ArticlePloS one2009
BtubA-BtubB heterodimer is an essential intermediate in protofilament assembly.
Article in PloS one, 2009. 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.
- Nanoparticle-assisted tubulin assembly is environment dependent.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- All tubulins are not alike: Heterodimer dissociation differs among different biological sources.The Journal of biological chemistry · 2019Article
- Bacterial Tubulins A and B Exhibit Polarized Growth, Mixed-Polarity Bundling, and Destabilization by GTP Hydrolysis.Journal of bacteriology · 2017Article
- The Chloroplast Tubulin Homologs FtsZA and FtsZB from the Red AlgaThe Journal of biological chemistry · 2017Article
- Bacterial kinesin light chain (Bklc) links the Btub cytoskeleton to membranes.Scientific reports · 2017Article
- Tubulin Dimer Reversible Dissociation: AFFINITY, KINETICS, AND DEMONSTRATION OF A STABLE MONOMER.The Journal of biological chemistry · 2016Article
- Biochemical methods for studying kinetic regulation of Arf1 activation by Sec7.Methods in cell biology · 2015Article
- Six subgroups and extensive recent duplications characterize the evolution of the eukaryotic tubulin protein family.Genome biology and evolution · 2014Article
- SulA inhibits assembly of FtsZ by a simple sequestration mechanism.Biochemistry · 2012Article
- Microtubules in bacteria: Ancient tubulins build a five-protofilament homolog of the eukaryotic cytoskeleton.PLoS biology · 2011Article
- Transitional forms between the three domains of life and evolutionary implications.Proceedings. Biological sciences · 2011Article
- The evolution of the cytoskeleton.The Journal of cell biology · 2011Review
- Inside-out Z rings--constriction with and without GTP hydrolysis.Molecular microbiology · 2011Article
- Bacterial tubulin distinct loop sequences and primitive assembly properties support its origin from a eukaryotic tubulin ancestor.The Journal of biological chemistry · 2011Article
- FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one.Microbiology and molecular biology reviews : MMBR · 2010Review
- GTP-dependent heteropolymer formation and bundling of chloroplast FtsZ1 and FtsZ2.The Journal of biological chemistry · 2010Article
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Authors and funding
3 authors.
Funding
Abstract
backgroundBtubA and BtubB are two tubulin-like genes found in the bacterium Prosthecobacter. Our work and a previous crystal structure suggest that BtubB corresponds to alpha-tubulin and BtubA to beta-tubulin. A 1:1 mixture of the two proteins assembles into tubulin-like protofilaments, which further aggregate into pairs and bundles. The proteins also form a BtubA/B heterodimer, which appears to be a repeating subunit in the protofilament. METHODOLOGY/PRINCIPAL
findingsWe have designed point mutations to disrupt the longitudinal interfaces bonding subunits into protofilaments. The mutants are in two classes, within dimers and between dimers. We have characterized one mutant of each class for BtubA and BtubB. When mixed 1:1 with a wild type partner, none of the mutants were capable of assembly. An excess of between-dimer mutants could depolymerize preformed wild type polymers, while within-dimer mutants had no activity.
conclusionsAn essential first step in assembly of BtubA + BtubB is formation of a heterodimer. An excess of between-dimer mutants depolymerize wild type BtubA/B by sequestering the partner wild type subunit into inactive dimers. Within-dimer mutants cannot form dimers and have no activity.
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