Literature DB >> 8930908

FtsZ-spirals and -arcs determine the shape of the invaginating septa in some mutants of Escherichia coli.

S G Addinall1, J Lutkenhaus.   

Abstract

The essential cell division protein FtsZ forms a dynamic ring structure at the future division site. This Z-ring contracts during cell division while maintaining a position at the leading edge of the invaginating septum. Using immunofluorescence microscopy we have characterized two situations in which non-ring FtsZ structures are formed. In ftsZ26 (temperature sensitive, Ts) mutant cells, FtsZ-spirals are formed and lead to formation of spirally invaginating septa, which in turn cause morphological abnormalities. In rodAoul mutant cells, which grow as spheres instead of rods, FtsZ-arcs are formed where asymmetric septal invaginations are initiated. The FtsZ-arcs later mature into complete FtsZ-rings. Our data show that Z-spirals and Z-arcs can contract and that in doing so, they determine the shape of the invaginating septa. These results also strongly suggest that in normal cell division, FtsZ is positioned to a single nucleation site on the inner membrane, from which it polymerizes bidirectionally around the cell circumference to form the Z-ring.

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Year:  1996        PMID: 8930908     DOI: 10.1046/j.1365-2958.1996.00100.x

Source DB:  PubMed          Journal:  Mol Microbiol        ISSN: 0950-382X            Impact factor:   3.501


  91 in total

1.  Direct interaction between the cell division protein FtsZ and the cell differentiation protein SpoIIE.

Authors:  I Lucet; A Feucht; M D Yudkin; J Errington
Journal:  EMBO J       Date:  2000-04-03       Impact factor: 11.598

2.  On the origin of branches in Escherichia coli.

Authors:  B Gullbrand; T Akerlund; K Nordström
Journal:  J Bacteriol       Date:  1999-11       Impact factor: 3.490

3.  Straight and curved conformations of FtsZ are regulated by GTP hydrolysis.

Authors:  C Lu; M Reedy; H P Erickson
Journal:  J Bacteriol       Date:  2000-01       Impact factor: 3.490

4.  Cell division in Escherichia coli: role of FtsL domains in septal localization, function, and oligomerization.

Authors:  J M Ghigo; J Beckwith
Journal:  J Bacteriol       Date:  2000-01       Impact factor: 3.490

5.  The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization.

Authors:  Z Hu; A Mukherjee; S Pichoff; J Lutkenhaus
Journal:  Proc Natl Acad Sci U S A       Date:  1999-12-21       Impact factor: 11.205

6.  Tubulin-like protofilaments in Ca2+-induced FtsZ sheets.

Authors:  J Löwe; L A Amos
Journal:  EMBO J       Date:  1999-05-04       Impact factor: 11.598

7.  Constitutive septal murein synthesis in Escherichia coli with impaired activity of the morphogenetic proteins RodA and penicillin-binding protein 2.

Authors:  M A de Pedro; W D Donachie; J V Höltje; H Schwarz
Journal:  J Bacteriol       Date:  2001-07       Impact factor: 3.490

8.  Exploring intracellular space: function of the Min system in round-shaped Escherichia coli.

Authors:  Brian D Corbin; Xuan-Chuan Yu; William Margolin
Journal:  EMBO J       Date:  2002-04-15       Impact factor: 11.598

9.  Targeting of (D)MinC/MinD and (D)MinC/DicB complexes to septal rings in Escherichia coli suggests a multistep mechanism for MinC-mediated destruction of nascent FtsZ rings.

Authors:  Jay E Johnson; Laura L Lackner; Piet A J de Boer
Journal:  J Bacteriol       Date:  2002-06       Impact factor: 3.490

Review 10.  Biochemistry and comparative genomics of SxxK superfamily acyltransferases offer a clue to the mycobacterial paradox: presence of penicillin-susceptible target proteins versus lack of efficiency of penicillin as therapeutic agent.

Authors:  Colette Goffin; Jean-Marie Ghuysen
Journal:  Microbiol Mol Biol Rev       Date:  2002-12       Impact factor: 11.056

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