scholarly journals The Cajal Body and Histone Locus Body

2010 ◽  
Vol 2 (7) ◽  
pp. a000653-a000653 ◽  
Author(s):  
Z. Nizami ◽  
S. Deryusheva ◽  
J. G. Gall
Keyword(s):  
Cajal Body ◽  
Histone Locus Body ◽  
Histone Locus

scholarly journals Developmental and Cell Cycle Regulation of the Drosophila Histone Locus Body

2007 ◽  
Vol 18 (7) ◽  
pp. 2491-2502 ◽  
Author(s):  
Anne E. White ◽  
Michelle E. Leslie ◽  
Brian R. Calvi ◽  
William F. Marzluff ◽  
Robert J. Duronio
Keyword(s):  
Cyclin E ◽  
Early Embryo ◽  
Cajal Body ◽  
Histone Mrna ◽  
Small Nuclear Ribonucleoprotein ◽  
Histone Locus Body ◽  
Histone Transcription ◽  
Nuclear Ribonucleoprotein ◽  
Histone Locus ◽  
Cycle Regulation

Cyclin E/Cdk2 is necessary for replication-dependent histone mRNA biosynthesis, but how it controls this process in early development is unknown. We show that in Drosophila embryos the MPM-2 monoclonal antibody, raised against a phosphoepitope from human mitotic cells, detects Cyclin E/Cdk2-dependent nuclear foci that colocalize with nascent histone transcripts. These foci are coincident with the histone locus body (HLB), a Cajal body-like nuclear structure associated with the histone locus and enriched in histone pre-mRNA processing factors such as Lsm11, a core component of the U7 small nuclear ribonucleoprotein. Using MPM-2 and anti-Lsm11 antibodies, we demonstrate that the HLB is absent in the early embryo and occurs when zygotic histone transcription begins during nuclear cycle 11. Whereas the HLB is found in all cells after its formation, MPM-2 labels the HLB only in cells with active Cyclin E/Cdk2. MPM-2 and Lsm11 foci are present in embryos lacking the histone locus, and MPM-2 foci are present in U7 mutants, which cannot correctly process histone pre-mRNA. These data indicate that MPM-2 recognizes a Cdk2-regulated protein that assembles into the HLB independently of histone mRNA biosynthesis. HLB foci are present in histone deletion embryos, although the MPM-2 foci are smaller, and some Lsm11 foci are not associated with MPM-2 foci, suggesting that the histone locus is important for HLB integrity.

scholarly journals A Sequence in the Drosophila H3-H4 Promoter Triggers Histone Locus Body Assembly and Biosynthesis of Replication-Coupled Histone mRNAs

2013 ◽  
Vol 24 (6) ◽  
pp. 623-634 ◽  
Author(s):  
Harmony R. Salzler ◽  
Deirdre C. Tatomer ◽  
Pamela Y. Malek ◽  
Stephen L. McDaniel ◽  
Anna N. Orlando ◽  
...  
Keyword(s):  
Histone Mrnas ◽  
Histone Locus Body ◽  
Histone Locus

scholarly journals Drosophila Symplekin localizes dynamically to the histone locus body and tricellular junctions

Nucleus ◽  
2014 ◽  
Vol 5 (6) ◽  
pp. 613-625 ◽  
Author(s):  
Deirdre C Tatomer ◽  
Lindsay F Rizzardi ◽  
Kaitlin P Curry ◽  
Alison M Witkowski ◽  
William F Marzluff ◽  
...  
Keyword(s):  
Histone Locus Body ◽  
Histone Locus

scholarly journals Concentrating pre-mRNA processing factors in the histone locus body facilitates efficient histone mRNA biogenesis

2016 ◽  
Vol 213 (5) ◽  
pp. 557-570 ◽  
Author(s):  
Deirdre C. Tatomer ◽  
Esteban Terzo ◽  
Kaitlin P. Curry ◽  
Harmony Salzler ◽  
Ivan Sabath ◽  
...  
Keyword(s):  
Messenger Rna ◽  
Mrna Processing ◽  
Histone Mrna ◽  
Histone Mrnas ◽  
Assembly Factor ◽  
U7 Snrnp ◽  
Histone Locus Body ◽  
Histone Locus ◽  
Processing Factors

The histone locus body (HLB) assembles at replication-dependent histone genes and concentrates factors required for histone messenger RNA (mRNA) biosynthesis. FLASH (Flice-associated huge protein) and U7 small nuclear RNP (snRNP) are HLB components that participate in 3′ processing of the nonpolyadenylated histone mRNAs by recruiting the endonuclease CPSF-73 to histone pre-mRNA. Using transgenes to complement a FLASH mutant, we show that distinct domains of FLASH involved in U7 snRNP binding, histone pre-mRNA cleavage, and HLB localization are all required for proper FLASH function in vivo. By genetically manipulating HLB composition using mutations in FLASH, mutations in the HLB assembly factor Mxc, or depletion of the variant histone H2aV, we find that failure to concentrate FLASH and/or U7 snRNP in the HLB impairs histone pre-mRNA processing. This failure results in accumulation of small amounts of polyadenylated histone mRNA and nascent read-through transcripts at the histone locus. Thus, the HLB concentrates FLASH and U7 snRNP, promoting efficient histone mRNA biosynthesis and coupling 3′ end processing with transcription termination.

scholarly journals Coilin Is Essential for Cajal Body Organization in Drosophila melanogaster

2009 ◽  
Vol 20 (6) ◽  
pp. 1661-1670 ◽  
Author(s):  
Ji-Long Liu ◽  
Zheng'an Wu ◽  
Zehra Nizami ◽  
Svetlana Deryusheva ◽  
T.K. Rajendra ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Survival Motor Neuron ◽  
Cajal Body ◽  
Homology Search ◽  
Insertion Mutant ◽  
Small Nuclear Rna ◽  
Histone Locus Bodies ◽  
Piggybac Insertion ◽  
Smn Protein ◽  
Histone Locus

Cajal bodies (CBs) are nuclear organelles that occur in a variety of organisms, including vertebrates, insects, and plants. They are most often identified with antibodies against the marker protein coilin. Because the amino acid sequence of coilin is not strongly conserved evolutionarily, coilin orthologues have been difficult to recognize by homology search. Here, we report the identification of Drosophila melanogaster coilin and describe its distribution in tissues of the fly. Surprisingly, we found coilin not only in CBs but also in histone locus bodies (HLBs), calling into question the use of coilin as an exclusive marker for CBs. We analyzed two null mutants in the coilin gene and a piggyBac insertion mutant, which leads to specific loss of coilin from the germline. All three mutants are homozygous viable and fertile. Cells that lack coilin also lack distinct foci of other CB markers, including fibrillarin, the survival motor neuron (SMN) protein, U2 small nuclear RNA (snRNA), U5 snRNA, and the small CB-specific (sca) RNA U85. However, HLBs are not obviously affected in coilin-null flies. Thus, coilin is required for normal CB organization in Drosophila but is not essential for viability or production of functional gametes.

scholarly journals The Drosophila melanogaster Cajal body

2006 ◽  
Vol 172 (6) ◽  
pp. 875-884 ◽  
Author(s):  
Ji-Long Liu ◽  
Christine Murphy ◽  
Michael Buszczak ◽  
Sarah Clatterbuck ◽  
Robyn Goodman ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Motor Neurons ◽  
Nuclear Body ◽  
Nuclear Bodies ◽  
Cajal Body ◽  
Small Nuclear Rna ◽  
Nuclear Rna ◽  
Survival Of Motor Neurons ◽  
And Function ◽  
Histone Locus

Cajal bodies (CBs) are nuclear organelles that are usually identified by the marker protein p80-coilin. Because no orthologue of coilin is known in Drosophila melanogaster, we identified D. melanogaster CBs using probes for other components that are relatively diagnostic for CBs in vertebrate cells. U85 small CB–specific RNA, U2 small nuclear RNA, the survival of motor neurons protein, and fibrillarin occur together in a nuclear body that is closely associated with the nucleolus. Based on its similarity to CBs in other organisms, we refer to this structure as the D. melanogaster CB. Surprisingly, the D. melanogaster U7 small nuclear RNP resides in a separate nuclear body, which we call the histone locus body (HLB). The HLB is invariably colocalized with the histone gene locus. Thus, canonical CB components are distributed into at least two nuclear bodies in D. melanogaster. The identification of these nuclear bodies now permits a broad range of questions to be asked about CB structure and function in a genetically tractable organism.

scholarly journals Drosophila Prp40 localizes to the histone locus body and regulates gene transcription and development

2020 ◽  
Vol 133 (7) ◽  
pp. jcs239509 ◽  
Author(s):  
Silvia Prieto-Sánchez ◽  
Cristina Moreno-Castro ◽  
Cristina Hernández-Munain ◽  
Carlos Suñé
Keyword(s):  
Gene Transcription ◽  
Histone Locus Body ◽  
Histone Locus

scholarly journals Integrator Subunit 4 is a ‘Symplekin-like’ Scaffold that Associates with INTS9/11 to Form the Integrator Cleavage Module

2017 ◽  
Author(s):  
Todd R. Albrecht ◽  
Sergey P. Shevtsov ◽  
Lauren G. Mascibroda ◽  
Natoya J. Peart ◽  
Iain A. Sawyer ◽  
...  
Keyword(s):  
Rna Polymerase Ii ◽  
Cajal Body ◽  
Catalytic Core ◽  
Histone Locus Bodies ◽  
Transcriptional Regulatory ◽  
Significant Homology ◽  
Regulatory Complex ◽  
Cleavage And Polyadenylation ◽  
Histone Locus ◽  
Β Sheet

AbstractIntegrator (INT) is a transcriptional regulatory complex associated with RNA polymerase II that is required for the 3’-end processing of both UsnRNAs and enhancer RNAs. Integrator subunits 9 (INTS9) and INTS11 constitute the catalytic core of INT and are paralogues of the cleavage and polyadenylation specificity factors CPSF100 and CPSF73. While CPSF73/100 are known to associate with a third protein called Symplekin, there is no paralog of Symplekin within INT raising the question of how INTS9/11 associate with the other INT subunits. Here, we have identified that INTS4 is a specific and conserved interaction partner of INTS9/11 that does not interact with either subunit individually. Although INTS4 has no significant homology with Symplekin, it possesses N-terminal HEAT repeats similar to Symplekin but also contains a β-sheet rich C-terminal region, both of which are important to bind INTS9/11. We assess three functions of INT including UsnRNA 3’-end processing, maintenance of Cajal body integrity, and formation of histone locus bodies to conclude that INTS4/9/11 are the most critical of the INT subunits for UsnRNA biogenesis. Altogether, these results indicate that INTS4/9/11 compose a heterotrimeric complex that likely represents the Integrator ‘cleavage module’ responsible for its endonucleolytic activity.

scholarly journals Distinct self-interaction domains promote Multi Sex Combs accumulation in and formation of the Drosophila histone locus body

2015 ◽  
Vol 26 (8) ◽  
pp. 1559-1574 ◽  
Author(s):  
Esteban A. Terzo ◽  
Shawn M. Lyons ◽  
John S. Poulton ◽  
Brenda R. S. Temple ◽  
William F. Marzluff ◽  
...  
Keyword(s):  
Amino Acids ◽  
Nuclear Bodies ◽  
Confocal Imaging ◽  
Histone Mrna ◽  
Mrna Accumulation ◽  
Sex Combs ◽  
Histone Locus Body ◽  
Histone Locus ◽  
Multiple Domains

Nuclear bodies (NBs) are structures that concentrate proteins, RNAs, and ribonucleoproteins that perform functions essential to gene expression. How NBs assemble is not well understood. We studied the Drosophila histone locus body (HLB), a NB that concentrates factors required for histone mRNA biosynthesis at the replication-dependent histone gene locus. We coupled biochemical analysis with confocal imaging of both fixed and live tissues to demonstrate that the Drosophila Multi Sex Combs (Mxc) protein contains multiple domains necessary for HLB assembly. An important feature of this assembly process is the self-interaction of Mxc via two conserved N-terminal domains: a LisH domain and a novel self-interaction facilitator (SIF) domain immediately downstream of the LisH domain. Molecular modeling suggests that the LisH and SIF domains directly interact, and mutation of either the LisH or the SIF domain severely impairs Mxc function in vivo, resulting in reduced histone mRNA accumulation. A region of Mxc between amino acids 721 and 1481 is also necessary for HLB assembly independent of the LisH and SIF domains. Finally, the C-terminal 195 amino acids of Mxc are required for recruiting FLASH, an essential histone mRNA-processing factor, to the HLB. We conclude that multiple domains of the Mxc protein promote HLB assembly in order to concentrate factors required for histone mRNA biosynthesis.

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