+ Site Statistics
References:
54,258,434
Abstracts:
29,560,870
PMIDs:
28,072,757
+ Search Articles
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ PDF Full Text
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Translate
+ Recently Requested

Nuclear matrix, dynamic histone acetylation and transcriptionally active chromatin



Nuclear matrix, dynamic histone acetylation and transcriptionally active chromatin



Molecular Biology Reports. 24(3): 207



The nuclear matrix, the RNA-protein skeleton of the nucleus, has a role in the organization and function of nuclear DNA. Nuclear processes associated with the nuclear matrix include transcription, replication and dynamic histone acetylation. Nuclear matrix proteins, which are tissue and cell type specific, are altered with transformation and state of differentiation. Transcription factors are associated with the nuclear matrix, with the spectra of nuclear matrix bound factors being cell type specific. There is compelling evidence that the transcription machinery is anchored to the nuclear matrix, and the chromatin fiber is spooled through this complex. Transcriptionally active chromatin domains are associated with dynamically acetylated histones. The energy exhaustive process of dynamic histone acetylation has several functions. Acetylation of the N-terminal tails of the core histones alters nucleosome and higher order chromatin structure, aiding transcriptional elongation and facilitating the binding of transcription factors to nucleosomes associated with regulatory DNA sequences. Histone acetylation can manipulate the interactions of regulatory proteins that bind to the N-terminal tails of the core histones. Lastly, dynamic acetylation may contribute to the transient attachment of transcriptionally active chromatin to the nuclear matrix. Reversible histone acetylation is catalyzed by histone acetyltransferase and deacetylase, enzymes associated with the nuclear matrix. The recent isolation and characterization of histone acetyltransferase and deacetylase reveals that these enzymes are related to transcriptional regulators, providing us with new insights about how these enzymes are targeted to nuclear matrix sites engaged in transcription.

(PDF emailed within 0-6 h: $19.90)

Accession: 009112079

Download citation: RISBibTeXText

PMID: 9291093

DOI: 10.1023/a:1006811817247


Related references

Histone composition and core histone acetylation of transcriptionally active ribosomal chromatin of Physarum polycephalum. Cell Biology International Reports 16(11): 1177-1183, 1992

A direct link between core histone acetylation and transcriptionally active chromatin. Embo Journal 7(5): 1395-1402, 1988

Histone acetylation alters the capacity of the H1 histones to condense transcriptionally active/competent chromatin. Journal of Biological Chemistry 265(9): 5150-5156, 1990

Factors affecting nucleosome structure in transcriptionally active chromatin. Histone acetylation, nascent RNA and inhibitors of RNA synthesis. European Journal of Biochemistry 194(3): 811-823, 1990

Transcriptionally active chromatin 1. non histone proteins of transcriptionally active chromatin. Postepy Biologii Komorki 12(1): 55-80, 1985

Histone acetylation in chicken erythrocytes. Rates of acetylation and evidence that histones in both active and potentially active chromatin are rapidly modified. Biochemical Journal 250(1): 233-240, 1988

The 5 regions of human transcriptionally active genes are highly enriched for acetylation of histone H3 and methylation of lysine 4 of histone H3. Proceedings of the American Association for Cancer Research Annual Meeting 44: 14, 2003

Hmg protein binding to transcriptionally active chromatin requires changes in histone histone contact and physiologic salt conditions. Clinical Research 36(6): 874A, 1988

Histone acetylation increases the solubility of chromatin and occurs sequentially over most of the chromatin. A novel model for the biological role of histone acetylation. Journal of Biological Chemistry 257(13): 7336-7347, 1982

Non-histone proteins in transcriptionally active chromatin. Basic and Applied Histochemistry 31(3): 239-246, 1987

Histone H1 and the conformation of transcriptionally active chromatin. Bioessays 13(2): 87-88, 1991

Acetylation of Histone H2AX at Lys 5 by the TIP60 Histone Acetyltransferase Complex Is Essential for the Dynamic Binding of NBS1 to Damaged Chromatin. Molecular and Cellular Biology 35(24): 4147-4157, 2016

Dynamic changes in chromatin acetylation and the expression of histone acetyltransferases and histone deacetylases regulate the SM22alpha transcription in response to Smad3-mediated TGFbeta1 signaling. Biochemical and Biophysical Research Communications 348(2): 351-358, 2006

Ubiquitinated histone H2B is preferentially located in transcriptionally active chromatin. Ubiquitin system edited by Milton Schlesinger Avram Hershko: 163, 1988

Ubiquitinated histone H2B is preferentially located in transcriptionally active chromatin. Biochemistry 28(3): 958-963, 1989