 10.1073/pnas.88.21.9784 . PMC   52805 . PMID   1835087.
  60. ↑ Bond UM, Yario TA, Steitz JA (1991). "Multiple processing-defective mutations in a mammalian histone pre-mRNA are suppressed by compensatory changes in U7 RNA both in vivo and in vitro". Genes Dev. 5 (9): 1709–1722. doi: 10.1101/gad.5.9.1709 . PMID   1885007.
  61. ↑ Phillips SC, Turner PC (1991). "Deletions downstream of the 3' box of the mouse U7 small nuclear RNA gene dramatically affect transcription". Biochem Soc Trans. 19 (3): 342S. doi:10.1042/bst019342s. PMID   1783173.
  62. ↑ Turner PC, Phillips SC (1991). "Unusual compartmentalisation of mouse U7 small nuclear transcripts in Xenopus oocytes". Biochem Soc Trans. 19 (3): 341S. doi:10.1042/bst019341s. PMID   1783172.
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