scholarly journals Monocistronic transcription is the physiological mechanism of sea urchin embryonic histone gene expression.

1981 ◽  
Vol 1 (7) ◽  
pp. 661-671 ◽  
Author(s):  
A Mauron ◽  
S Levy ◽  
G Childs ◽  
L Kedes
Keyword(s):  
Gene Expression ◽  
Steady State ◽  
Early Development ◽  
Sea Urchin ◽  
Dna Sequences ◽  
Messenger Rna ◽  
Physiological Mechanism ◽  
Histone Gene ◽  
Histone Genes ◽  
Histone Gene Expression

We have examined histone gene expression during the early stages of sea urchin embryogenesis. The five histone genes expressed at that time are contained in tandem repetitive segments. It has been suggested that adjacent coding regions and their intervening spacer sequences are transcribed into large polycistronic messenger ribonucleic acid (RNA) precursors. We have subcloned into pBR322 deoxyribonucleic acid (DNA) sequences mapping either in the coding region, the 5' spacer, or the 3' spacer of the H2B histone gene. These clones were used to produce radioiodinated hybridization probes. We measured the steady-state quantity of H2B messenger RNA as well as spacer-specific RNA in the total RNA from embryos taken at various stages of development from fertilization to hatching of blastulae (0 to 22 h post-fertilization). Small amounts of RNA hybridizing to both spacer probes could be found. However, we show that these RNAs form mismatched hybrids with the spacer DNA and therefore cannot originate from the spacers present in the histone genes. We conclude that there is no detectable transcription of the spacer regions on either side of the H2B histone gene. The detection limit for RNA complementary to the 5' spacer sequence corresponds to a maximum of about three RNA molecules per cell, an amount shown to be far less than the projected steady-state pool size of a putative polycistronic transcript, if such a precursor were to be the obligatory transcript of the histone genes. (This conclusion was derived by using the known rates of production of H2B mRNA throughout early development [R. E. Maxson and F. H. Wilt, Dev. Biol., in press].) The physiologically relevant transcript of the histone genes in early development is therefore monocistronic and probably identical to the messenger RNA itself.

scholarly journals Monocistronic transcription is the physiological mechanism of sea urchin embryonic histone gene expression

1981 ◽  
Vol 1 (7) ◽  
pp. 661-671
Author(s):  
A Mauron ◽  
S Levy ◽  
G Childs ◽  
L Kedes
Keyword(s):  
Gene Expression ◽  
Steady State ◽  
Early Development ◽  
Sea Urchin ◽  
Dna Sequences ◽  
Messenger Rna ◽  
Physiological Mechanism ◽  
Histone Gene ◽  
Histone Genes ◽  
Histone Gene Expression

We have examined histone gene expression during the early stages of sea urchin embryogenesis. The five histone genes expressed at that time are contained in tandem repetitive segments. It has been suggested that adjacent coding regions and their intervening spacer sequences are transcribed into large polycistronic messenger ribonucleic acid (RNA) precursors. We have subcloned into pBR322 deoxyribonucleic acid (DNA) sequences mapping either in the coding region, the 5' spacer, or the 3' spacer of the H2B histone gene. These clones were used to produce radioiodinated hybridization probes. We measured the steady-state quantity of H2B messenger RNA as well as spacer-specific RNA in the total RNA from embryos taken at various stages of development from fertilization to hatching of blastulae (0 to 22 h post-fertilization). Small amounts of RNA hybridizing to both spacer probes could be found. However, we show that these RNAs form mismatched hybrids with the spacer DNA and therefore cannot originate from the spacers present in the histone genes. We conclude that there is no detectable transcription of the spacer regions on either side of the H2B histone gene. The detection limit for RNA complementary to the 5' spacer sequence corresponds to a maximum of about three RNA molecules per cell, an amount shown to be far less than the projected steady-state pool size of a putative polycistronic transcript, if such a precursor were to be the obligatory transcript of the histone genes. (This conclusion was derived by using the known rates of production of H2B mRNA throughout early development [R. E. Maxson and F. H. Wilt, Dev. Biol., in press].) The physiologically relevant transcript of the histone genes in early development is therefore monocistronic and probably identical to the messenger RNA itself.

Sea urchin histone genes: the beginning and end of the message

1984 ◽  
Vol 307 (1132) ◽  
pp. 293-295
Keyword(s):  
Gene Expression ◽  
Cell Cycle ◽  
Gene Transcription ◽  
Sea Urchin ◽  
Nuclear Dna ◽  
Gene Clusters ◽  
Histone Gene ◽  
Histone Genes ◽  
Histone Gene Expression ◽  
Histone Gene Transcription

The purpose of studies on the regulation of histone gene expression is to explain, for instance, how histone proteins arise in defined stoichiometric relationships in the chromatin, how transcription of histone genes is regulated in the cell cycle and how during the development of some species, histone variant genes are activated sequentially. The control of histone gene expression has m any interesting facets. One is struck by the major differences in balance and importance of the various regulatory mechanisms as they become apparent from investigations in m any laboratories. For example, in yeast, histone gene transcription is tightly coupled to the cell cycle, and the amounts of histone synthesized are determined largely by regulation of histone m RN A turnover (Hereford & Osley 1981). At the other extreme, there is the example of the maturing frog oöcyte where histone m RN A synthesis is uncoupled from DNA synthesis and yields pools of histone 1000-fold in excess of nuclear DNA mass (reviewed by Woodland 1980). Recent reports suggest that even the details of histone gene transcription may vary during the development of the species. The tandem histone gene clusters of sea urchin (G. Spinelli, unpublished results) and frog oocytes are transcribed polycistronically at least at some stages of their development (J. Gall, personal communication), whereas histone gene clusters of the cleaving sea urchin embryos appear to be transcribed monocistronically (Mauron et al. 1981). Finally, in the early embryo the partitioning of the m RN A between nucleus and cytoplasm may be also a regulative process (DeLeon al. 1983).

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 Effect of adenovirus infection on expression of human histone genes.

1984 ◽  
Vol 4 (7) ◽  
pp. 1363-1371 ◽  
Author(s):  
S J Flint ◽  
M A Plumb ◽  
U C Yang ◽  
G S Stein ◽  
J L Stein
Keyword(s):  
Gene Expression ◽  
Dna Synthesis ◽  
Histone Gene ◽  
Adenovirus Infection ◽  
Histone Genes ◽  
Histone Mrna ◽  
Intact Cells ◽  
Mrna Species ◽  
Histone Gene Expression ◽  
Infected Cells

The influence of adenovirus type 2 infection of HeLa cells upon expression of human histone genes was examined as a function of the period of infection. Histone RNA synthesis was assayed after run-off transcription in nuclei isolated from mock-infected cells and after various periods of adenovirus infection. Histone protein synthesis was measured by [3H]leucine labeling of intact cells and fluorography of electrophoretically fractionated nuclear and cytoplasmic proteins. The cellular representation of RNA species complementary to more than 13 different human histone genes was determined by RNA blot analysis of total cellular, nuclear or cytoplasmic RNA by using a series of 32P-labeled cloned human histone genes as hybridization probes and also by analysis of 3H-labeled histone mRNA species synthesized in intact cells. By 18 h after infection, HeLa cell DNA synthesis and all parameters of histone gene expression, including transcription and the nuclear and cytoplasmic concentrations of core and H1 mRNA species, were reduced to less than 5 to 10% of the control values. By contrast, transcription and processing of other cellular mRNA sequences have been shown to continue throughout this period of infection. The early period of adenovirus infection was marked by an inhibition of transcription of histone genes that accompanied the reduction in rate of HeLa cell DNA synthesis. These results suggest that the adenovirus-induced inhibition of histone gene expression is mediated in part at the transcriptional level. However, the persistence of histone mRNA species at concentrations comparable to those of mock-infected control cells during the early phase of the infection, despite a reduction in histone gene transcription and histone protein synthesis, implies that histone gene expression is also regulated post-transcriptionally in adenovirus-infected cells. These results suggest that the tight coupling between histone mRNA concentrations and the rate of cellular DNA synthesis, observed when DNA replication is inhibited by a variety of drugs, is not maintained after adenovirus infection.

Kinetics of histone gene expression during early development of Xenopus laevis

1988 ◽  
Vol 135 (2) ◽  
pp. 139-167 ◽  
Author(s):  
Johanna G. Koster ◽  
Olivier H.J. Destrée ◽  
Hans V. Westerhoff
Keyword(s):  
Gene Expression ◽  
Xenopus Laevis ◽  
Early Development ◽  
Histone Gene ◽  
Histone Gene Expression ◽  
Kinetics Of

scholarly journals Analysis of histone gene expression during the cell cycle in HeLa cells by using cloned human histone genes.

1982 ◽  
Vol 79 (3) ◽  
pp. 749-753 ◽  
Author(s):  
R. Rickles ◽  
F. Marashi ◽  
F. Sierra ◽  
S. Clark ◽  
J. Wells ◽  
...  
Keyword(s):  
Gene Expression ◽  
Cell Cycle ◽  
Hela Cells ◽  
Histone Gene ◽  
Histone Genes ◽  
Histone Gene Expression

Are multiple checkpoint mediators involved in a checkpoint linking histone gene expression with DNA replication?

2007 ◽  
Vol 35 (5) ◽  
pp. 1369-1371 ◽  
Author(s):  
B. Müller ◽  
J. Blackburn ◽  
C. Feijoo ◽  
X. Zhao ◽  
C. Smythe
Keyword(s):  
Gene Expression ◽  
Dna Replication ◽  
Transcriptional Control ◽  
Molecular Mechanisms ◽  
S Phase ◽  
Histone Gene ◽  
Control Mechanisms ◽  
Histone Genes ◽  
Checkpoint Kinases ◽  
Histone Gene Expression

In metazoans, accurate replication of chromosomes is ensured by the coupling of DNA synthesis to the synthesis of histone proteins. Expression of replication-dependent histone genes is restricted to S-phase by a combination of cell cycle-regulated transcriptional and post-transcriptional control mechanisms and is linked to DNA replication by a poorly understood mechanism involving checkpoint kinases [Su, Gao, Schneider, Helt, Weiss, O'Reilly, Bohmann and Zhao (2004) EMBO J. 23, 1133–1143; Kaygun and Marzluff (2005) Nat. Struct. Mol. Biol. 12, 794–800]. Here we propose a model for the molecular mechanisms that link these two important processes within S-phase, and propose roles for multiple checkpoints in this mechanism.

scholarly journals Replication stress-induced alternative mRNA splicing alters properties of the histone RNA-binding protein HBP/SLBP: a key factor in the control of histone gene expression

2013 ◽  
Vol 33 (5) ◽  
Author(s):  
Alexander M. J. Rattray ◽  
Pamela Nicholson ◽  
Berndt Müller
Keyword(s):  
Gene Expression ◽  
Alternative Splicing ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Replication Stress ◽  
S Phase ◽  
Histone Gene ◽  
Histone Genes ◽  
Histone Gene Expression

Animal replication-dependent histone genes produce histone proteins for the packaging of newly replicated genomic DNA. The expression of these histone genes occurs during S phase and is linked to DNA replication via S-phase checkpoints. The histone RNA-binding protein HBP/SLBP (hairpin-binding protein/stem-loop binding protein), an essential regulator of histone gene expression, binds to the conserved hairpin structure located in the 3′UTR (untranslated region) of histone mRNA and participates in histone pre-mRNA processing, translation and histone mRNA degradation. Here, we report the accumulation of alternatively spliced HBP/SLBP transcripts lacking exons 2 and/or 3 in HeLa cells exposed to replication stress. We also detected a shorter HBP/SLBP protein isoform under these conditions that can be accounted for by alternative splicing of HBP/SLBP mRNA. HBP/SLBP mRNA alternative splicing returned to low levels again upon removal of replication stress and was abrogated by caffeine, suggesting the involvement of checkpoint kinases. Analysis of HBP/SLBP cellular localization using GFP (green fluorescent protein) fusion proteins revealed that HBP/SLBP protein and isoforms lacking the domains encoded by exon 2 and exons 2 and 3 were found in the nucleus and cytoplasm, whereas HBP/SLBP lacking the domain encoded by exon 3 was predominantly localised to the nucleus. This isoform lacks the conserved region important for protein–protein interaction with the CTIF [CBP80/20 (cap-binding protein 80/20)]-dependent initiation translation factor and the eIF4E (eukaryotic initiation factor 4E)-dependent translation factor SLIP1/MIF4GD (SLBP-interacting protein 1/MIF4G domain). Consistent with this, we have previously demonstrated that this region is required for the function of HBP/SLBP in cap-dependent translation. In conclusion, alternative splicing allows the synthesis of HBP/SLBP isoforms with different properties that may be important for regulating HBP/SLBP functions during replication stress.

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