Identifiers and Description

Gene Model Identifier

TTHERM_00836580

Standard Name

BTU2 (Beta-Tubulin )

Aliases

146.m00071 | PreTt17770 | 3743.m00003

Description

Beta-tubulin; ciliary form is phosphorylated by CaMK; multiple polyglycation sites are required for survival and partial removal affects growth, motility, and cytokinesis; transcript destabilized by heat shock; protein identical to Btu1p

Genome Browser (Macronucleus)

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Genome Browser (Micronucleus)

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Gene Ontology Annotations

Cellular Component

Molecular Function

Biological Process

Domains

  • ( PF00091 ) Tubulin/FtsZ family, GTPase domain
  • ( PF03953 ) tubulin/FtsZ family, C-terminal domain

Gene Expression Profile

  • Tetrahymena Functional Genomics Database:

TetraMine Data

TTHERM_00836580

WebApollo

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Tetrahymena Stock Center

No Data fetched for StockID

Homologs (v.2006 protein sequences)

SourceIdentifierScoreDescription
Stentor CoeruleusSteCoe_228510
WormBaseWBGene000065389.997093137033517e-262locus:tbb-4 Tubulin beta-4 c
hain status:Partially_confir
med UniProt:P41937 protein
_id:CAA86310.1
Tetrahymena borealisEI9_09761.19.997093137033517e-262tubulin/FtsZ family, GTPase do
main-containing protein (444 a
a)
DictyBaseDDB_G02691969.997093137033517e-262tubB on chromosome: 1 position
3261649 to 3263130
OxytrichaContig8792.0.g749.997093137033517e-262Tubulin/FtsZ family, GTPase do
main
SGDYFL037W9.997093137033517e-262TUB2 Beta-tubulin; associates
with alpha-tubulin (Tub1p and
Tub3p) to form tubulin dimer,
which polymerizes to form micr
otubules

General Information

No Data fetched for General Information

Associated Literature

  1. Ref:15470250: Smith JJ, Yakisich JS, Kapler GM, Cole ES, Romero DP (2004) A beta-tubulin mutation selectively uncouples nuclear division and cytokinesis in Tetrahymena thermophila. Eukaryotic cell 3(5):1217-26
  2. Ref:11864572: Duan J, Gorovsky MA (2002) Both carboxy-terminal tails of alpha- and beta-tubulin are essential, but either one will suffice. Current biology : CB 12(4):313-6
  3. Ref:11862218: Thazhath R, Liu C, Gaertig J (2002) Polyglycylation domain of beta-tubulin maintains axonemal architecture and affects cytokinesis in Tetrahymena. Nature cell biology 4(3):256-9
  4. Ref:10831613: Xia L, Hai B, Gao Y, Burnette D, Thazhath R, Duan J, Bré MH, Levilliers N, Gorovsky MA, Gaertig J (2000) Polyglycylation of tubulin is essential and affects cell motility and division in Tetrahymena thermophila. The Journal of cell biology 149(5):1097-106
  5. Ref:10847334: Gaertig J (2000) Molecular mechanisms of microtubular organelle assembly in Tetrahymena. The Journal of eukaryotic microbiology 47(3):185-90
  6. Ref:10331805: Gaertig J, Gao Y, Tishgarten T, Clark TG, Dickerson HW (1999) Surface display of a parasite antigen in the ciliate Tetrahymena thermophila. Nature biotechnology 17(5):462-5
  7. Ref:10403369: Nakazawa M, Moreira D, Laurent J, Le Guyader H, Fukami Y, Ito K (1999) Biochemical analysis of the interaction between elongation factor 1alpha and alpha/beta-tubulins from a ciliate, Tetrahymena pyriformis. FEBS letters 453(1-2):29-34
  8. Ref:7775576: Gaertig J, Cruz MA, Bowen J, Gu L, Pennock DG, Gorovsky MA (1995) Acetylation of lysine 40 in alpha-tubulin is not essential in Tetrahymena thermophila. The Journal of cell biology 129(5):1301-10
  9. Ref:7804247: Levasseur PJ, Meng Q, Bouck GB (1995) Tubulin genes in the algal protist Euglena gracilis. The Journal of eukaryotic microbiology 41(5):468-77
  10. Ref:9072048: Nakamura K, Shigaki Y, Takaya C (1995) Proteolysis of tubulin isotypes within Tetrahymena axonemes. Biological chemistry Hoppe-Seyler 376(12):729-32
  11. Ref:7651434: Gu L, Gaertig J, Stargell LA, Gorovsky MA (1995) Gene-specific signal transduction between microtubules and tubulin genes in Tetrahymena thermophila. Molecular and cellular biology 15(9):5173-9
  12. Ref:7910408: Gaertig J, Thatcher TH, Gu L, Gorovsky MA (1994) Electroporation-mediated replacement of a positively and negatively selectable beta-tubulin gene in Tetrahymena thermophila. Proceedings of the National Academy of Sciences of the United States of America 91(10):4549-53
  13. Ref:7816630: Gaertig J, Gu L, Hai B, Gorovsky MA (1994) High frequency vector-mediated transformation and gene replacement in Tetrahymena. Nucleic acids research 22(24):5391-8
  14. Ref:8102139: Soares H, Galego L, Cóias R, Rodrigues-Pousada C (1993) The mechanisms of tubulin messenger regulation during Tetrahymena pyriformis reciliation. The Journal of biological chemistry 268(22):16623-30
  15. Ref:8102497: Mitchison TJ (1993) Localization of an exchangeable GTP binding site at the plus end of microtubules. Science (New York, N.Y.) 261(5124):1044-7
  16. Ref:8221902: Gaertig J, Thatcher TH, McGrath KE, Callahan RC, Gorovsky MA (1993) Perspectives on tubulin isotype function and evolution based on the observation that Tetrahymena thermophila microtubules contain a single alpha- and beta-tubulin. Cell motility and the cytoskeleton 25(3):243-53
  17. Ref:1339345: Dupuis P (1992) The beta-tubulin genes of Paramecium are interrupted by two 27 bp introns. The EMBO journal 11(10):3713-9
  18. Ref:1640053: Nakamura K, Okuya Y, Katahira M, Yoshida S, Wada S, Okuno M (1992) Analysis of tubulin isoforms by two-dimensional gel electrophoresis using SDS-polyacrylamide gel electrophoresis in the first dimension. Journal of biochemical and biophysical methods 24(3-4):195-203
  19. Ref:1900051: Penque D, Galego L, Rodrigues-Pousada C (1991) Multiple alpha-tubulin isoforms in cilia and cytoskeleton of Tetrahymena pyriformis generated by post-translational modifications. Studies during reciliation. European journal of biochemistry 195(2):487-94
  20. Ref:1902785: Soares H, Cyrne L, Barahona I, Rodrigues-Pousada C (1991) Different patterns of expression of beta-tubulin genes in Tetrahymena pyriformis during reciliation. European journal of biochemistry 197(2):291-9
  21. Ref:1689806: Krawczyńska W, Kludkiewicz B (1990) Polyadenylated RNA during DAPI-arrested regeneration of Tetrahymena cilia. Molecular and cellular biochemistry 92(1):53-60
  22. Ref:2470096: Harper DS, Jahn CL (1989) Differential use of termination codons in ciliated protozoa. Proceedings of the National Academy of Sciences of the United States of America 86(9):3252-6
  23. Ref:2768213: Hirano-Ohnishi J, Watanabe Y (1989) Ca2+/calmodulin-dependent phosphorylation of ciliary beta-tubulin in Tetrahymena. Journal of biochemistry 105(6):858-60
  24. Ref:3139885: Barahona I, Soares H, Cyrne L, Penque D, Denoulet P, Rodrigues-Pousada C (1988) Sequence of one alpha- and two beta-tubulin genes of Tetrahymena pyriformis. Structural and functional relationships with other eukaryotic tubulin genes. Journal of molecular biology 202(3):365-82
  25. Ref:3137027: Cóias R, Galego L, Barahona I, Rodrigues-Pousada C (1988) Destabilization of tubulin mRNA during heat shock in Tetrahymena pyriformis. European journal of biochemistry 175(3):467-74
  26. Ref:3901010: Suprenant KA, Hays E, LeCluyse E, Dentler WL (1985) Multiple forms of tubulin in the cilia and cytoplasm of Tetrahymena thermophila. Proceedings of the National Academy of Sciences of the United States of America 82(20):6908-12
  27. Ref:6192014: Barahona I, Rodrigues-Pousada C (1983) Site of tubulin synthesis in Tetrahymena pyriformis. FEBS letters 158(2):271-5
  28. Ref:6413210: Little M, Quinlan RA, Hoffman EJ, Ludueña RF (1983) Identification and characterization of axopodial tubulins from Echinosphaerium nucleofilum. European journal of cell biology 31(1):55-61
  29. Ref:7458914: Roobol A, Pogson CI, Gull K (1980) Identification and characterization of microtubule proteins from myxamoebae of Physarum polycephalum. The Biochemical journal 189(2):305-12
  30. Ref:7440655: Gavin RH (1980) The oral apparatus of Tetrahymena. V. Oral apparatus polypeptides and their distribution. Journal of cell science 44( ):317-33
  31. Ref:111932: Marcaud L, Hayes D (1979) RNA synthesis in starved deciliated Tetrahymena pyriformis. European journal of biochemistry 98(1):267-73
  32. Ref:119852: Fliss ER, Suyama Y (1979) Tetrahymena tubulins and in vitro translation of Tetrahymena RNA. The Journal of protozoology 26(3):505-9

Sequences

>TTHERM_00836580(coding)
ATGAGAGAAATCGTTCACATTCAAGGTGGTCAATGTGGTAACCAAATCGGTGCCAAGTTC
TGGGAAGTCATTTCCGATGAACACGGTATCGACCCCACTGGTACCTATCACGGTGATTCT
GATTTACAATTAGAAAGAATCAATGTTTACTACAATGAAGCTACTGGTGGTAGATACGTT
CCCAGAGCCATTTTGATGGATTTGGAACCTGGTACCATGGATTCCGTCAGAGCTGGTCCT
TTCGGTCAACTCTTCAGACCTGATAACTTCGTTTTCGGTCAAACTGGTGCTGGTAACAAC
TGGGCTAAGGGTCACTACACTGAAGGTGCTGAATTAATTGACTCCGTTTTGGACGTTGTC
AGAAAGGAAGCTGAAGGTTGCGATTGCCTCTAAGGTTTCCAAATCACCCACTCCCTCGGT
GGTGGTACTGGTTCTGGTATGGGTACCCTCCTTATCTCCAAGGTCAGAGAAGAATATCCC
GATAGAATCATGGAAACTTTCTCCGTCGTCCCCTCTCCCAAGGTCTCCGATACCGTCGTT
GAACCCTACAATGCTACTCTTTCCGTCCATCAATTGGTCGAAAATGCTGATGAATGTATG
GTCATCGATAACGAAGCTCTTTACGATATCTGCTTCAGAACCCTTAAGCTCACCACCCCC
ACTTATGGTGATCTTAACCACTTGGTCTCTGCTGCTATGTCTGGTGTTACTTGCTGTCTC
AGATTCCCTGGTCAATTGAACTCTGATCTTAGAAAGCTCGCTGTCAACTTGATTCCCTTC
CCTCGTCTCCACTTCTTCATGATTGGTTTCGCTCCCCTTACCTCCAGAGGTTCTCAATAA
TACAGAGCCCTCACTGTTCCCGAATTAACCCAATAAATGTTCGATGCCAAGAACATGATG
TGCGCTGCTGATCCCAGACACGGTAGATATTTGACTGCCTCTGCTCTCTTCAGAGGAAGA
ATGTCCACCAAGGAAGTTGACGAATAAATGCTTAATGTCTAAAACAAGAACTCTTCTTAC
TTCGTTGAATGGATTCCCAACAACATCAAGTCCTCCATTTGTGATATTCCTCCTAAGGGT
CTTAAGATGGCTGTTACCTTCGTCGGTAACTCCACTGCTATCTAAGAAATGTTCAAGAGA
GTCGCTGAATAATTCACTGCTATGTTCAGAAGAAAGGCTTTCTTACATTGGTACACTGGT
GAAGGTATGGACGAAATGGAATTCACTGAAGCTGAATCCAACATGAACGATCTCGTCTCC
GAATATCAATAATATCAAGATGCTACCGCTGAAGAAGAAGGTGAATTCGAAGAAGAAGAA
GGTGAAAACTGA


>TTHERM_00836580(protein)
MREIVHIQGGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLERINVYYNEATGGRYV
PRAILMDLEPGTMDSVRAGPFGQLFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVV
RKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPDRIMETFSVVPSPKVSDTVV
EPYNATLSVHQLVENADECMVIDNEALYDICFRTLKLTTPTYGDLNHLVSAAMSGVTCCL
RFPGQLNSDLRKLAVNLIPFPRLHFFMIGFAPLTSRGSQQYRALTVPELTQQMFDAKNMM
CAADPRHGRYLTASALFRGRMSTKEVDEQMLNVQNKNSSYFVEWIPNNIKSSICDIPPKG
LKMAVTFVGNSTAIQEMFKRVAEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATAEEEGEFEEEEGEN


>TTHERM_00836580(gene)
ATGAGAGAAATCGTTCACATTCAAGGTGGTCAATGTGGTAACCAAATCGGTGCCAAGTTC
TGGGAAGTCATTTCCGATGAACACGGTATCGACCCCACTGGTACCTATCACGGTGATTCT
GATTTACAATTAGAAAGAATCAATGTTTACTACAATGAAGCTACTGGTGGTAGATACGTT
CCCAGAGCCATTTTGATGGATTTGGAACCTGGTACCATGGATTCCGTCAGAGCTGGTCCT
TTCGGTCAACTCTTCAGACCTGATAACTTCGTTTTCGGTCAAACTGGTGCTGGTAACAAC
TGGGCTAAGGGTCACTACACTGAAGGTGCTGAATTAATTGACTCCGTTTTGGACGTTGTC
AGAAAGGAAGCTGAAGGTTGCGATTGCCTCTAAGGTTTCCAAATCACCCACTCCCTCGGT
GGTGGTACTGGTTCTGGTATGGGTACCCTCCTTATCTCCAAGGTCAGAGAAGAATATCCC
GATAGAATCATGGAAACTTTCTCCGTCGTCCCCTCTCCCAAGGTCTCCGATACCGTCGTT
GAACCCTACAATGCTACTCTTTCCGTCCATCAATTGGTCGAAAATGCTGATGAATGTATG
GTCATCGATAACGAAGCTCTTTACGATATCTGCTTCAGAACCCTTAAGCTCACCACCCCC
ACTTATGGTGATCTTAACCACTTGGTCTCTGCTGCTATGTCTGGTGTTACTTGCTGTCTC
AGATTCCCTGGTCAATTGAACTCTGATCTTAGAAAGCTCGCTGTCAACTTGATTCCCTTC
CCTCGTCTCCACTTCTTCATGATTGGTTTCGCTCCCCTTACCTCCAGAGGTTCTCAATAA
TACAGAGCCCTCACTGTTCCCGAATTAACCCAATAAATGTTCGATGCCAAGAACATGATG
TGCGCTGCTGATCCCAGACACGGTAGATATTTGACTGCCTCTGCTCTCTTCAGAGGAAGA
ATGTCCACCAAGGAAGTTGACGAATAAATGCTTAATGTCTAAAACAAGAACTCTTCTTAC
TTCGTTGAATGGATTCCCAACAACATCAAGTCCTCCATTTGTGATATTCCTCCTAAGGGT
CTTAAGATGGCTGTTACCTTCGTCGGTAACTCCACTGCTATCTAAGAAATGTTCAAGAGA
GTCGCTGAATAATTCACTGCTATGTTCAGAAGAAAGGCTTTCTTACATTGGTACACTGGT
GAAGGTATGGACGAAATGGAATTCACTGAAGCTGAATCCAACATGAACGATCTCGTCTCC
GAATATCAATAATATCAAGATGCTACCGCTGAAGAAGAAGGTGAATTCGAAGAAGAAGAA
GGTGAAAACTGA