ArticleThe Plant cell1990
Missense mutations at lysine 350 in beta 2-tubulin confer altered sensitivity to microtubule inhibitors in Chlamydomonas.
Article in The Plant cell, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- A Novel Variant in TUBB4B Causes Progressive Cone-Rod Dystrophy and Early Onset Sensorineural Hearing Loss.Molecular genetics & genomic medicine · 2025Article
- Dinitroaniline herbicides: a comprehensive review of toxicity and side effects on animal non-target organisms.Environmental science and pollution research international · 2022Review
- Chlamydomonas reinhardtii tubulin-gene disruptants for efficient isolation of strains bearing tubulin mutations.PloS one · 2020Article
- Novel α-Tubulin Mutations Conferring Resistance to Dinitroaniline Herbicides inFrontiers in plant science · 2018Article
- HeLife · 2017Article
- Microtubule drugs: action, selectivity, and resistance across the kingdoms of life.Protoplasma · 2014Review
- Random mutagenesis of β-tubulin defines a set of dispersed mutations that confer paclitaxel resistance.Pharmaceutical research · 2012Article
- Molecular bases for sensitivity to tubulin-binding herbicides in green foxtail.Plant physiology · 2004Article
- Molecular characterization of four beta-tubulin genes from dinitroaniline susceptible and resistant biotypes of Eleusine indica.Plant molecular biology · 1999Article
- Alpha-tubulin missense mutations correlate with antimicrotubule drug resistance in Eleusine indica.The Plant cell · 1998Article
- Gene-specific signal transduction between microtubules and tubulin genes in Tetrahymena thermophila.Molecular and cellular biology · 1995Article
- ida4-1, ida4-2, and ida4-3 are intron splicing mutations affecting the locus encoding p28, a light chain of Chlamydomonas axonemal inner dynein arms.Molecular biology of the cell · 1995Article
- 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 · 1994Article
- Molecular Modeling Indicates that Two Chemically Distinct Classes of Anti-Mitotic Herbicide Bind to the Same Receptor Site(s).Plant physiology · 1994Article
- Article
- The colR4 and colR15 beta-tubulin mutations in Chlamydomonas reinhardtii confer altered sensitivities to microtubule inhibitors and herbicides by enhancing microtubule stability.The Journal of cell biology · 1991Article
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2 authors.
Funding
Abstract
Two beta-tubulin mutants of Chlamydomonas reinhardtii, colR4 and colR15, were previously isolated in our laboratory. Each mutant expressed an acidic beta-tubulin variant as a result of an alteration in the coding sequence of one of the two beta-tubulin genes in C. reinhardtii, which in the wild type encode identical proteins. In this report, we describe the identity of the specific beta-tubulin altered in the colR mutants and the precise nature of the genetic lesions. Hybrid selection of mutant poly(A)+ RNA with cDNA probes specific for the two beta-tubulins in C. reinhardtii indicated that both mutations resided in the beta 2-tubulin gene. cDNA libraries were constructed with mutant poly(A)+ RNA, and beta 2-tubulin cDNA clones were isolated. Results of in vitro transcription of cloned beta 2-tubulin cDNAs confirmed the identity of the altered genes. Sequencing of the entire coding regions of the beta 2-tubulin cDNA clones revealed that the mutants carried different single-base substitutions in the same codon for the amino acid at position 350 in the beta 2-tubulin sequence, effecting a change from a lysine to a glutamic acid in the colR4 variant and to a methionine in the colR15 variant. These changes in amino acids are consistent with the difference in the charge of the two variant polypeptides observed in isoelectric focusing. Because both the colR4 and colR15 mutations confer an altered sensitivity to a number of different microtubule inhibitors and herbicides, lysine 350 appears to be of functional importance in the structure of the tubulin molecule.
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