Document Detail


Characterization of CrgA, a new partner of the Mycobacterium tuberculosis peptidoglycan polymerization complexes.
MedLine Citation:
PMID:  21531798     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The role(s) in cell division of the Mycobacterium tuberculosis Rv0011c gene product, a homolog of the Streptomyces CrgA protein that is responsible for coordinating growth and cytokinesis in sporogenic aerial hyphae, is largely unknown. We show that an enhanced cyan fluorescent protein-M. tuberculosis CrgA (ECFP-CrgA(MT)) fusion protein is localized to the cell membrane, midcell, and cell pole regions in Mycobacterium smegmatis. Furthermore, the ECFP-CrgA(MT) fusion protein colocalized with FtsZ-enhanced yellow fluorescent protein (EYFP) in M. smegmatis. Bacterial two-hybrid assays indicated strong interactions of M. tuberculosis CrgA with FtsZ, FtsQ, and the class B penicillin-binding proteins, FtsI (PBPB) and PBPA. The midcell localization of CrgA(MT) was severely compromised under conditions of FtsZ depletion, which indicated that CrgA localizes to the midcell region after assembly of the FtsZ ring. M. tuberculosis cells with reduced CrgA levels were elongated and grew more slowly than wild-type cells, which indicated defects in cell division, whereas CrgA overproduction did not show growth defects. A M. smegmatis ΔcrgA strain exhibited a bulged cell morphology, elongated cells with a chain-like phenotype, cells with polar bulbous structures, and a modest growth defect. FtsZ and FtsI levels were not affected in cells producing altered levels of CrgA. Septal and membrane localization of GFP-FtsI was enhanced by CrgA overproduction and was diminished in a ΔcrgA strain, which indicates that one role of CrgA is to promote and/or stabilize FtsI localization. Overall, these data indicate that CrgA is a novel member of the cell division complex in mycobacteria and possibly facilitates septum formation.
Authors:
P Plocinski; M Ziolkiewicz; M Kiran; S I Vadrevu; H B Nguyen; J Hugonnet; C Veckerle; M Arthur; J Dziadek; T A Cross; M Madiraju; M Rajagopalan
Related Documents :
1514628 - Immunocytochemical studies suggest two pathways for enteroendocrine cell differentiatio...
2611028 - The whole-mount method as a technique for measuring experimental changes in airway gobl...
2457978 - In vitro translation of rat intestinal rna prepared from isolated villus and crypt cell...
2606508 - Antigen processing by isolated rat intestinal villus enterocytes.
20062078 - Defective dna double-strand break repair underlies enhanced tumorigenesis and chromosom...
8460718 - Cell-specific posttranslational processing of the surfactant-associated protein sp-b.
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2011-04-29
Journal Detail:
Title:  Journal of bacteriology     Volume:  193     ISSN:  1098-5530     ISO Abbreviation:  J. Bacteriol.     Publication Date:  2011 Jul 
Date Detail:
Created Date:  2011-06-15     Completed Date:  2011-08-23     Revised Date:  2013-06-30    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3246-56     Citation Subset:  IM    
Affiliation:
The University of Texas Health Science Center, Tyler, TX 75708, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Bacterial Proteins / analysis,  metabolism*
Cell Membrane / chemistry
Cytoskeletal Proteins / analysis
Genes, Reporter
Green Fluorescent Proteins / analysis,  genetics
Microscopy, Confocal
Mycobacterium tuberculosis / chemistry,  cytology,  genetics,  metabolism*
Penicillin-Binding Proteins / metabolism
Peptidoglycan / biosynthesis*
Protein Binding
Protein Interaction Mapping
Recombinant Fusion Proteins / analysis,  genetics
Transcription Factors / metabolism*
Two-Hybrid System Techniques
Grant Support
ID/Acronym/Agency:
AI084734/AI/NIAID NIH HHS; AI48417/AI/NIAID NIH HHS; AI73891/AI/NIAID NIH HHS; R01 AI048417-05/AI/NIAID NIH HHS; R01 AI073891-05/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/CrgA protein, Neisseria meningitidis; 0/Cytoskeletal Proteins; 0/FtsZ protein, Bacteria; 0/Penicillin-Binding Proteins; 0/Peptidoglycan; 0/Recombinant Fusion Proteins; 0/Transcription Factors; 0/enhanced cyan fluorescent protein; 147336-22-9/Green Fluorescent Proteins
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  The anaerobe-specific orange protein complex of Desulfovibrio vulgaris hildenborough is encoded by t...
Next Document:  Dual function of a tip fimbrillin of Actinomyces in fimbrial assembly and receptor binding.