Antibodies specific to histone H1 inhibitin vitro transcription in isolated mammalian nuclei

Srebreva, Ljuba; Zlatanova, Jordanka

doi:10.1007/bf02385010

Cited by 4 publications

(2 citation statements)

References 24 publications

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“…For the majority of the nucleosomes, however, transcription occurs efficiently and is an indication that these structures are not immovable objects. Additional factors that may be involved in limiting disruption are proteins such as histone H1 (Srebreva & Zlatanova, 1992) or the HMG proteins (Bustin & Reeves, 1996) which were not included in our study. The level of transcription-induced stress that is obtainable in these in Vitro conditions may also be a limiting factor.…”

Section: Discussionmentioning

confidence: 99%

Measurement of the Frequency of Histone Displacement during the in Vitro Transcription of Nucleosomes: RNA Is a Competitor for These Histones

Peng

Jackson

1997

Biochemistry

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Transcription through tandemly arranged nucleosomes was studied to determine the frequency at which the nucleosomes would disrupt and cause displacement of the associated histones to a competitor DNA. In order to more effectively preserve topological effects, the template that was used in the in vitro transcription system was a large covalently, closed circular plasmid (8.9 kb). The plasmid contained two promoters for T7 RNA polymerase, each separated by 4.4 kb, and transcription was done in the presence of topoisomerase I at physiological ionic strength. Nucleosome disruption was observed at an approximate frequency of 1 in 4 nucleosomes such that after several rounds of transcription on the plasmid 80% of the nucleosomes were disrupted. Unexpectedly, all four histones were found associated with the RNA rather than the competitor DNA. The histones bound the competitor DNA only after removal of the RNA by RNase A treatment. By analyzing the topological state of the competitor DNA, it was observed that the majority of the histones that were displaced from the RNA were able to re-form nucleosomes. Additional experiments were done to determine the reasons for the preferential binding of histones to the newly synthesized RNA. It was found that the large molecular weight RNA binds histones with an approximate 100-fold greater affinity relative to DNA when at physiological ionic strength. Within the cell, this high-affinity binding would be expected to require cellular mechanisms to regulate the interaction of RNA with histones. The relatively high frequency of displacement of all four histones during transcription is higher than what is observed in vivo and suggests that additional factors are needed to regulate this displacement. These observations are discussed and compared with previous studies that have examined the process of transcription through nucleosomes.

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Section: Discussionmentioning

confidence: 99%

Measurement of the Frequency of Histone Displacement during the in Vitro Transcription of Nucleosomes: RNA Is a Competitor for These Histones

Peng

Jackson

1997

Biochemistry

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“…Among them, histone HI selectively inhibits transcription (3,4). However, an antibody specific to histone HI inhibits in-vitro transcription in isolated mammalian nuclei (5),…”

Section: Introductionmentioning

confidence: 99%

Interaction of polyadenylic acid (5′) with histone H1 or protamine

1996

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The interaction between polyadenylic acid (5′) (poly[A]) and histone (or protamine) was analyzed by electrophoretic retardation of poly[A]‐histone (or protamine) complex in agarose gel. The potency of interaction was protamine > histone H1, arginine‐rich histone > other histones. The catalytic subunit of cyclic AMP‐dependent protein kinase effectively decreased the electrophoretic retardation of poly[A]‐histone H1. The interaction between poly[A] and histone H1 was also detected by the drastically enhanced absorbance around 340 nm. The findings may implicate a regulatory role of histone H1 on mRNAs through its binding on poly[A] tails.

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Specific non-enzymatic glycation of the rat histone H1 nucleotide binding site in vitro in the presence of AlF4−. A putative mechanism for impaired chromatin function

Tarkka¹,

Yli-Mäyry

Mannermaa

et al. 1993

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Diseas

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Antibodies specific to histone H1 inhibitin vitro transcription in isolated mammalian nuclei

Cited by 4 publications

References 24 publications

Measurement of the Frequency of Histone Displacement during the in Vitro Transcription of Nucleosomes: RNA Is a Competitor for These Histones

Measurement of the Frequency of Histone Displacement during the in Vitro Transcription of Nucleosomes: RNA Is a Competitor for These Histones

Interaction of polyadenylic acid (5′) with histone H1 or protamine

Specific non-enzymatic glycation of the rat histone H1 nucleotide binding site in vitro in the presence of AlF4−. A putative mechanism for impaired chromatin function

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