» Articles » PMID: 3344202

Sequence of CDNAs for Mammalian H2A.Z, an Evolutionarily Diverged but Highly Conserved Basal Histone H2A Isoprotein Species

Overview
Specialty Biochemistry
Date 1988 Feb 11
PMID 3344202
Citations 25
Authors
Affiliations
Soon will be listed here.
Abstract

The nucleotide sequences of cDNAs for the evolutionarily diverged but highly conserved basal H2A isoprotein, H2A.Z, have been determined for the rat, cow, and human. As a basal histone, H2A.Z is synthesized throughout the cell cycle at a constant rate, unlinked to DNA replication, and at a much lower rate in quiescent cells. Each of the cDNA isolates encodes the entire H2A.Z polypeptide. The human isolate is about 1.0 kilobases long. It contains a coding region of 387 nucleotides flanked by 106 nucleotides of 5'UTR and 376 nucleotides of 3'UTR, which contains a polyadenylation signal followed by a poly A tail. The bovine and rat cDNAs have 97 and 94% nucleotide positional identity to the human cDNA in the coding region and 98% in the proximal 376 nucleotides of the 3'UTR which includes the polyadenylation signal. A potential stem-forming sequence imbedded in a direct repeat is found centered at 261 nucleotides into the 3'UTR. Each of the cDNA clones could be transcribed and translated in vitro to yield H2A.Z protein. The mammalian H2A.Z cDNA coding sequences are approximately 80% similar to those in chicken and 75% to those in sea urchin.

Citing Articles

Histone H2A variant H2A.B is enriched in transcriptionally active and replicating HSV-1 lytic chromatin.

Flores Cortes E, Saddoris S, Owens A, Gibeault R, Depledge D, Schang L J Virol. 2024; 98(4):e0201523.

PMID: 38451083 PMC: 11019955. DOI: 10.1128/jvi.02015-23.


Deciphering the Enigma of the Histone H2A.Z-1/H2A.Z-2 Isoforms: Novel Insights and Remaining Questions.

Cheema M, Good K, Kim B, Soufari H, OSullivan C, Freeman M Cells. 2020; 9(5).

PMID: 32397240 PMC: 7290884. DOI: 10.3390/cells9051167.


MS_HistoneDB, a manually curated resource for proteomic analysis of human and mouse histones.

Kennani S, Adrait A, Shaytan A, Khochbin S, Bruley C, Panchenko A Epigenetics Chromatin. 2017; 10:2.

PMID: 28096900 PMC: 5223428. DOI: 10.1186/s13072-016-0109-x.


Global dynamics of newly constructed oligonucleosomes of conventional and variant H2A.Z histone.

Ramaswamy A, Ioshikhes I BMC Struct Biol. 2007; 7:76.

PMID: 17996059 PMC: 2216022. DOI: 10.1186/1472-6807-7-76.


H2A.Z has a function reminiscent of an activator required for preferential binding to intergenic DNA.

Larochelle M, Gaudreau L EMBO J. 2003; 22(17):4512-22.

PMID: 12941702 PMC: 202369. DOI: 10.1093/emboj/cdg427.


References
1.
Moss T, Cary P, Abercrombie B, Crane-Robinson C, Bradbury E . A pH-dependent interaction between histones H2A and H2B involving secondary and tertiary folding. Eur J Biochem. 1976; 71(2):337-50. DOI: 10.1111/j.1432-1033.1976.tb11120.x. View

2.
Dodgson J, Yamamoto M, Engel J . Chicken histone H3.3B cDNA sequence confirms unusual 3' UTR structure. Nucleic Acids Res. 1987; 15(15):6294. PMC: 306085. DOI: 10.1093/nar/15.15.6294. View

3.
SANGER F, Nicklen S, Coulson A . DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977; 74(12):5463-7. PMC: 431765. DOI: 10.1073/pnas.74.12.5463. View

4.
West M, Bonner W . Histone 2A, a heteromorphous family of eight protein species. Biochemistry. 1980; 19(14):3238-45. DOI: 10.1021/bi00555a022. View

5.
Bonner W, West M, Stedman J . Two-dimensional gel analysis of histones in acid extracts of nuclei, cells, and tissues. Eur J Biochem. 1980; 109(1):17-23. DOI: 10.1111/j.1432-1033.1980.tb04762.x. View