scholarly journals Drosophila histone locus body assembly and function involves multiple interactions

2020 ◽  
Vol 31 (14) ◽  
pp. 1525-1537
Author(s):  
Kaitlin P. Koreski ◽  
Leila E. Rieder ◽  
Lyndsey M. McLain ◽  
Ashlesha Chaubal ◽  
William F. Marzluff ◽  
...  
Keyword(s):  
Gene Expression ◽  
Gene Replacement ◽  
Histone Gene ◽  
Gene Arrays ◽  
Multiple Factors ◽  
Histone Gene Expression ◽  
Number Of Genes ◽  
And Function ◽  
Histone Locus ◽  
Multiple Interactions

By using a histone gene replacement platform in Drosophila, we show that interactions among multiple factors contribute to HLB formation, and that the large number of genes at the endogenous histone locus sequesters available factors from attenuated transgenic histone gene arrays, thereby preventing HLB formation and histone gene expression from these arrays.

scholarly journals Super resolution light microscopy of the Drosophila Histone Locus Body reveals a core-shell organization associated with expression of replication dependent histone genes

2021 ◽  
pp. mbc.E20-10-0645
Author(s):  
James P. Kemp ◽  
Xiao-Cui Yang ◽  
Zbigniew Dominski ◽  
William F. Marzluff ◽  
Robert J. Duronio
Keyword(s):  
Gene Expression ◽  
Gene Transcription ◽  
Nuclear Body ◽  
Histone Gene ◽  
Core Shell ◽  
Histone Genes ◽  
The Core ◽  
Histone Gene Expression ◽  
Histone Locus ◽  
Histone Gene Transcription

The Histone Locus Body (HLB) is an evolutionarily conserved nuclear body that regulates the transcription and processing of replication-dependent (RD) histone mRNAs, which are the only eukaryotic mRNAs lacking a poly-A tail. Many nuclear bodies contain distinct domains, but how internal organization is related to nuclear body function is not fully understood. Here, we demonstrate using structured illumination microscopy that Drosophila HLBs have a “core-shell” organization in which the internal core contains transcriptionally active RD histone genes. The N-terminus of Mxc, which contains a domain required for Mxc oligomerization, HLB assembly, and RD histone gene expression, is enriched in the HLB core. In contrast, the C-terminus of Mxc is enriched in the HLB outer shell as is FLASH, a component of the active U7 snRNP that co-transcriptionally cleaves RD histone pre-mRNA. Consistent with these results, we show biochemically that FLASH binds directly to the Mxc C-terminal region. In the rapid S-M nuclear cycles of syncytial blastoderm Drosophila embryos, the HLB disassembles at mitosis and reassembles the core-shell arrangement as histone gene transcription is activated immediately after mitosis. Thus, the core-shell organization is coupled to zygotic histone gene transcription, revealing a link between HLB internal organization and RD histone gene expression.

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 ALS-linked FUS mutants affect the localization of U7 snRNP and replication-dependent histone gene expression in human cells

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Ankur Gadgil ◽  
Agnieszka Walczak ◽  
Agata Stępień ◽  
Jonas Mechtersheimer ◽  
Agnes Lumi Nishimura ◽  
...  
Keyword(s):  
Gene Expression ◽  
Rna Polymerase Ii ◽  
Histone Gene ◽  
Cytoplasmic Inclusions ◽  
Cellular Models ◽  
Histone Gene Expression ◽  
Genes Encoding ◽  
U7 Snrnp ◽  
Processing Event ◽  
Fus Protein

AbstractGenes encoding replication-dependent histones lack introns, and the mRNAs produced are a unique class of RNA polymerase II transcripts in eukaryotic cells that do not end in a polyadenylated tail. Mature mRNAs are thus formed by a single endonucleolytic cleavage that releases the pre-mRNA from the DNA and is the only processing event necessary. U7 snRNP is one of the key factors that determines the cleavage site within the 3ʹUTR of replication-dependent histone pre-mRNAs. We have previously showed that the FUS protein interacts with U7 snRNA/snRNP and regulates the expression of histone genes by stimulating transcription and 3ʹ end maturation. Mutations in the FUS gene first identified in patients with amyotrophic lateral sclerosis (ALS) lead to the accumulation of the FUS protein in cytoplasmic inclusions. Here, we report that mutations in FUS lead to disruption of the transcriptional activity of FUS and mislocalization of U7 snRNA/snRNP in cytoplasmic aggregates in cellular models and primary neurons. As a consequence, decreased transcriptional efficiency and aberrant 3ʹ end processing of histone pre-mRNAs were observed. This study highlights for the first time the deregulation of replication-dependent histone gene expression and its involvement in ALS.

Cell-cycle regulation of histone gene expression

Cell ◽  
1986 ◽  
Vol 45 (4) ◽  
pp. 471-472 ◽  
Author(s):  
Daniel Schümperli
Keyword(s):  
Gene Expression ◽  
Cell Cycle ◽  
Cell Cycle Regulation ◽  
Histone Gene ◽  
Histone Gene Expression ◽  
Cycle Regulation

Histone Gene Expression and Chromatin Structure during Spermatogenesis

1997 ◽  
pp. 37-48 ◽  
Author(s):  
D. Doenecke ◽  
B. Drabent ◽  
C. Bode ◽  
B. Bramlage ◽  
K. Franke ◽  
...  
Keyword(s):  
Gene Expression ◽  
Chromatin Structure ◽  
Histone Gene ◽  
Histone Gene Expression

scholarly journals Epigenetic Control of Cell Cycle-Dependent Histone Gene Expression Is a Principal Component of the Abbreviated Pluripotent Cell Cycle

2012 ◽  
Vol 32 (19) ◽  
pp. 3860-3871 ◽  
Author(s):  
R. Medina ◽  
P. N. Ghule ◽  
F. Cruzat ◽  
A. R. Barutcu ◽  
M. Montecino ◽  
...  
Keyword(s):  
Gene Expression ◽  
Cell Cycle ◽  
Principal Component ◽  
Histone Gene ◽  
Pluripotent Cell ◽  
Epigenetic Control ◽  
Histone Gene Expression ◽  
Cycle Dependent
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