HDT1_MAIZE
ID HDT1_MAIZE Reviewed; 307 AA.
AC O24591;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Histone deacetylase HDT1;
DE AltName: Full=Histone deacetylase 2a;
DE Short=HD2a;
DE AltName: Full=Nucleolar histone deacetylase HD2-p39;
DE AltName: Full=Zm-HD2a;
GN Name=HDT1; Synonyms=HD2a;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBUNIT, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND PHOSPHORYLATION.
RC STRAIN=cv. Cuzco 251;
RX PubMed=9204905; DOI=10.1126/science.277.5322.88;
RA Lusser A., Brosch G., Loidl A., Haas H., Loidl P.;
RT "Identification of maize histone deacetylase HD2 as an acidic nucleolar
RT phosphoprotein.";
RL Science 277:88-91(1997).
RN [2]
RP PROTEIN SEQUENCE OF 50-103 AND 284-295, BLOCKAGE OF N-TERMINUS, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8961957; DOI=10.1021/bi961294x;
RA Brosch G., Lusser A., Goralik-Schramel M., Loidl P.;
RT "Purification and characterization of a high molecular weight histone
RT deacetylase complex (HD2) of maize embryos.";
RL Biochemistry 35:15907-15914(1996).
RN [3]
RP SUBSTRATE SPECIFICITY.
RX PubMed=10346897; DOI=10.1021/bi982702v;
RA Koelle D., Brosch G., Lechner T., Pipal A., Helliger W., Taplick J.,
RA Loidl P.;
RT "Different types of maize histone deacetylases are distinguished by a
RT highly complex substrate and site specificity.";
RL Biochemistry 38:6769-6773(1999).
RN [4]
RP NOMENCLATURE.
RX PubMed=11469594; DOI=10.1007/s004250000506;
RA Dangl M., Brosch G., Haas H., Loidl P., Lusser A.;
RT "Comparative analysis of HD2 type histone deacetylases in higher plants.";
RL Planta 213:280-285(2001).
RN [5]
RP ACTIVITY REGULATION.
RX PubMed=14971890; DOI=10.1021/jm030990+;
RA Mai A., Massa S., Cerbara I., Valente S., Ragno R., Bottoni P., Scatena R.,
RA Loidl P., Brosch G.;
RT "3-(4-aroyl-1-methyl-1H-2-pyrrolyl)-N-hydroxy-2-propenamides as a new class
RT of synthetic histone deacetylase inhibitors. 2. Effect of pyrrole-C2 and/or
RT -C4 substitutions on biological activity.";
RL J. Med. Chem. 47:1098-1109(2004).
RN [6]
RP ACTIVITY REGULATION.
RX PubMed=14998325; DOI=10.1021/jm031036f;
RA Ragno R., Mai A., Massa S., Cerbara I., Valente S., Bottoni P., Scatena R.,
RA Jesacher F., Loidl P., Brosch G.;
RT "3-(4-aroyl-1-methyl-1H-pyrrol-2-yl)-N-hydroxy-2-propenamides as a new
RT class of synthetic histone deacetylase inhibitors. 3. Discovery of novel
RT lead compounds through structure-based drug design and docking studies.";
RL J. Med. Chem. 47:1351-1359(2004).
CC -!- FUNCTION: Mediates the deacetylation of lysine residues on the N-
CC terminal part of the core histones (H2A, H2B, H3 and H4). Histone
CC deacetylation gives a tag for epigenetic repression and plays an
CC important role in transcriptional regulation, cell cycle progression
CC and developmental events. Able to deacetylate all 4 core histones.
CC -!- ACTIVITY REGULATION: Inhibited by 3-(4-Aroyl-1-methyl-1H-pyrrol-2-yl)-
CC N-hydroxy-2-propenamides. 3-(1-methyl-4-phenylacetyl-1H-pyrrol-2-yl)-N-
CC hydroxy-2-propenamide 1b and 3-[1-methyl-4-(3-phenyl-2-propenoyl)-1H-
CC pyrrol-2-yl]-N-hydroxy-2-propenamide 1c are very potent inhibitors.
CC {ECO:0000269|PubMed:14971890, ECO:0000269|PubMed:14998325}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=55 uM for core histone {ECO:0000269|PubMed:8961957};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:8961957};
CC -!- SUBUNIT: Multimer. Isolated as a trimer composed of 3 proteins of 39,
CC 42 and 45 kDa, possibly a homotrimer with different phosphorylation
CC status or a heterotrimer with HDT2 and/or HDT3.
CC {ECO:0000269|PubMed:9204905}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:9204905}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout germination. Increases during
CC the initial 30 hours of germination, slightly decreases between 30 and
CC 48 hours, and increases again at 60 hours, correlating with the
CC proliferative activity of embryo cells. {ECO:0000269|PubMed:9204905}.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: Phosphorylated. Required for enzyme activity.
CC {ECO:0000269|PubMed:9204905}.
CC -!- SIMILARITY: Belongs to the histone deacetylase HD2 family.
CC {ECO:0000305}.
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DR EMBL; U82815; AAB63262.1; -; mRNA.
DR EMBL; AF026917; AAC61674.1; -; Genomic_DNA.
DR PIR; T04141; T04141.
DR AlphaFoldDB; O24591; -.
DR SMR; O24591; -.
DR iPTMnet; O24591; -.
DR PRIDE; O24591; -.
DR MaizeGDB; 314821; -.
DR SABIO-RK; O24591; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; O24591; baseline and differential.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR InterPro; IPR041232; NPL.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF17800; NPL; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Direct protein sequencing; Hydrolase; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..307
FT /note="Histone deacetylase HDT1"
FT /id="PRO_0000195208"
FT ZN_FING 276..299
FT /note="C2H2-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 98..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..113
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..194
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 307 AA; 33238 MW; 9CFF6B036D274FC1 CRC64;
MEFWGLEVKP GSTVKCEPGY GFVLHLSQAA LGESKKSDNA LMYVKIDDQK LAIGTLSVDK
NPHIQFDLIF DKEFELSHTS KTTSVFFTGY KVEQPFEEDE MDLDSEDEDE ELNVPVVKEN
GKADEKKQKS QEKAVAAPSK SSPDSKKSKD DDDSDEDETD DSDEDETDDS DEGLSSEEGD
DDSSDEDDTS DDEEEDTPTP KKPEVGKKRP AESSVLKTPL SDKKAKVATP SSQKTGGKKG
AAVHVATPHP AKGKTIVNND KSVKSPKSAP KSGGSVPCKP CSKSFISETA LQAHSRAKMG
ASESQVQ
