TUB2/YFL037W Summary 
TUB2 BASIC INFORMATION
| Standard Name | TUB2 1 |
|---|---|
| Systematic Name | YFL037W |
| Alias | ARM10 , SHE8 2 |
| Feature Type | ORF, Verified |
| Description | Beta-tubulin; associates with alpha-tubulin (Tub1p and Tub3p) to form tubulin dimer, which polymerizes to form microtubules (1 and see Summary Paragraph) 
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| Name Description | TUBulin 1 |
| GO Annotations | All TUB2 GO evidence and references |
|---|---|
| View Computational GO annotations for TUB2 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated |
| Mutant Phenotype | All TUB2 Phenotype details and references |
|---|---|
| Classical genetics | |
| conditional | |
| overexpression | |
| Large-scale survey | |
| null | |
| overexpression |
| Interactions | TUB2 All interactions details and references |
|---|---|
| 109 total interaction(s) for 84 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| External Links | All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB |
|---|
| Primary SGDID | S000001857 |
|---|
TUB2 RESOURCES
| SGD ORF map | GBrowse |
|---|---|
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Click on histogram for expression summary
Expression Summary
ADDITIONAL INFORMATION for TUB2
SUMMARY PARAGRAPH for TUB2
In S. cerevisiae, TUB2 encodes the single essential beta-tubulin (1). Tub2p belongs to the tubulin superfamily, which includes alpha- and gamma-tubulin and the prokaryotic tubulin-like gene FtsZ (reviewed in 3, 4). Beta- and alpha-tubulin form tubulin heterodimers, which polymerize into microtubules. Microtubules are conserved cytoskeletal elements that function in nuclear processes: chromosome segregation in mitosis and meiosis, spindle orientation, and nuclear migration during mitosis and mating (5; for reviews, see 6, 7). All microtubules in S. cerevisiae emanate from a microtubule organizing center called the spindle pole body (SPB), which is embedded in the nuclear envelope (for review, see 8). Microtubules extend from both faces of the SPB, generating two types of microtubules: nuclear and cytoplasmic microtubules (9; for review, see 8). The distribution and length of these two types of microtubules is regulated throughout the cell cycle (9; reviewed in 10).
TUB2 was cloned based on its strong homology with its counterparts in other eukaryotes (1). There is an abundance of tub2 conditional mutants resulting from genetic screens for chromosome loss and sensitivity/resistance to anti-microtubule drugs (such as benomyl), suppressor analysis, and in vitro mutagenesis (11, 12, 13, 14). One benomyl-resistant allele of TUB2, tub2-150, actually requires benomyl for growth at high temperatures, suggesting that microtubules in this mutant are hyper-stable (13, 15). Most conditional tub2 mutants are cold sensitive, presumably reflecting the intrinsic cold-sensitivity of the microtubule polymer. Tub2p interacts with numerous proteins involved in the regulation of microtubules, such as microtubule motors, SPB components, kinetochore components, tubulin biogenesis factors, and alpha-tubulin (encoded by TUB1 and TUB3) (reviewed in 6, 7).
Tub2p is a GTP-binding protein (for review, see 16). Tub2p hydrolyzes its GTP following tubulin dimer addition to the microtubule end, whereas the GTP bound to Tub1p and Tub3p is non-hydrolyzable (16). The structure of tubulin has been crystallized in the polymerized state; Tub3p and Tub1p, rather than Tub2p, are believed to interact directly with the SPB (17).
Last updated: 2003-12-18
REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for TUB2]
| 1) | Neff NF, et al. (1983) Isolation of the beta-tubulin gene from yeast and demonstration of its essential function in vivo. Cell 33(1):211-9 |
| 2) | Espinet C, et al. (1995) An efficient method to isolate yeast genes causing overexpression-mediated growth arrest. Yeast 11(1):25-32 |
| 3) | McKean PG, et al. (2001) The extended tubulin superfamily. J Cell Sci 114(Pt 15):2723-33 |
| 4) | Nogales E, et al. (1998) Tubulin and FtsZ form a distinct family of GTPases. Nat Struct Biol 5(6):451-8 |
| 5) | Jacobs CW, et al. (1988) Functions of microtubules in the Saccharomyces cerevisiae cell cycle. J Cell Biol 107(4):1409-26 |
| 6) | Winsor B and Schiebel E (1997) Review: an overview of the Saccharomyces cerevisiae microtubule and microfilament cytoskeleton. Yeast 13(5):399-434 |
| 7) | Botstein D, et al. (1997) "The yeast cytoskeleton." Pp. 1-90 in The Molecular and Cellular Biology of the Yeast Saccharomyces: Cell Cycle and Cell Biology, edited by Pringle JR, Broach JR and Jones EW. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press |
| 8) | Knop M, et al. (1999) Microtubule organization by the budding yeast spindle pole body. Biol Cell 91(4-5):291-304 |
| 9) | Kilmartin JV and Adams AE (1984) Structural rearrangements of tubulin and actin during the cell cycle of the yeast Saccharomyces. J Cell Biol 98(3):922-33 |
| 10) | Carminati JL and Stearns T (1999) Cytoskeletal dynamics in yeast. Methods Cell Biol 58:87-105 |
| 11) | Hoyt MA, et al. (1990) Chromosome instability mutants of Saccharomyces cerevisiae that are defective in microtubule-mediated processes. Mol Cell Biol 10(1):223-34 |
| 12) | Stearns T, et al. (1990) Yeast mutants sensitive to antimicrotubule drugs define three genes that affect microtubule function. Genetics 124(2):251-62 |
| 13) | Thomas JH, et al. (1985) Isolation and characterization of mutations in the beta-tubulin gene of Saccharomyces cerevisiae. Genetics 111(4):715-34 |
| 14) | Huffaker TC, et al. (1988) Diverse effects of beta-tubulin mutations on microtubule formation and function. J Cell Biol 106(6):1997-2010 |
| 15) | Machin NA, et al. (1995) Microtubule stability in budding yeast: characterization and dosage suppression of a benomyl-dependent tubulin mutant. Mol Biol Cell 6(9):1241-59 |
| 16) | Mandelkow E and Mandelkow EM (1989) Microtubular structure and tubulin polymerization. Curr Opin Cell Biol 1(1):5-9 |
| 17) | Nogales E, et al. (1999) High-resolution model of the microtubule. Cell 96(1):79-88 |
