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Mutations in the bacterial cell division protein FtsZ highlight the role of GTP binding and longitudinal subunit interactions in assembly and function

Overview of attention for article published in BMC Microbiology, October 2015
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  • Above-average Attention Score compared to outputs of the same age and source (64th percentile)

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Title
Mutations in the bacterial cell division protein FtsZ highlight the role of GTP binding and longitudinal subunit interactions in assembly and function
Published in
BMC Microbiology, October 2015
DOI 10.1186/s12866-015-0544-z
Pubmed ID
Authors

Heidi A. Arjes, Bradley Lai, Ezinwanne Emelue, Adriana Steinbach, Petra Anne Levin

Abstract

Assembly of the tubulin-like GTPase, FtsZ, at the future division site initiates the process of bacterial cytokinesis. The FtsZ ring serves as a platform for assembly of the division machinery and constricts at the leading edge of the invaginating septum during cytokinesis. In vitro, FtsZ assembles in a GTP-dependent manner, forming straight filaments that curve upon GTP hydrolysis. FtsZ binds but cannot hydrolyze GTP as a monomer. Instead, the active site for GTP hydrolysis is formed at the monomer-monomer interface upon dimerization. While the dynamics of GTP hydrolysis and assembly have been extensively studied in vitro, significantly less is known about the role of GTP binding and hydrolysis in vivo. ftsZ84, a GTPase defective allele of Escherichia coli ftsZ, provides a striking example of the disconnect between in vivo and in vitro FtsZ assembly. Although ftsZ84 mutants are defective for FtsZ ring formation and division under nonpermissive conditions, they are near wild type for ring formation and division under permissive conditions. In vitro, however, purified FtsZ84 is defective in GTP binding, hydrolysis and assembly under standard reaction conditions. To clarify the nature of the FtsZ84 assembly defect, we isolated and characterized three intragenic suppressors of ftsZ84. All three suppressor mutations increased the apparent affinity of FtsZ84 for GTP, consistent with improved subunit-subunit interactions along the longitudinal interface. Although kinetic analysis indicates that the suppressor mutations increase the affinity of FtsZ84 for GTP, all three exhibit reduced rates of GTP hydrolysis and fail to support assembly in vitro. Together, our data suggest that FtsZ, and potentially other enzymes whose assembly is similarly regulated, can compensate for defects in catalysis through increases in substrate binding and subunit-subunit interactions. In addition, these results highlight the dichotomy between commonly used in vitro assembly conditions and FtsZ ring formation in the complex intracellular milieu.

Twitter Demographics

The data shown below were collected from the profiles of 2 tweeters who shared this research output. Click here to find out more about how the information was compiled.

Mendeley readers

The data shown below were compiled from readership statistics for 50 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 1 2%
Unknown 49 98%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 19 38%
Researcher 6 12%
Student > Bachelor 5 10%
Student > Master 4 8%
Student > Doctoral Student 4 8%
Other 5 10%
Unknown 7 14%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 15 30%
Agricultural and Biological Sciences 12 24%
Immunology and Microbiology 6 12%
Medicine and Dentistry 4 8%
Chemistry 2 4%
Other 3 6%
Unknown 8 16%

Attention Score in Context

This research output has an Altmetric Attention Score of 2. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 27 October 2015.
All research outputs
#2,873,359
of 6,496,325 outputs
Outputs from BMC Microbiology
#537
of 1,189 outputs
Outputs of similar age
#100,863
of 206,609 outputs
Outputs of similar age from BMC Microbiology
#18
of 68 outputs
Altmetric has tracked 6,496,325 research outputs across all sources so far. This one has received more attention than most of these and is in the 53rd percentile.
So far Altmetric has tracked 1,189 research outputs from this source. They receive a mean Attention Score of 2.9. This one is in the 49th percentile – i.e., 49% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 206,609 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 46th percentile – i.e., 46% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 68 others from the same source and published within six weeks on either side of this one. This one has gotten more attention than average, scoring higher than 64% of its contemporaries.