Identifiers and Description

Gene Model Identifier

TTHERM_00016170

Standard Name

HHT3 (Histone H Three)

Aliases

PreTt11924 | 1.m00972

Description

Histone minor H3 variant, H3.3; replication independent replacement variant found primarily in macronuclei; constitutively expressed; not essential for cell growth

Genome Browser (Macronucleus)

GBrowse

Genome Browser (Micronucleus)

GBrowse

Gene Ontology Annotations

Cellular Component

Domains

  • ( PF00125 ) Core histone H2A/H2B/H3/H4

Gene Expression Profile

  • Tetrahymena Functional Genomics Database:

Change in Gene Expression

TMHMM

TMHMM

Signal Peptide

Signal Peptide Present?: No
Presense Probability: 10.7%

TetraMine Data

TTHERM_00016170

WebApollo

Fullscreen View

Tetrahymena Stock Center

No Data fetched for StockID

Homologs (v.2006 protein sequences)

SourceIdentifierScoreDescription
Tetrahymena borealisEI9_02628.15.998946283774988e-95histone H3 (137 aa)
WormBaseWBGene000018873.0005855096961235e-80locus:his-13 Histone H3 st
atus:Predicted UniProt:P0889
8 protein_id:CAB05834.1
OxytrichaContig1081.1.g606.00277790667473e-79Core histone H2A/H2B/H3/H4
DictyBaseDDB_G02674029.998819815181669e-76H3a on chromosome: 1 position
1520754 to 1521173
SGDYNL031C2.000299424410363e-74HHT2 Histone H3, core histone
protein required for chromatin
assembly, part of heterochrom
atin-mediated telomeric and HM
silencing; one of two identic
al histone H3 proteins (see HH
T1); regulated by acetylation,
methylation, and phosphorylat
ion
Stentor CoeruleusSteCoe_353112.6786369618080778e-33

General Information

No Data fetched for General Information

Associated Literature

  1. Ref:16908532: Cui B, Liu Y, Gorovsky MA (2006) Deposition and function of histone H3 variants in Tetrahymena thermophila. Molecular and cellular biology 26(20):7719-30
  2. Ref:14755052: Liu Y, Mochizuki K, Gorovsky MA (2004) Histone H3 lysine 9 methylation is required for DNA elimination in developing macronuclei in Tetrahymena. Proceedings of the National Academy of Sciences of the United States of America 101(6):1679-84
  3. Ref:15196465: Mochizuki K, Gorovsky MA (2004) Small RNAs in genome rearrangement in Tetrahymena. Current opinion in genetics & development 14(2):181-7
  4. Ref:14661947: Poux AN, Marmorstein R (2003) Molecular basis for Gcn5/PCAF histone acetyltransferase selectivity for histone and nonhistone substrates. Biochemistry 42(49):14366-74
  5. Ref:12665578: Ren Q, Gorovsky MA (2003) The nonessential H2A N-terminal tail can function as an essential charge patch on the H2A.Z variant N-terminal tail. Molecular and cellular biology 23(8):2778-89
  6. Ref:12522258: Zilberman D, Cao X, Jacobsen SE (2003) ARGONAUTE4 control of locus-specific siRNA accumulation and DNA and histone methylation. Science (New York, N.Y.) 299(5607):716-9
  7. Ref:14536085: Clements A, Poux AN, Lo WS, Pillus L, Berger SL, Marmorstein R (2003) Structural basis for histone and phosphohistone binding by the GCN5 histone acetyltransferase. Molecular cell 12(2):461-73
  8. Ref:11972045: Dou Y, Gorovsky MA (2002) Regulation of transcription by H1 phosphorylation in Tetrahymena is position independent and requires clustered sites. Proceedings of the National Academy of Sciences of the United States of America 99(9):6142-6
  9. Ref:12123289: Waterborg JH (2002) Dynamics of histone acetylation in vivo. A function for acetylation turnover? Biochemistry and cell biology = Biochimie et biologie cellulaire 80(3):363-78
  10. Ref:11784863: Crosio C, Fimia GM, Loury R, Kimura M, Okano Y, Zhou H, Sen S, Allis CD, Sassone-Corsi P (2002) Mitotic phosphorylation of histone H3: spatio-temporal regulation by mammalian Aurora kinases. Molecular and cellular biology 22(3):874-85
  11. Ref:12297044: Taverna SD, Coyne RS, Allis CD (2002) Methylation of histone h3 at lysine 9 targets programmed DNA elimination in tetrahymena. Cell 110(6):701-11
  12. Ref:12351775: Jenuwein T (2002) Molecular biology. An RNA-guided pathway for the epigenome. Science (New York, N.Y.) 297(5590):2215-8
  13. Ref:11994311: Langer MR, Fry CJ, Peterson CL, Denu JM (2002) Modulating acetyl-CoA binding in the GCN5 family of histone acetyltransferases. The Journal of biological chemistry 277(30):27337-44
  14. Ref:11891286: Shang Y, Song X, Bowen J, Corstanje R, Gao Y, Gaertig J, Gorovsky MA (2002) A robust inducible-repressible promoter greatly facilitates gene knockouts, conditional expression, and overexpression of homologous and heterologous genes in Tetrahymena thermophila. Proceedings of the National Academy of Sciences of the United States of America 99(6):3734-9
  15. Ref:12455963: Duharcourt S, Yao MC (2002) Role of histone deacetylation in developmentally programmed DNA rearrangements in Tetrahymena thermophila. Eukaryotic cell 1(2):293-303
  16. Ref:11135657: Tan S (2001) One HAT size fits all? Nature structural biology 8(1):8-10
  17. Ref:11467741: Green GR (2001) Phosphorylation of histone variant regions in chromatin: unlocking the linker? Biochemistry and cell biology = Biochimie et biologie cellulaire 79(3):275-87
  18. Ref:11751634: Briggs SD, Bryk M, Strahl BD, Cheung WL, Davie JK, Dent SY, Winston F, Allis CD (2001) Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae. Genes & development 15(24):3286-95
  19. Ref:10503205: Wiley EA, Mizzen CA, Allis CD (2000) Isolation and characterization of in vivo modified histones and an activity gel assay for identification of histone acetyltransferases. Methods in cell biology 62( ):379-94
  20. Ref:10975520: De Souza CP, Osmani AH, Wu LP, Spotts JL, Osmani SA (2000) Mitotic histone H3 phosphorylation by the NIMA kinase in Aspergillus nidulans. Cell 102(3):293-302
  21. Ref:10975519: Hsu JY, Sun ZW, Li X, Reuben M, Tatchell K, Bishop DK, Grushcow JM, Brame CJ, Caldwell JA, Hunt DF, Lin R, Smith MM, Allis CD (2000) Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes. Cell 102(3):279-91
  22. Ref:11112280: Trievel RC, Li FY, Marmorstein R (2000) Application of a fluorescent histone acetyltransferase assay to probe the substrate specificity of the human p300/CBP-associated factor. Analytical biochemistry 287(2):319-28
  23. Ref:10536141: Hettmann C, Soldati D (1999) Cloning and analysis of a Toxoplasma gondii histone acetyltransferase: a novel chromatin remodelling factor in Apicomplexan parasites. Nucleic acids research 27(22):4344-52
  24. Ref:10199406: Wei Y, Yu L, Bowen J, Gorovsky MA, Allis CD (1999) Phosphorylation of histone H3 is required for proper chromosome condensation and segregation. Cell 97(1):99-109
  25. Ref:10551870: Karrer KM, VanNuland TA (1999) Nucleosome positioning is independent of histone H1 in vivo. The Journal of biological chemistry 274(46):33020-4
  26. Ref:10549296: Dou Y, Mizzen CA, Abrams M, Allis CD, Gorovsky MA (1999) Phosphorylation of linker histone H1 regulates gene expression in vivo by mimicking H1 removal. Molecular cell 4(4):641-7
  27. Ref:10611321: Strahl BD, Ohba R, Cook RG, Allis CD (1999) Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in Tetrahymena. Proceedings of the National Academy of Sciences of the United States of America 96(26):14967-72
  28. Ref:9343391: Yu L, Gorovsky MA (1997) Constitutive expression, not a particular primary sequence, is the important feature of the H3 replacement variant hv2 in Tetrahymena thermophila. Molecular and cellular biology 17(11):6303-10
  29. Ref:8121802: Thatcher TH, MacGaffey J, Bowen J, Horowitz S, Shapiro DL, Gorovsky MA (1994) Independent evolutionary origin of histone H3.3-like variants of animals and Tetrahymena. Nucleic acids research 22(2):180-6

Sequences

>TTHERM_00016170(coding)
ATGGCTAGAACTAAATAAACTGCTAGAAAGTCAACTGGTGTTAAGGCTCCTAGAAAACAA
CTCGCTACCAAGGCTGCCAGAAAGTCTGCCCCCGTCTCTGGTGGTGTCAAGAAGCCCCAT
AAATTCAGACCTGGTACCGTCGCCTTGAGAGAAATCAGAAAGTATTAAAAGACTACTGAC
TTACTTATTAGAAAGCTCCCCTTCTAAAGACTTGTCAGAGATATTGCTATGGAAATGAAG
AGTGATATCAGATTCCAATCCCAAGCTATCCTTGCCCTCCAAGAAGCCGCTGAAGCCTAC
CTCGTCGGTTTATTCGAAGATACCAACCTCTGCGCTATCCACGCTAGAAGAGTTACTATT
ATGACCAAGGATCTCCACCTTGCTAGAAGAATTAGAGGAGAAAGATTCTGA


>TTHERM_00016170(protein)
MARTKQTARKSTGVKAPRKQLATKAARKSAPVSGGVKKPHKFRPGTVALREIRKYQKTTD
LLIRKLPFQRLVRDIAMEMKSDIRFQSQAILALQEAAEAYLVGLFEDTNLCAIHARRVTI
MTKDLHLARRIRGERF


>TTHERM_00016170(gene)
ATGGCTAGAACTAAATAAACTGCTAGAAAGTCAACTGGTGTTAAGGCTCCTAGAAAACAA
CTCGCTACCAAGGCTGCCAGAAAGTCTGCCCCCGTCTCTGGTGGTGTCAAGAAGCCCCAT
AAATTCAGACCTGGTACCGTCGCCTTGAGAGAAATCAGAAAGTATTAAAAGACTACTGAC
TTACTTATTAGAAAGCTCCCCTTCTAAAGACTTGTCAGAGATATTGCTATGGAAATGAAG
AGTGATATCAGATTCCAATCCCAAGCTATCCTTGCCCTCCAAGAAGCCGCTGAAGCCTAC
CTCGTCGGTTTATTCGAAGATACCAACCTCTGCGCTATCCACGCTAGAAGAGTTACTATT
ATGACCAAGGATCTCCACCTTGCTAGAAGAATTAGAGGAGAAAGATTCTGA