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Título: | Control by Potassium of the Size Distribution of Escherichia coli FtsZ Polymers Is Independent of GTPase Activity |
Autor: | Ahijado-Guzmán, Rubén CSIC ORCID; Alfonso, Carlos CSIC ORCID ; Reija, Belén CSIC; Salvarelli, Estefanía; Mingorance, Jesús CSIC ORCID; Zorrilla, Silvia CSIC ORCID ; Monterroso, Begoña CSIC ORCID ; Rivas, Germán CSIC ORCID CVN | Fecha de publicación: | 2013 | Editor: | American Society for Biochemistry and Molecular Biology | Citación: | Journal of Biological Chemistry 288: 27358- 27365 (2013) | Resumen: | The influence of potassium content (at neutral pH and millimolar Mg(2+)) on the size distribution of FtsZ polymers formed in the presence of constantly replenished GTP under steady-state conditions was studied by a combination of biophysical methods. The size of the GTP-FtsZ polymers decreased with lower potassium concentration, in contrast with the increase in the mass of the GDP-FtsZ oligomers, whereas no effect was observed on FtsZ GTPase activity and critical concentration of polymerization. Remarkably, the concerted formation of a narrow size distribution of GTP-FtsZ polymers previously observed at high salt concentration was maintained in all KCl concentrations tested. Polymers induced with guanosine 5'-(¿,ß-methylene)triphosphate, a slowly hydrolyzable analog of GTP, became larger and polydisperse as the potassium concentration was decreased. Our results suggest that the potassium dependence of the GTP-FtsZ polymer size may be related to changes in the subunit turnover rate that are independent of the GTP hydrolysis rate. The formation of a narrow size distribution of FtsZ polymers under very different solution conditions indicates that it is an inherent feature of FtsZ, not observed in other filament-forming proteins, with potential implications in the structural organization of the functional Z-ring | URI: | http://hdl.handle.net/10261/114623 | DOI: | 10.1074/jbc.M113.482943 | Identificadores: | doi: 10.1074/jbc.M113.482943 issn: 0021-9258 |
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