Identification of Maize Histone Deacetylase HD2 as an Acidic Nucleolar Phosphoprotein

Lusser, Alexandra; Brosch, Gerald; Loidl, Adele; Haas, Hubertus; Loidl, Peter

doi:10.1126/science.277.5322.88

Cited by 219 publications

(225 citation statements)

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“…Also, the question concerning the existence of additional human HDAC(s) that resembles yeast RPD3 remains open. Recently, an acidic nucleolar phosphoprotein that was not homologous to yeast RPD3 was identified as a maize histone deacetylase (35). Our finding of three human HDACs closely related to yeast RPD3 therefore does not exclude the possibility that there are additional human histone deacetylases with little or no nucleotide and amino acid sequences homology to yeast RPD3.…”

Section: Cloning Of Human Cdnas Encoding a Novel Member Of Thementioning

confidence: 64%

“…In Vitro Transcription/Translation and in Vitro Binding Assays-To generate 35 S-labeled YY1, pT7-YY1 was transcribed and translated with T7 RNA polymerase and [ 35 S]methionine in a transcription/translation coupled system (Promega). Bacterially expressed GST protein and different GST fusion proteins were purified according to Frangioni and Neel (33) with modifications.…”

Section: Methodsmentioning

confidence: 99%

“…For binding assays, beads were mixed with in vitro translated, 35 Slabeled YY1 protein for 1 h at room temperature. Unbounded proteins were washed extensively with STE buffer containing 0.2% Nonidet P-40, and bound proteins were eluted from the beads by boiling in SDS loading buffer (50 mM Tris-HCl, pH 6.8, 0.3 M 2-mercaptoethanol, 2% SDS, 0.1% bromphenol blue, and 10% glycerol).…”

Section: Methodsmentioning

confidence: 99%

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Isolation and Characterization of cDNAs Corresponding to an Additional Member of the Human Histone Deacetylase Gene Family

Yang

Yao

Sun

et al. 1997

Journal of Biological Chemistry

402

301

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Several human cDNAs encoding a histone deacetylase protein, HDAC3, have been isolated. Analysis of the predicted amino acid sequence of HDAC3 revealed an open reading frame of 428 amino acids with a predicted molecular mass of 49 kDa. The HDAC3 protein is 50% identical in DNA sequence and 53% identical in protein sequence compared with the previously cloned human HDAC1. Comparison of the HDAC3 sequence with human HDAC2 also yielded similar results, with 51% identity in DNA sequence and 52% identity in protein sequence. The expressed HDAC3 protein is functionally active because it possesses histone deacetylase activity, represses transcription when tethered to a promoter, and binds transcription factor YY1. Similar to HDAC1 and HDAC2, HDAC3 is ubiquitously expressed in many different cell types.The organization of chromatin structure is a fundamental and significant component of transcriptional regulation in all eukaryotic cells. Transcriptionally active or repressed chromatin is determined, at least in part, by the modification of histones. For example, hyperacetylation of histones generally leads to an increase in transcription, whereas hypoacetylation of histones appears to have the opposite effect (reviewed in Refs. 1-4). Nuclear histone acetyltransferases such as transcription factors GCN5, PCAF, p300/CBP, and TAF II 230/250 have been identified from different organisms (5-9).Several yeast and mammalian histone deacetylases have been identified, and their corresponding genes have been cloned (10 -12). In yeast, the HDA1 protein, which shares sequence similarity to RPD3, is a subunit of a large histone deacetylase complex HDA. RPD3 is also associated with another yeast histone deacetylase complex HDB. Using a trapoxin (an inhibitor of histone deacetylase) affinity matrix, Taunton et al. (10) purified and cloned a human 55-kDa protein related to the yeast protein RPD3. Immunoprecipitation of this 55-kDa protein, HDAC1 (also called HD1), showed that it contains histone deacetylase activity. A second human histone deacetylase protein, HDAC2, with high homology to yeast RPD3 was identified based on a yeast two-hybrid trap experiment with the YY1 transcription factor as a bait (11). YY1 negatively regulates transcription by tethering HDAC2 to DNA as a corepressor. Both HDAC1 and HDAC2 exist in a complex with the corepressor mSIN3 and mediate Mad transcriptional repression (13-15). In addition, HDAC1 and HDAC2 are essential components of two thyroid hormone receptor corepressors, N-CoR and SMRT (16 -18). HDAC1 is also an important factor that represses transactivation by progesterone receptor (19).The yeast RPD3 protein was originally identified in genetic screens for transcriptional repressors (20). Besides human and mouse, highly homologous yeast RPD3 sequences have been identified in Drosophila (21), Caenorhabditis elegans (X78454 and 1176665), and Xenopus laevis (gi:576995). Currently, it has not yet been established whether the C. elegans or X. laevis RPD3-related proteins have histone deacetylase activities o...

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Section: Cloning Of Human Cdnas Encoding a Novel Member Of Thementioning

confidence: 64%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Isolation and Characterization of cDNAs Corresponding to an Additional Member of the Human Histone Deacetylase Gene Family

Yang

Yao

Sun

et al. 1997

Journal of Biological Chemistry

402

301

View full text Add to dashboard Cite

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“…HD2-type HDACs have only been detected in plants and are distantly related to peptidyl-prolyl cis-trans isomerases from insects, yeast and parasitic apicomplexans (Lusser et al, 1997;Aravind et al, 1998). The Arabidopsis genome encodes four members of this family, AtHDT1-4 (Pandey et al, 2002).…”

Section: Arabidopsis Hdacsmentioning

confidence: 99%

Arabidopsis histone deacetylase 6: a green link to RNA silencing

et al. 2007

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Epigenetic reprogramming is at the base of cancer initiation and progression. Generally, genome-wide reduction in cytosine methylation contrasts with the hypermethylation of control regions of functionally wellestablished tumor suppressor genes and many other genes whose role in cancer biology is not yet clear. While insight into mechanisms that induce aberrant cytosine methylation in cancer cells is just beginning to emerge, the initiating signals for analogous promoter methylation in plants are well documented. In Arabidopsis, the silencing of promoters requires components of the RNA interference machinery and promoter double-stranded RNA (dsRNA) to induce a repressive chromatin state that is characterized by cytosine methylation and histone deacetylation catalysed by the RPD3-type histone deacetylase AtHDA6. Similar mechanisms have been shown to occur in fission yeast and mammals. This review focuses on the connections between cytosine methylation, dsRNA and AtHDA6-controlled histone deacetylation during promoter silencing in Arabidopsis and discusses potential mechanistic similarities of these silencing events in cancer and plant cells.

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“…Members of the SRT gene family are related to yeast SIR2 (Imai et al, 2000;Landry et al, 2000). In contrast to other eukaryotes, plants contain a third family of enzymes that is unrelated to the other classes, the HD2-related deacetylases, which were identified initially in maize (Lusser et al, 1997;Dangl et al, 2001). …”

Section: Introductionmentioning

confidence: 99%

Regulation and Processing of Maize Histone Deacetylase Hda1 by Limited Proteolysis

et al. 2003

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A maize histone deacetylase gene was identified as a homolog of yeast Hda1. The predicted protein corresponds to a previously purified maize deacetylase that is active as a protein monomer with a molecular weight of 48,000 and is expressed in all tissues of germinating embryos. Hda1 is synthesized as an enzymatically inactive protein with an apparent molecular weight of 84,000 that is processed to the active 48-kD form by proteolytic removal of the C-terminal part, presumably via a 65-kD intermediate. The enzymatically inactive 84-kD protein also is part of a 300-kD protein complex of unknown function. The proteolytic cleavage of ZmHda1 is regulated during maize embryo germination in vivo. Expression of the recombinant full-length protein and the 48-kD form confirmed that only the smaller enzyme form is active as a histone deacetylase. In line with this finding, we show that the 48-kD protein is able to repress transcription efficiently in a reporter gene assay, whereas the full-length protein, including the C-terminal part, lacks full repression activity. This report on the processing of Hda1-p84 to enzymatically active Hda1-p48 demonstrates that proteolytic cleavage is a mechanism to regulate the function of Rpd3/Hda1-type histone deacetylases.

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Identification of Maize Histone Deacetylase HD2 as an Acidic Nucleolar Phosphoprotein

Cited by 219 publications

References 21 publications

Isolation and Characterization of cDNAs Corresponding to an Additional Member of the Human Histone Deacetylase Gene Family

Isolation and Characterization of cDNAs Corresponding to an Additional Member of the Human Histone Deacetylase Gene Family

Arabidopsis histone deacetylase 6: a green link to RNA silencing

Regulation and Processing of Maize Histone Deacetylase Hda1 by Limited Proteolysis

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