Substitution of a conserved aspartate allows cation-induced polymerization of FtsZ.

Abstract:

:The prokaryotic tubulin homologue FtsZ polymerizes in vitro in a nucleotide dependent fashion. Here we report that replacement of the strictly conserved Asp212 residue of Escherichia coli FtsZ by a Cys or Asn, but not by a Glu residue results in FtsZ that polymerizes with divalent cations in the absence of added GTP. FtsZ D212C and D212N mutants co-purify with GTP as bound nucleotide, providing an explanation for the unusual phenotype. We conclude that D212 plays a critical role in the coordination of a metal ion and the nucleotide at the interface of two FtsZ monomers.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Scheffers DJ,de Wit JG,den Blaauwen T,Driessen AJ

doi

10.1016/s0014-5793(01)02310-9

keywords:

subject

Has Abstract

pub_date

2001-04-06 00:00:00

pages

34-7

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(01)02310-9

journal_volume

494

pub_type

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