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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

Abstract

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 formore » FtsZ in Chlamydia.« less

Authors:
 [1];  [2];  [1];  [1];  [1];  [3];  [4];  [1]
  1. Univ. of Kansas, Lawrence, KS (United States). Dept. of Molecular Biosciences
  2. Univ. of Kansas, Lawrence, KS (United States). Dept. of Pharmaceutical Chemistry
  3. Univ. of Kansas, Lawrence, KS (United States). Del Shankel Structural Biology Center. Protein Structure Lab.
  4. IMCA-CAT Hauptman-Woodward Medical Research Inst., Argonne, IL (United States)
Publication Date:
Research Org.:
Univ. of Kansas, Lawrence, KS (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES); National Inst. of Health (NIH) (United States)
Contributing Org.:
IMCA-CAT Hauptman-Woodward Medical Research Inst., Argonne, IL (United States)
OSTI Identifier:
1171843
Grant/Contract Number:  
AC02-06CH11357; R03AI081099; AI070089; AI079083; AI103711; 5P20RR017708-10; 8P20GM103420-10
Resource Type:
Accepted Manuscript
Journal Name:
Molecular Microbiology
Additional Journal Information:
Journal Volume: 95; Journal Issue: 3; Journal ID: ISSN 0950-382X
Publisher:
Wiley
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; Chlamydia; RodZ; Morphogenesis; Structure

Citation Formats

Kemege, Kyle E., Hickey, John M., Barta, Michael L., Wickstrum, Jason, Balwalli, Namita, Lovell, Scott, Battaile, Kevin P., and Hefty, P. Scott. Chlamydia trachomatis protein CT009 is a structural and functional homolog to the key morphogenesis component RodZ and interacts with division septal plane localized MreB. United States: N. p., 2014. Web. doi:10.1111/mmi.12855.
Kemege, Kyle E., Hickey, John M., Barta, Michael L., Wickstrum, Jason, Balwalli, Namita, Lovell, Scott, Battaile, Kevin P., & Hefty, P. Scott. Chlamydia trachomatis protein CT009 is a structural and functional homolog to the key morphogenesis component RodZ and interacts with division septal plane localized MreB. United States. https://doi.org/10.1111/mmi.12855
Kemege, Kyle E., Hickey, John M., Barta, Michael L., Wickstrum, Jason, Balwalli, Namita, Lovell, Scott, Battaile, Kevin P., and Hefty, P. Scott. Mon . "Chlamydia trachomatis protein CT009 is a structural and functional homolog to the key morphogenesis component RodZ and interacts with division septal plane localized MreB". United States. https://doi.org/10.1111/mmi.12855. https://www.osti.gov/servlets/purl/1171843.
@article{osti_1171843,
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},
author = {Kemege, Kyle E. and Hickey, John M. and Barta, Michael L. and Wickstrum, Jason and Balwalli, Namita and Lovell, Scott and Battaile, Kevin P. and Hefty, P. Scott},
abstractNote = {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.},
doi = {10.1111/mmi.12855},
journal = {Molecular Microbiology},
number = 3,
volume = 95,
place = {United States},
year = {Mon Nov 10 00:00:00 EST 2014},
month = {Mon Nov 10 00:00:00 EST 2014}
}

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Cited by: 21 works
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