scholarly journals Organ identity specification factor WGE localizes to the histone locus body and regulates histone expression to ensure genomic stability in Drosophila

2016 ◽  
Vol 21 (5) ◽  
pp. 442-456 ◽  
Author(s):  
Nao Ozawa ◽  
Hirofumi Furuhashi ◽  
Keita Masuko ◽  
Eriko Numao ◽  
Takashi Makino ◽  
...  
Keyword(s):  
Genomic Stability ◽  
Organ Identity ◽  
Histone Locus Body ◽  
Histone Locus

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 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 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.

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 Drosophila Histone Locus Body assembly and function involves multiple interactions

2020 ◽  
Author(s):  
Kaitlin P. Koreski ◽  
Leila E. Rieder ◽  
Lyndsey M. McLain ◽  
William F. Marzluff ◽  
Robert J. Duronio
Keyword(s):  
Gene Expression ◽  
Repeat Unit ◽  
Gene Array ◽  
Homozygous Deletion ◽  
Histone Gene ◽  
Histone Genes ◽  
Histone Mrna ◽  
Histone Gene Expression ◽  
Histone Locus Body ◽  
Histone Locus

AbstractThe histone locus body (HLB) assembles at replication-dependent (RD) histone loci and concentrates factors required for RD histone mRNA biosynthesis. The D. melanogaster genome has a single locus comprised of ∼100 copies of a tandemly arrayed repeat unit containing one copy of each of the 5 RD histone genes. To determine sequence elements required for D. melanogaster HLB formation and histone gene expression, we used transgenic gene arrays containing 12 copies of the histone repeat unit that functionally complement loss of the ∼200 endogenous RD histone genes. A 12x histone gene array in which all H3-H4 promoters were replaced with H2a-H2b promoters does not form an HLB or express high levels of RD histone mRNA in the presence of the endogenous histone genes. In contrast, this same transgenic array is active in HLB assembly and RD histone gene expression in the absence of the endogenous RD histone genes and rescues the lethality caused by homozygous deletion of the RD histone locus. The HLB formed in the absence of endogenous RD histone genes on the mutant 12x array contains all known factors present in the wild type HLB including CLAMP, which normally binds to GAGA repeats in the H3-H4 promoter. These data suggest that multiple protein-protein and/or protein-DNA interactions contribute to HLB formation, and that the large number of endogenous RD histone gene copies sequester available factor(s) from attenuated transgenic arrays, thereby preventing HLB formation and gene expression.

scholarly journals Muscle wasted: a novel component of the Drosophila histone locus body required for muscle integrity

2010 ◽  
Vol 123 (16) ◽  
pp. 2697-2707 ◽  
Author(s):  
S. Bulchand ◽  
S. D. Menon ◽  
S. E. George ◽  
W. Chia
Keyword(s):  
Histone Locus Body ◽  
Histone Locus

scholarly journals Nuclear bodies: Built to boost

2016 ◽  
Vol 213 (5) ◽  
pp. 509-511 ◽  
Author(s):  
Iain A. Sawyer ◽  
Miroslav Dundr
Keyword(s):  
Direct Evidence ◽  
Nuclear Bodies ◽  
Key Factors ◽  
Cell Biol ◽  
Histone Locus Body ◽  
Specific Reactions ◽  
Histone Locus

The classic archetypal function of nuclear bodies is to accelerate specific reactions within their crowded space. In this issue, Tatomer et al. (2016. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201504043) provide the first direct evidence that the histone locus body acts to concentrate key factors required for the proper processing of histone pre-mRNAs.

Sign in / Sign up

Export Citation Format

Share Document