Chlamydia trachomatis protein CT009 is a structural and functional homolog to the key morphogenesis component RodZ and interacts with division septal plane localized MreB

Kemege, Kyle E.; Hickey, John M.; Barta, Michael L.; Wickstrum, Jason; Balwalli, Namita; Lovell, Scott; Battaile, Kevin P.; Hefty, P. Scott

doi:10.1111/mmi.12855

Title: Chlamydia trachomatis protein CT009 is a structural and functional homolog to the key morphogenesis component RodZ and interacts with division septal plane localized MreB

Journal Article · Mon Nov 10 00:00:00 EST 2014 · Molecular Microbiology

DOI:https://doi.org/10.1111/mmi.12855· OSTI ID:1171843

Kemege, Kyle E. ^[1]; Hickey, John M. ^[2]; Barta, Michael L. ^[1]; Wickstrum, Jason ^[1]; Balwalli, Namita ^[1]; Lovell, Scott ^[3]; Battaile, Kevin P. ^[4]; Hefty, P. Scott ^[1]

Univ. of Kansas, Lawrence, KS (United States). Dept. of Molecular Biosciences
Univ. of Kansas, Lawrence, KS (United States). Dept. of Pharmaceutical Chemistry
Univ. of Kansas, Lawrence, KS (United States). Del Shankel Structural Biology Center. Protein Structure Lab.
IMCA-CAT Hauptman-Woodward Medical Research Inst., Argonne, IL (United States)

Cell division in Chlamydiae is poorly understood as apparent homologs to most conserved bacterial cell division proteins are lacking and presence of elongation (rod shape) associated proteins indicate non-canonical mechanisms may be employed. The rod-shape determining protein MreB has been proposed as playing a unique role in chlamydial cell division. In other organisms, MreB is part of an elongation complex that requires RodZ for proper function. A recent study reported that the protein encoded by ORF CT009 interacts with MreB despite low sequence similarity to RodZ. The studies in this paper expand on those observations through protein structure, mutagenesis and cellular localization analyses. Structural analysis indicated that CT009 shares high level of structural similarity to RodZ, revealing the conserved orientation of two residues critical for MreB interaction. Substitutions eliminated MreB protein interaction and partial complementation provided by CT009 in RodZ deficient Escherichia coli. Cellular localization analysis of CT009 showed uniform membrane staining in Chlamydia. This was in contrast to the localization of MreB, which was restricted to predicted septal planes. Finally, MreB localization to septal planes provides direct experimental observation for the role of MreB in cell division and supports the hypothesis that it serves as a functional replacement for FtsZ in Chlamydia.

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Research Organization:: Univ. of Kansas, Lawrence, KS (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES); National Inst. of Health (NIH) (United States)

Contributing Organization:: IMCA-CAT Hauptman-Woodward Medical Research Inst., Argonne, IL (United States)

Grant/Contract Number:: AC02-06CH11357; R03AI081099; AI070089; AI079083; AI103711; 5P20RR017708-10; 8P20GM103420-10

OSTI ID:: 1171843

Journal Information:: Molecular Microbiology, Vol. 95, Issue 3; ISSN 0950-382X

Publisher:: WileyCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 21 works

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59 BASIC BIOLOGICAL SCIENCES
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Title: Chlamydia trachomatis protein CT009 is a structural and functional homolog to the key morphogenesis component RodZ and interacts with division septal plane localized MreB

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