Literature DB >> 14763969

Cellular engineering in a minimal microbe: structure and assembly of the terminal organelle of Mycoplasma pneumoniae.

Duncan C Krause1, Mitchell F Balish.   

Abstract

Mycoplasma pneumoniae is a minimal microbe with respect to cell envelope composition, biosynthetic and regulatory capabilities and genome size, yet it possesses a remarkably complex, multifunctional terminal organelle. This membrane-bound extension of the mycoplasma cell is defined by the presence of an electron-dense core that appears as paired, parallel bars oriented longitudinally and enlarging at the distal end to form a terminal button. Most non-cytadhering mutants of M. pneumoniae isolated to date exhibit defects in the architecture of the terminal organelle. Detailed characterization of those mutants has revealed the identities of many component proteins of the terminal organelle as well as the likely order in which some of those components are required. Additional questions regarding the composition of the electron-dense core, the means by which the terminal organelle is duplicated during cell division and the manner in which this process is regulated remain to be answered. Thus, it seems that there is much to be learned about cellular engineering and spatial regulation in these 'simple' cell wall-less bacteria.

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Year:  2004        PMID: 14763969     DOI: 10.1046/j.1365-2958.2003.03899.x

Source DB:  PubMed          Journal:  Mol Microbiol        ISSN: 0950-382X            Impact factor:   3.501


  50 in total

1.  Loss of co-chaperone TopJ impacts adhesin P1 presentation and terminal organelle maturation in Mycoplasma pneumoniae.

Authors:  Jason M Cloward; Duncan C Krause
Journal:  Mol Microbiol       Date:  2011-06-23       Impact factor: 3.501

2.  Use of fluorescent-protein tagging to determine the subcellular localization of mycoplasma pneumoniae proteins encoded by the cytadherence regulatory locus.

Authors:  Tsuyoshi Kenri; Shintaro Seto; Atsuko Horino; Yuko Sasaki; Tsuguo Sasaki; Makoto Miyata
Journal:  J Bacteriol       Date:  2004-10       Impact factor: 3.490

3.  P65 truncation impacts P30 dynamics during Mycoplasma pneumoniae gliding.

Authors:  Benjamin M Hasselbring; Edward S Sheppard; Duncan C Krause
Journal:  J Bacteriol       Date:  2012-04-27       Impact factor: 3.490

4.  Isolation and characterization of P1 adhesin, a leg protein of the gliding bacterium Mycoplasma pneumoniae.

Authors:  Daisuke Nakane; Jun Adan-Kubo; Tsuyoshi Kenri; Makoto Miyata
Journal:  J Bacteriol       Date:  2010-11-19       Impact factor: 3.490

5.  Functional analysis of the Mycoplasma genitalium MG312 protein reveals a specific requirement of the MG312 N-terminal domain for gliding motility.

Authors:  Raul Burgos; Oscar Q Pich; Enrique Querol; Jaume Piñol
Journal:  J Bacteriol       Date:  2007-08-03       Impact factor: 3.490

6.  HMW1 is required for stability and localization of HMW2 to the attachment organelle of Mycoplasma pneumoniae.

Authors:  Melisa J Willby; Mitchell F Balish; Stephanie M Ross; Kyungok K Lee; Jarrat L Jordan; Duncan C Krause
Journal:  J Bacteriol       Date:  2004-12       Impact factor: 3.490

7.  Identification and complementation of a mutation associated with loss of Mycoplasma pneumoniae virulence-specific proteins B and C.

Authors:  Robert H Waldo; Jarrat L Jordan; Duncan C Krause
Journal:  J Bacteriol       Date:  2005-01       Impact factor: 3.490

8.  Morphology of isolated Gli349, a leg protein responsible for Mycoplasma mobile gliding via glass binding, revealed by rotary shadowing electron microscopy.

Authors:  Jun Adan-Kubo; Atsuko Uenoyama; Toshiaki Arata; Makoto Miyata
Journal:  J Bacteriol       Date:  2006-04       Impact factor: 3.490

Review 9.  New insights into the pathogenesis and detection of Mycoplasma pneumoniae infections.

Authors:  Ken B Waites; Mitchell F Balish; T Prescott Atkinson
Journal:  Future Microbiol       Date:  2008-12       Impact factor: 3.165

10.  Identification of a 123-kilodalton protein (Gli123) involved in machinery for gliding motility of Mycoplasma mobile.

Authors:  Atsuko Uenoyama; Makoto Miyata
Journal:  J Bacteriol       Date:  2005-08       Impact factor: 3.490

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