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Structural biology

Synchronized division proteins

Nature volume 391, pages 121–123 (1998)Cite this article

The molecular mechanisms of prokaryotic cell division and eukaryotic mitosis seem to have little in common, yet similarities between the structures of two GTPases published in this week's issue1,2 (pages 199 and 203) will reinforce the need for microbiologists and cell biologists to compare notes. Nogales et al.1 report the 3.8-Å image reconstruction of the tubulin α/β heterodimer, which assembles into the microtubules of, for example, eukaryotic mitotic spindles. Löwe and Amos2, on the other hand, describe the 2.8-Å crystallographic structure of Methanococcus jannaschii FtsZ, which forms a filamentous ring-shaped septum at the division site of prokaryotes.

It has been said that many of the best intelligence-analysts are trained as biologists, because they can solve complex problems from fragmentary, and sometimes conflicting, evidence. The 3.8-Å structure1 of the α/β tubulin dimer is a testament to this skill. It confirms many aspects of the working model built up over the past 30 years from indirect biochemical analysis, such as the effects due to the reactivity of specific cysteine residues on ligand binding, sequence analysis and site-directed mutagenesis. The structure is, of course, more tangible than any previous model, even though its resolution is insufficient to assign functions to specific residues. But it will greatly influence studies into the mechanisms of microtubule assembly, microtubule-based motility and the effects of the commercially important anti-mitotic ligands.

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Figure 1: Orientations of FtsZ and the α- and β-tubulins.

E. NOGALES

Notes

  1. *Bristol-Myers Squibb has registered Taxol as a trademark and wishes the scientific community to use the name paclitaxel.

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  1. the Biophysics Section, Blackett Laboratory, Imperial College of Science, Technology and Medicine, London, SW7 2BZ, UK

    Roy Burns

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  1. Roy Burns
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Burns, R. Synchronized division proteins. Nature 391, 121–123 (1998). https://doi.org/10.1038/34286

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