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Tetramerization of ZapA is required for FtsZ bundling
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Pacheco‑Gómez, Raúl, Cheng, Xi, Hicks, Matthew R., Smith, Corinne J., Roper, David I., Addinall, Stephen G., Rodger, Alison and Dafforn, Tim (2013) Tetramerization of ZapA is required for FtsZ bundling. Biochemical Journal, Volume 449 (Number 3). pp. 795-802. doi:10.1042/BJ20120140
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Official URL: http://dx.doi.org/10.1042/BJ20120140
Abstract
Prokaryotic cell division is a highly orchestrated process requiring the formation of a wide range of biomolecular complexes, perhaps the most important of these involving the prokaryotic tubulin homologue FtsZ, a fibre-forming GTPase. FtsZ assembles into a ring (the Z-ring) on the inner surface of the inner membrane at the site of cell division. The Z-ring then acts as a recruitment site for at least ten other proteins which form the division apparatus. One of these proteins, ZapA, acts to enhance lateral associations between FtsZ fibres to form bundles. Previously we have expressed, purified and crystallized ZapA and demonstrated that it exists as a tetramer. We also showed that ZapA binds to FtsZ polymers, strongly promoting their bundling, while inhibiting FtsZ GTPase activity by inducing conformational changes in the bound nucleotide. In the present study we investigate the importance of the tetramerization of ZapA on its function. We generated a number of mutant forms of ZapA with the aim of disrupting the dimer–dimer interface. We show that one of these mutants, I83E, is fully folded and binds to FtsZ, but is a constitutive dimer. Using this mutant we show that tetramerization is a requirement for both FtsZ bundling and GTPase modulation activities.
| Item Type: | Journal Article | ||||
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| Divisions: | Faculty of Science > Chemistry Faculty of Science > Life Sciences (2010- ) |
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| Journal or Publication Title: | Biochemical Journal | ||||
| Publisher: | Portland Press | ||||
| ISSN: | 0264-6021 | ||||
| Official Date: | 1 February 2013 | ||||
| Dates: |
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| Volume: | Volume 449 | ||||
| Number: | Number 3 | ||||
| Page Range: | pp. 795-802 | ||||
| DOI: | 10.1042/BJ20120140 | ||||
| Status: | Peer Reviewed | ||||
| Publication Status: | Published | ||||
| Access rights to Published version: | Restricted or Subscription Access | ||||
| Funder: | Biotechnology and Biological Sciences Research Council (BBSRC), Medical Research Council (MRC), Engineering and Physical Sciences Research Council (EPSRC) |
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