The review provides modern classification of evolutionarily conserved coilin-containing nuclear bodies of somatic and germ cells that is based on the characteristic features of their molecular composition and the nature of their functions. The main differences between Cajal bodies and histone locus bodies, which are involved in the biogenesis of small nuclear spliceosomal and nucleolar RNAs and in the 3′-end processing of histone precursor messenger RNA, respectively, are considered. It is shown that a significant contribution to the investigation of the diversity of coilin-containing bodies was made by the studies on the architecture of the RNA processing machinery in oocyte nuclei in a number of model organisms. The characteristics features of the molecular composition of coilin-containing bodies in growing oocyte nuclei (the so-called germinal vesicles) of vertebrates, including amphibians and birds, are described.
This is a preview of subscription content, access via your institution.
Buy single article
Instant access to the full article PDF.
Price includes VAT (USA)
Tax calculation will be finalised during checkout.
small nuclear RNAs
small nuclear ribonucleoproteins
small nucleolar RNAs
precursor messenger RNAs
histone locus body
small Cajal body-specific RNAs
Abbot, J., Marzluff, W.F., and Gall, J.G., The stem-loop binding protein (SLBP) is present in coiled bodies of the Xenopus germinal vesicle, Moll. Biol. Cell, 1999, vol. 10, no. 2, pp. 487–499.
Andrade, L.E.C., Chan, E.K.L., Raska, I., et al., Human autoantibody to a novel protein of the nuclear coiled body: immunological characterization and cDNA cloning of p80-coilin, J. Exp. Med., 1991, vol. 173, no. 6, pp. 1407–1419.
Andrade, L.E.C., Tan, E.M., and Chart, E.K.L., Immunocytochemical analysis of the coiled body in the cell cycle and during cell proliferation, Proc. Natl. Acad. Sci. USA, 1993, vol. 90, no. 5, pp. 1947–1951.
Batalova, F.M., Stepanova, I.S., Skovorodkin, I.N., et al., Identification and dynamics of Cajal bodies in relation to karyosphere formation in scorpionfly oocytes, Chromosoma, 2005, vol. 113, no. 8, pp. 428–439.
Bellini, M., Coilin, more than a molecular marker of the Cajal (coiled) body, BioEssays, 2000, vol. 22, no. 9, pp. 861–867.
Bellini, M. and Gall, J.G., Coilin can form a complex with the U7 small nuclear ribonucleoprotein, Mol. Biol. Cell, 1998, vol. 9, pp. 2987–3001.
Bogolyubov, D. and Parfenov, V., Structure of the insect oocyte nucleus with special reference to interchromatin granule clusters and Cajal bodies, Int. Rev. Cell Mol. Biol., 2008, vol. 269, pp. 59–110.
Bogolyubov, D., Stepanova, I., and Parfenov, V., Universal nuclear domains of somatic and germ cells: some lessons from oocyte interchromatin granule cluster and Cajal body structure and molecular composition, BioEssays, 2009, vol. 31, no. 4, pp. 400–409.
Bogolyubova, I.O. and Bogolyubov, D.S., Chapter IV: Oocyte nuclear structure during mammalian oogenesis, in Recent Advances in Germ Cells Research, Nova Biomedical, 2013, pp. 105–131.
Bongiorno-Borbone, L., De Cola, A., Vernole, P., et al., FLASH and NPAT positive but not coilin positive Cajal bodies correlate with cell ploidy, Cell Cycle, 2008, vol. 7, no. 15, pp. 2357–2367.
Broome, H.J. and Hebert, M.D., In vitro RNAse and nucleic acid binding activities implicate coilin in u snRNA processing, PLoS One, 2012, vol. 7, no. 4. doi: 10.1371/jour-nal.pone.0036300
Callan, H.G., Lampbrush Chromosomes. Molecular Biology, Biochemistry and Biohysics, Berlin: Springer-Verlag, 1986.
Callan, H.G. and Lloyd, L., Lampbrush chromosomes of crested newts Triturus cristatus (Laurenti), Philos. Trans. R. Soc. Lond. B: Biol. Sci., 1960, vol. 243, pp. 135–219.
Callan, H.G., Gall, J.G., and Murphy, C., Histone genes are located at the sphere loci of Xenopus lampbrush chromosomes, Chromosoma, 1991, vol. 101, no. 4, pp. 245–251.
Carmo-Fonseca, M., New clues to the function of the Cajal body, EMBO Rep., 2002, vol. 3, no. 8, pp. 726–727.
Carmo-Fonseca, M., Pepperkok, R., Sproat, B.S., et al., In vivo detection of snRNP-rich organelles in the nuclei of mammalian cells, EMBO J., 1991, vol. 10, no. 7, pp. 1863–1873.
Carmo-Fonseca, M., Pepperkok, R., Carvalho, M.T., et al., Transcription-dependent colocalization of the U1, U2, U4/U6, and U5 snRNPs in coiled bodies, J. Cell Biol., 1992, vol. 117, no. 1, pp. 1–14.
Carmo-Fonseca, M., Ferreira, J., and Lamond, A.I., Assembly of snRNP-containing coiled bodies is regulated in interphase and mitosis-evidence that the coiled body is a kinetic nuclear structure, J. Cell Biol., 1993, vol. 120, no. 4, pp. 841–852.
Cioce, M. and Lamond, A.I., Cajal bodies: a long history of discovery, Annu. Rev. Cell Dev. Biol., 2005, vol. 21, pp. 105–131.
Darzacq, X., Jády, B.E., Verheggen, C., et al., Cajal bodyspecific small nuclear RNAs: a novel class of 2′-O-methylation and pseudouridylation guide RNAs, EMBO J., 2002, vol. 21, no. 11, pp. 2746–2756.
Dedukh, D., Mazepa, G., Shabanov, D., et al., Cytological maps of lampbrush chromosomes of European water frogs (Pelophylax esculentus complex) from the Eastern Ukraine, BMC Genetics, 2013, vol. 14, no. 26. doi: 10.1186/1471-2156-14-26
Deryusheva, S. and Gall, J.G., Small Cajal body-specific RNAs of Drosophila function in the absence of Cajal bodies, Mol. Biol. Cell, 2009, vol. 20, no. 24, pp. 5250–5259.
Dundr, M., Nuclear bodies: multifunctional companions of the genome, Curr. Opin. Cell Biol., 2012, vol. 24, no. 3, pp. 415–422.
Dundr, M. and Misteli, T., Functional architecture in the cell nucleus, Biochem. J., 2001, vol. 356, no. 2, pp. 297–310.
Dundr, M. and Misteli, T., Biogenesis of nuclear bodies, Cold Spring Harb. Perspect. Biol., 2010, vol. 2, no. 12. doi: 10.1101/cshperspect.a000711
Dundr, M., Hebert, M.D., Karpova, T.S., et al., In vivo kinetics of Cajal body components, J. Cell Biol., 2004, vol. 164, no. 6, pp. 831–842.
Ferrai, C., de Castro, I.J., Lavitas, L., et al., Gene positioning, Cold Spring Harb. Perspect. Biol., 2010, vol. 2, no. 6. doi: 10.1101/cshperspect.a000588
Fischer, U., Liu, Q., and Dreyfuss, G., The SMN-SIP1 complex has an essential role in spliceosomal snRNP biogenesis, Cell, 1997, vol. 90, no. 6, pp. 1023–1029.
Gaginskaya, E.R., Functional morphology of chromosomes in the oogenesis of birds, Extended Abstract of Cand. Sci. (Biol.) Dissertation, Leningrad: LGU, 1989.
Gaginskaya, E.R. and Gruzova, M.N., Characteristics of oogenesis in the chaffinch, Tsitologiia, 1969, vol. 9, no. 10, pp. 1241–1251.
Gaginskaya, E.R. and Gruzova, M.N., Detection of the amplified rDNA in ovarial cells of some insects and birds by hybridization in situ, Tsitologiia, 1975, vol. 17, no. 10, pp. 1132–1137.
Gaginskaya, E., Kulikova, T., and Krasikova, A., Avian lampbrush chromosomes: a powerful tool for exploration of genome expression, Cytogenet. Genome Res., 2009, vol. 124, nos. 3–4, pp. 251–267.
Galardi, S., Fatica, A., Bachi, A., et al., Purified box C/D snoRNPs are able to reproduce site-specific 2′-O-methylation of target RNA in vitro, Mol. Cell Biol., 2002, vol. 22, no. 19, pp. 6663–6668.
Gall, J.G., Cajal bodies: the first 100 years, Annu. Rev. Cell Dev. Biol., 2000, vol. 16, pp. 273–300.
Gall, J.G., Stephenson, E.C., Erba, H.P., et al., Histone genes are located at the sphere loci of newt lampbrush chromosomes, Chromosoma, 1981, vol. 84, no. 2, pp. 159–171.
Gall, J.G., Tsvetkov, A., Wu, Z., et al., Is the sphere organelle/coiled body a universal nuclear component?, Dev. Genet., 1995, vol. 16, no. 1, pp. 25–35.
Gall, J.G., Bellini, M., Wu, Z., et al., Assembly of the nuclear transcription and processing machinery: Cajal bodies (coiled bodies) and transcriptosomes, Mol. Biol. Cell, 1999, vol. 10, no. 12, pp. 4385–4402.
Gall, J.G., Wu, Z., Murphy, C., et al., Structure in the amphibian germinal vesicle, Exp. Cell Res., 2004, vol. 296, no. 1, pp. 28–34.
Greenfield, M.L., The oocyte of the domestic chicken shortly after hatching, studied by electron microscopy, Embryol. Exp. Morph., 1966, vol. 15, no. 3, pp. 297–316.
Hebert, M.D. and Matera, A.G., Self-association of coilin reveals a common theme in nuclear body localization, Mol. Biol. Cell, 2000, vol. 11, no. 12, pp. 4159–4171.
Hebert, M.D., Szymczyk, P.W., Shpargel, K.B., et al., Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular atrophy protein, Genes Dev., 2001, vol. 15, no. 20, pp. 2720–2729.
Hofmann, I., Schnolzer, M., Kaufmann, I., et al., Symplekin, a constitutive protein of karyo- and cytoplasmic particles involved in mRNA biogenesis in Xenopus laevis oocytes, Mol. Biol. Cell, 2002, vol. 13, pp. 1665–1676.
Jády, B.E. and Kiss, T., A small nucleolar guide RNA functions both in 2′-O-ribose methylation and pseudouridylation of the U5 spliceosomal RNA, EMBO J., 2001, vol. 20, no. 3, pp. 541–551.
Jády, B.E., Bertrand, E., and Kiss, T., Human telomerase RNA and box H/ACA scaRNAs share a common Cajal body-specific localization signal, J. Cell Biol., 2004, vol. 164, no. 5, pp. 647–652.
Kaiser, T.E., Intine, R.V., and Dundr, M., De novo formation of a subnuclear body, Science, 2008, vol. 322, no. 5908, pp. 1713–1717.
Khodyuchenko, T., Gaginskaya, E., and Krasikova, A., Noncanonical Cajal bodies form in the nucleus of late stage avian oocytes lacking functional nucleolus, Histochem. Cell Biol., 2012, vol. 138, no. 1, pp. 57–73.
Khutinaeva, M.A., Kropotova, E.V., and Gaginskaya, E.R., The characteristics of the morphofunctional organization of the lampbrush chromosomes from the oocytes of the rock dove, Tsitologiya, 1989, vol. 31, no. 10, pp. 1185–1192.
Kiss, A.M., Jády, B.E., Darzacq, X., et al., A Cajal body specifc pseudouridylation guide RNA is composed of two box H/ACA snoRNA-like domains, Nucleic Acids Res., 2002, vol. 30, pp. 4643–4649.
Kolb, S.J., Battle, D.J., and Dreyfuss, G., Molecular functions of the SMN complex, J. Child. Neurol., 2007, vol. 22, no. 8, pp. 990–994.
Kołowerzo, A., Smolin-ski, D.J., and Bednarska, E., Poly(A) RNA a new component of Cajal bodies, Protoplasma, 2009, vol. 236, nos. 1–4, pp. 13–19.
Kopecny-, V., Biggiogera, M., Pivko, J., et al., The cell nucleus in early bovine and caprine preimplantation embryos: fine structural cytochemistry and immunoelectron microscopy, Eur. J. Cell Biol., 1996, vol. 70, no. 4, pp. 361–372.
Krasikova, A., Kulikova, T., Saifitdinova, A., et al., Centromeric protein bodies on avian lampbrush chromosomes contain a protein detectable with an antibody against DNA topoisomerase II, Chromosoma, 2004, vol. 113, no. 6, pp. 316–323.
Krasikova, A., Barbero, J.L., and Gaginskaya, E., Cohesion proteins are present in centromere protein bodies associated with avian lampbrush chromosomes, Chromosome Res., 2005, vol. 13, pp. 675–685.
Krasikova, A.V. and Gaginskaya, E.R., Organization of centromere regions of chromosomes in the lampbrush phase, Tsitologiya, 2010, vol. 52, no. 7, pp. 515–533.
Krasikova, A., Khodyuchenko, T., Maslova, A., et al., Threedimensional organisation of RNA-processing machinery in avian growing oocyte nucleus, Chromosome Res., 2012, vol. 20, no. 8, pp. 979–994.
Kumaran, R.I., Thakar, R., and Spector, D.L., Chromatin dynamics and gene positioning, Cell, 2008, vol. 132, no. 6, pp. 929–934.
Lefebvre, S., Bürglen, L., Reboullet, S., et al., Identification and characterization of a spinal muscular atrophy-determining gene, Cell, 1995, vol. 80, no. 1, pp. 155–165.
Lemm, I., Girard, C., Kuhn, A.N., et al., Ongoing U snRNP biogenesis is required for the integrity of Cajal bodies, Mol. Biol. Cell, 2006, vol. 17, no. 7, pp. 3221–3231.
Liu, Q. and Dreyfuss, G., A novel nuclear structure containing the survival of motor neurons protein, EMBO J., 1996, vol. 15, no. 14, pp. 3555–3365.
Liu, J.-L., Buszczak, M., and Gall, J.G., Nuclear bodies in the drosophila germinal vesicle, Chrom. Res., 2006a, vol. 14, no. 4, pp. 465–475.
Liu, J.L., Murphy, C., Buszczak, M., et al., The Drosophila melanogaster Cajal body, J. Cell Biol., 2006b, vol. 172, no. 6, pp. 875–884.
Liu, J.-L., Wu, Z., Nizami, Z., et al., Coilin is essential for Cajal body organization in Drosophila melanogaster, Mol. Biol. Cell, 2009, vol. 20, no. 6, pp. 1661–1670.
Machyna, M., Heyn, P., and Neugebauer, K.M., Cajal bodies: where form meets function, WIREs RNA, 2013, vol. 4, no. 1, pp. 17–34.
Makarova, J. A. and Kramerov, D. A., Noncoding RNAs, Biochemistry, 2007, vol. 72, no. 11, pp. 1427–1448.
Matera, A.G. and Shpargel, K.B., Pumping RNA: nuclear bodybuilding along the RNP pipeline, Curr. Opin. Cell Biol., 2006, vol. 18, no. 3, pp. 317–324.
Matera, A.G., Izaguire-Sierra, M., Praveen, K., et al., Nuclear bodies: random aggregates of sticky proteins or crucibles of macromolecular assembly?, Dev. Cell, 2009, vol. 17, no. 5, pp. 639–647.
Monneron, A. and Bernhard, W., Fine structural organization of the interphase nucleus in some mammalian cells, J. Ultrastruct. Res., 1969, vol. 27, no. 3, pp. 266–288.
Morgan, G.T., Lampbrush chromosomes and associated bodies: new insights into principles of nuclear structure and function, Chromosome Res., 2002, vol. 10, pp. 177–200.
Morimoto, M. and Boerkoel, C.F., The role of nuclear bodies in gene expression and disease, Biology (Basel), 2013, vol. 2, no. 3, pp. 976–1033.
Morris, G.E., The Cajal body, Biochim. Biophys. Acta, 2008, vol. 1783, no. 11, pp. 2108–2115.
Navascues, J., Bengoechea, R., and Tapia, O., SUMO-1 transiently localizes to Cajal bodies in mammalian neurons, J. Struct. Biol., vol. 163, no. 2, pp. 137–146.
Nizami, Z.F. and Gall, J.G., Pearls are novel Cajal body-like structures in the Xenopus germinal vesicle that are dependent on RNA pol III transcription, Chromosome Res., 2012, vol. 20, no. 8, pp. 953–969.
Nizami, Z.F., Deryusheva, S., and Gall, J.G., Cajal bodies and histone locus bodies in Drosophila and Xenopus, Cold Spring Harb. Symp. Quant. Biol., 2010a, vol. 75, pp. 313–320.
Nizami, Z.F., Deryusheva, S., and Gall, J.G., The Cajal body and histone locus body, Cold Spring Harb. Perspect. Biol., 2010b. doi: 10.1101/cshperspect.a000653
Novotny, I., Blažíková, M., Staněk, D., et al., In vivo kinetics of U4/U6-U5 tri-snRNP formation in Cajal bodies, Mol. Biol. Cell, 2011, vol. 22, no. 4, pp. 513–523.
Ochs, R.L., Stein, T.W., Jr., Andrade, L.E.C., et al., Formation of nuclear bodies in hepatocytes of estrogen-treated roosters, Mol. Biol. Cell, 1995, vol. 6, no. 3, pp. 345–356.
Okuwaki, M., The structure and functions of NPM1/nucleophsmin/B23, a multifunctional nucleolar acidic protein, J. Biochem., 2008, vol. 143, no. 4, pp. 441–448.
Pochukalina, G.N. and Parfenov, V.N., The nucleolus in oocytes of multylayer mouse follicles: topography of fibrillarin, RNA polymerase I and coilin, Tsitologiia, 2006, vol. 48, no. 8, pp. 641–652.
Pontes, O. and Pikaard, C.S., siRNA and miRNA processing: new functions for Cajal bodies, Curr. Opin. Genet. Dev., 2008, vol. 18, no. 2, pp. 197–203.
Rajendra, T.K., Praveen, K., and Matera, A.G., Genetic analysis of nuclear bodies: from nondeterministic to deterministic order, Cold Spring Harb. Symp. Quant. Biol., 2010, vol. 75, pp. 365–374.
Raška, I., Andrade, L.E.C., Ochs, R.L., et al., Immunological and ultrastructural studies of the nuclear coiled body with autoimmune antibodies, Exp. Cell Res., 1991, vol. 195, no. 1, pp. 27–37.
Richard, P., Darzacq, X., Bertrand, E., et al., A common sequence motif determines the Cajal body-specific localization of box H/ACA scaRNAs, EMBO J., 2003, vol. 22, no. 16, pp. 4283–4293.
Saifitdinova, A., Derjusheva, S., Krasikova, A., et al., Lampbrush chromosomes of the chaffinch (Fringilla coelebs L.), Chromosome Res., 2003, vol. 11, pp. 99–113.
Salzler, H.R., Tatomer, D.C., Malek, P.Y., et al., A sequence in the drosophila H3-H4 promoter triggers histone locus body assembly and biosynthesis of replication-coupled histone mRNAs, Dev. Cell, 2013, vol. 24, no. 6, pp. 623–634.
Schul, W., van Der Kraan, I., Matera, A.G., et al., Nuclear domains enriched in RNA 3′-processing factors associate with coiled bodies and histone genes in a cell cycledependent manner, Mol. Biol. Cell, 1999, vol. 10, no. 11, pp. 3815–3824.
Semashko, M.A., Rakitina, D.V., Gonzales, I., et al., Movement protein of hordeivirus interacts in vitro and in vivo with coilin, a major structural protein of Cajal bodies, Doklady Biochem. Biophys., 2012, vol. 442, pp. 57–60.
Shaw, D.J., Eggleton, P., and Young, P.J., Joining the dots: production, processing and targeting of U snRNP to nuclear bodies, Biochim. Biophys. Acta, 2008, vol. 1783, no. 11, pp. 2137–2144.
Shevtsov, S.P. and Dundr, M., Nucleation of nuclear bodies by RNA, Nat. Cell Biol., 2011, vol. 13, no. 2, pp. 167–173.
Shpargel, K.B., Ospina, J.K., Tucker, K.E., et al., Control of Cajal body number is mediated by the coilin C-terminus, J. Cell Sci., 2003, vol. 116, no. 2, pp. 303–312.
Sleeman, J., A regulatory role for CRM1 in the multi-directional trafficking of splicing snRNPs in the mammalian nucleus, J. Cell Sci., 2007, vol. 120, no. 9, pp. 1540–1550.
Sleeman, J.E., Ajuh, P., and Lamond, A.I., snRNP protein expression enhances the formation of Cajal bodies containing p-80 coilin and SMN, J. Cell Sci., 2001, vol. 114, no. 24, pp. 4407–4419.
Smolin-ski, D.J. and Kołowerzo, A., mRNA accumulation in the Cajal bodies of the diplotene larch microsporocyte, Chromosoma, 2012, vol. 121, no. 1, pp. 37–48.
Spector, D.L., Snapshot: cellular bodies, Cell, 2006, vol. 127, no. 5, p. 1071.
Stanek, D. and Neugebauer, K.M., The Cajal body: a meeting place for spliceosomal snrnps in the nuclear maze, Chromosoma, 2006, vol. 115, no. 5, pp. 343–354.
Stanek, D., Pridalová-Hnilicová, J., Novotný, I., et al., Spliceosomal small nuclear ribonucleoprotein particles repeatedly cycle through Cajal bodies. Mol Biol Cell, 2008, vol. 19, no. 6, pp. 2534–2543.
Stepanova, I.S., Bogolyubov, D.S., Skovorodkin, I.N., et al., Cajal bodies and interchromatin granule clusters in cricket oocytes: composition, dynamics and interactions, Cell Biol. Int., 2007, vol. 31, no. 3, pp. 203–214.
Stepanova, I.S., Bogolyubov, D.S., and Parfenov, V.N., Cajal bodies in insect oocytes. II. New data on the molecular composition of Cajal bodies in oocytes of the house cricket Acheta domesticus with special reference to interactions between Cajal bodies and interchromatin granule cluster, Tsitologiia, 2007, vol. 49, no. 1, pp. 5–20.
Tapia, O., Bengoechea, R., Palanca, A., et al., Reorganization of Cajal bodies and nucleolar targeting of coilin in motor neurons of type I spinal muscular atrophy, Histochem. Cell Biol., 2012, vol. 137, no. 5, pp. 657–667.
Tsvetkov, A., Alexandrova, O., Bogolyubov, D., et al., Nuclear bodies from cricket and mealworm oocytes contain splicing factors of pre-mRNA, Eur. J. Entomol., 1997, vol. 94, no. 3, pp. 393–407.
Tucker, T.E., Berciano, M.T., Jacobs, E.Y., et al., Residual Cajal bodies in coilin knockout mice fail to recruit Sm snRNPs and SMN, the spinal muscular atrophy gene product, J. Cell Biol., 2001, vol. 154, no. 2, pp. 293–307.
Venteicher, A.S., Abreu, E.B., Meng, Z., et al., A human telomerase holoenzyme protein required for Cajal body localization and telomere synthesis, Science, 2009, vol. 323, no. 5914, pp. 644–648.
Verheggen, C., Lafontaine, D.L., Samarsky, D., et al., Mammalian and yeast U3 snoRNPs are matured in specific and related nuclear compartments, EMBO J., 2002, vol. 21, no. 11, pp. 2736–2745.
Visa, N., Puvion-Dutilleul, F., Harper, F., et al., Intranuclear distribution of poly(A) RNA determined by electron microscope in situ hybridization, Exp. Cell Res., 1993, vol. 208, no. 1, pp. 19–34.
White, A.E., Burch, B.D., Yang, X.C., et al., Drosophila histone locus bodies form by hierarchical recruitment of components, J. Cell Biol., 2011, vol. 193, no. 4, pp. 677–694.
Will, C.L. and Lührmann, R., Spliceosomal U snRNP biogenesis, structure and function, Curr. Opin. Cell Biol., 2001, vol. 13, no. 3, pp. 290–301.
Wu, C.H. and Gall, J.G., U7 small nuclear RNA in c snurposomes of the Xenopus germinal vesicle, Proc. Natl. Acad. Sci. USA, 1993, vol. 90, no. 13, pp. 6257–6259.
Wu, Z., Murphy, C., and Gall, J.G., Human p80-coilin is targeted to sphere organelles in the amphibian germinal vesicle, Mol. Biol. Cell, 1994, vol. 5, no. 10, pp. 1119–1127.
Xie, J., Zhang, M., Zhou, T., et al., Sno/scaRNAbase: a curated database for small nucleolar and Cajal body-specific RNAs, Nucleic Acids Res., 2007, vol. 35, pp. 183–187.
Xu, H., Pillai, R.S., Azzouz, T.N., et al., The C-terminal domain of coilin interacts with Sm proteins and u snRNPs, Chromosoma, 2005, vol. 114, no. 3, pp. 155–166.
Yang, X.C., Sabath, I., Debski, J., et al., A complex containing the CPSF73 endonuclease and other polyadenylation factors associates with U7 snRNP and is recruited to histone pre-mRNA for 3′-end processing, Mol. Cell. Biol., 2013, vol. 33, no. 1, pp. 28–37.
Zatsepina, O., Baly, C., Chebrout, M., and Debey, P., The step-wise assembly of a functional nucleolus in preimplantation mouse embryos involves the Cajal (coiled) body, Dev. Biol., 2003, vol. 253, no. 1, pp. 66–83.
Zhu, Y., Tomlinson, R.L., Lukowiak, A.A., et al., Telomerase RNA accumulates in Cajal bodies in human cancer cells, Mol. Biol. Cell, 2004, vol. 15, no. 1, pp. 81–90.
Zimber, A., Nguyen, Q.D., and Gespach, C., Nuclear bodies and compartments: functional roles and cellular signalling in health and disease, Cell Signal., 2004, vol. 16, no. 10, pp. 1085–1104.
Original Russian Text © T.A. Khodyuchenko, A.V. Krasikova, 2014, published in Ontogenez, 2014, Vol. 45, No. 6, pp. 363–379.
About this article
Cite this article
Khodyuchenko, T.A., Krasikova, A.V. Cajal bodies and histone locus bodies: Molecular composition and function. Russ J Dev Biol 45, 297–312 (2014). https://doi.org/10.1134/S106236041406006X
- coilin-containing bodies
- histone locus bodies
- Cajal bodies
- nuclear bodies
- oocyte nucleus