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PMID: 12003935 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

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.

Journal of bacteriology ·Vol. 184 ·No. 11 ·2002-06-00 ·Pages 2951-62

Johnson JE, Lackner LL, de Boer PA

Abstract

The MinC protein is an important determinant of septal ring positioning in Escherichia coli. The N-terminal domain ((Z)MinC) suppresses septal ring formation by interfering with FtsZ polymerization, whereas the C-terminal domain ((D)MinC) is required for dimerization as well as for interaction with the MinD protein. MinD oscillates between the membrane of both cell halves in a MinE-dependent fashion. MinC oscillates along with MinD such that the time-integrated concentration of (Z)MinC at the membrane is minimal, and hence the stability of FtsZ polymers is maximal, at the cell center. MinC is cytoplasmic and fails to block FtsZ assembly in the absence of MinD, indicating that recruitment of MinC by MinD to the membrane enhances (Z)MinC function. Here, we present evidence that the binding of (D)MinC to MinD endows the MinC/MinD complex with a more specific affinity for a septal ring-associated target in vivo. Thus, MinD does not merely attract MinC to the membrane but also aids MinC in specifically binding to, or in close proximity to, the substrate of its (Z)MinC domain. MinC-mediated division inhibition can also be activated in a MinD-independent fashion by the DicB protein of cryptic prophage Kim. DicB shows little homology to MinD, and how it stimulates MinC function has been unclear. Similar to the results obtained with MinD, we find that DicB interacts directly with (D)MinC, that the (D)MinC/DicB complex has a high affinity for some septal ring target(s), and that MinC/DicB interferes with the assembly and/or integrity of FtsZ rings in vivo. The results suggest a multistep mechanism for the activation of MinC-mediated division inhibition by either MinD or DicB and further expand the number of properties that can be ascribed to the Min proteins.

MeSH Terms
Adenosine Triphosphatases/metabolism Bacillus subtilis/metabolism Bacterial Proteins/metabolism Cell Cycle Proteins/metabolism Cell Division Cytoskeletal Proteins Escherichia coli/cytology,metabolism Escherichia coli Proteins GTP Phosphohydrolases/metabolism Membrane Proteins/metabolism
Chemicals
Bacterial Proteins Cell Cycle Proteins Cytoskeletal Proteins Escherichia coli Proteins FtsZ protein, Bacteria Membrane Proteins MinC protein, Bacteria Adenosine Triphosphatases GTP Phosphohydrolases MinD protein, E coli
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Johnson Jay E
Department of Molecular Biology and Microbiology, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106-4960, USA.
Lackner Laura L
de Boer Piet A J
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/JB.184.11.2951-2962.2002
Published
2002-06-00
Pages
2951-62
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC135045
Subset
IM
Grants
NIGMS NIH HHS · R01 GM057059 · United States
NIGMS NIH HHS · T32 GM008056 · United States
NIGMS NIH HHS · GM57059 · United States
NIGMS NIH HHS · T32GM08056 · United States
External Links
PubMed source DOI: 10.1128/JB.184.11.2951-2962.2002 PMC Full Text View journal details
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