Literature DB >> 8221902

Perspectives on tubulin isotype function and evolution based on the observation that Tetrahymena thermophila microtubules contain a single alpha- and beta-tubulin.

J Gaertig1, T H Thatcher, K E McGrath, R C Callahan, M A Gorovsky.   

Abstract

We have cloned and sequenced the two beta-tubulin genes of the ciliated protozoan Tetrahymena thermophila. The two genes encode identical 443 amino acid peptides which are 99.7% identical to the beta-tubulin proteins of T. pyriformis and 95% identical to human beta 1 tubulin. T. thermophila contains only one alpha-tubulin gene (Callahan et al., 1984: Cell 36:441-445). Thus, all of the extremely diverse microtubule structures in this unicellular organism can be formed from a single alpha- and a single beta-tubulin peptide. We have also carried out a phylogenetic analysis of 84 complete beta-tubulin peptide sequences. This analysis supports two hypotheses regarding beta-tubulin evolution and function: 1) Multifunctional beta-tubulins are under greater evolutionary constraint than beta-tubulins present in specialized cells or in cells with very few microtubule related functions, which can evolve rapidly; and 2) Cells which form axonemes maintain a homogeneous population of tubulins.

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Year:  1993        PMID: 8221902     DOI: 10.1002/cm.970250305

Source DB:  PubMed          Journal:  Cell Motil Cytoskeleton        ISSN: 0886-1544


  34 in total

1.  New class of cargo protein in Tetrahymena thermophila dense core secretory granules.

Authors:  Alex Haddad; Grant R Bowman; Aaron P Turkewitz
Journal:  Eukaryot Cell       Date:  2002-08

Review 2.  Post-translational regulation of the microtubule cytoskeleton: mechanisms and functions.

Authors:  Carsten Janke; Jeannette Chloë Bulinski
Journal:  Nat Rev Mol Cell Biol       Date:  2011-11-16       Impact factor: 94.444

3.  Constitutive expression, not a particular primary sequence, is the important feature of the H3 replacement variant hv2 in Tetrahymena thermophila.

Authors:  L Yu; M A Gorovsky
Journal:  Mol Cell Biol       Date:  1997-11       Impact factor: 4.272

4.  Distinct localization of a beta-tubulin epitope in the Tetrahymena thermophila and Paramecium caudatum cortex.

Authors:  L Libusová; T Sulimenko; V Sulimenko; R Janisch; P Hozák; P Dráber
Journal:  Protoplasma       Date:  2005-10-05       Impact factor: 3.356

5.  Basal body duplication and maintenance require one member of the Tetrahymena thermophila centrin gene family.

Authors:  Alexander J Stemm-Wolf; Garry Morgan; Thomas H Giddings; Erin A White; Robb Marchione; Heather B McDonald; Mark Winey
Journal:  Mol Biol Cell       Date:  2005-06-08       Impact factor: 4.138

Review 6.  Back on track - on the role of the microtubule for kinesin motility and cellular function.

Authors:  Stefan Lakämper; Edgar Meyhöfer
Journal:  J Muscle Res Cell Motil       Date:  2006-02-02       Impact factor: 2.698

7.  α-Tubulin mutations alter oryzalin affinity and microtubule assembly properties to confer dinitroaniline resistance.

Authors:  Sally Lyons-Abbott; Dan L Sackett; Dorota Wloga; Jacek Gaertig; Rachel E Morgan; Karl A Werbovetz; Naomi S Morrissette
Journal:  Eukaryot Cell       Date:  2010-09-24

8.  Tubulin polyglycylation: differential posttranslational modification of dynamic cytoplasmic and stable axonemal microtubules in paramecium.

Authors:  M H Bré; V Redeker; J Vinh; J Rossier; N Levilliers
Journal:  Mol Biol Cell       Date:  1998-09       Impact factor: 4.138

9.  Germ-line knockout heterokaryons of an essential alpha-tubulin gene enable high-frequency gene replacement and a test of gene transfer from somatic to germ-line nuclei in Tetrahymena thermophila.

Authors:  B Hai; M A Gorovsky
Journal:  Proc Natl Acad Sci U S A       Date:  1997-02-18       Impact factor: 11.205

10.  The marine red alga Chondrus crispus has a highly divergent beta-tubulin gene with a characteristic 5' intron: functional and evolutionary implications.

Authors:  M F Liaud; U Brandt; R Cerff
Journal:  Plant Mol Biol       Date:  1995-05       Impact factor: 4.076

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