Histone synthesis and turnover in alfalfa. Fast loss of highly acetylated replacement histone variant H3.2.

Waterborg, Jakob H.

doi:10.1016/s0021-9258(18)53482-7

Cited by 44 publications

(1 citation statement)

References 38 publications

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“…Interestingly, nucleosome turnover occurs over a longer timescale compatible with bursting, with multiple studies suggesting timescales of several minutes to hours [70][71][72][73][74]. Recent genome-wide studies have measured average nucleosome turnover time to be approximately 1 hour in the fly and in yeast [70,71].…”

Section: Acknowledgementsmentioning

confidence: 99%

A matter of time: Using dynamics and theory to uncover mechanisms of transcriptional bursting

Lammers,

Kim,

Zhao

et al. 2020

Preprint

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Eukaryotic transcription generally occurs in bursts of activity lasting minutes to hours; however, state-of-the-art measurements have revealed that many of the molecular processes that underlie bursting, such as transcription factor binding to DNA, unfold on timescales of seconds. This temporal disconnect lies at the heart of a broader challenge in physical biology of predicting transcriptional outcomes and cellular decision-making from the dynamics of underlying molecular processes. Here, we review how new dynamical information about the processes underlying transcriptional control can be combined with theoretical models that predict not only averaged transcriptional dynamics, but also their variability, to formulate testable hypotheses about the molecular mechanisms underlying transcriptional bursting and control.

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Section: Acknowledgementsmentioning

confidence: 99%

A matter of time: Using dynamics and theory to uncover mechanisms of transcriptional bursting

Lammers,

Kim,

Zhao

et al. 2020

Preprint

View full text Add to dashboard Cite

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Histone H3 transcript stability in alfalfa

1995

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The stability of histone H3 transcripts in alfalfa for replication-dependent and -independent gene variants was measured by northern analysis under conditions of inhibition of transcription and/or translation. Replication-dependent histone H3.1 transcripts were about three-fold less stable than the equally polyadenylated mRNA for replacement variant H3.2 histone. In actively growing suspension cultures treated with dactinomycin half-lives of 2 and 7 h were observed for H3.1 and H3.2 mRNAs, respectively. mRNA stabilities were also measured indirectly by histone protein synthesis. The translation inhibitor cycloheximide strongly increased mRNA levels for both histone H3 variants. The dependence of histone mRNA turnover on translation in animals also appears to exist in plants. The combination of inhibition of transcription and translation by dactinomycin and cycloheximide was used in an indirect assessment of H3 mRNA stability throughout the cell cycle in partially synchronized and cycle-arrested cultures. Destabilization of replication-dependent histone H3.1 mRNA was detected in non-S phase cells.

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Common features of analogous replacement histone H3 genes in animals and plants

Waterborg

Robertson

1996

J Mol Evol

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Phylogenetic analysis of histone H3 protein sequences demonstrates the independent origin of the replacement histone H3 genes in animals and in plants. Multiple introns in the replacement histone H3 genes of animals in a pattern distinct from that in plant replacement H3 genes supports this conclusion. It is suggested that replacement H3 genes arose at the same time that, independently, multicellular forms of animals and of plants evolved. Judged by the degree of invariant and functionally constrained amino acid positions, histones H3 and H4, which form together the tetramer kernel of the nucleosome, have co-evolved with equal rates of sequence divergence. Residues 31 and 87 in histone H3 are the only residues that consistently changed across each gene duplication event that created functional replacement histone H3 variant forms. Once changed, these residues have remained invariant across divergent speciation. This suggests that they are required to allow replacement histone H3 to participate in the assembly of nucleosomes in non-S-phase cells. The abundant occurrence of polypyrimidine sequences in the introns of all replacement H3 genes, and the replacement of an intron by a polypyrimidine motif upstream of the alfalfa replacement H3 gene, suggests a function. It is speculated that they may contribute to the characteristic cell-cycle-independent pattern of replacement histone H3 genes by binding nucleosome-excluding proteins.

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Histone synthesis and turnover in alfalfa. Fast loss of highly acetylated replacement histone variant H3.2.

Cited by 44 publications

References 38 publications

A matter of time: Using dynamics and theory to uncover mechanisms of transcriptional bursting

A matter of time: Using dynamics and theory to uncover mechanisms of transcriptional bursting

Histone H3 transcript stability in alfalfa

Common features of analogous replacement histone H3 genes in animals and plants

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