Literature DB >> 16525780

Polyhedral organelles compartmenting bacterial metabolic processes.

Thomas A Bobik1.   

Abstract

Bacterial polyhedral organelles are extremely large macromolecular complexes consisting of metabolic enzymes encased within a multiprotein shell that is somewhat reminiscent of a viral capsid. Recent investigations suggest that polyhedral organelles are widely used by bacteria for optimizing metabolic processes. The distribution and diversity of these unique structures has been underestimated because many are not formed during growth on standard laboratory media and because electron microscopy is required for their observation. However, recent physiological studies and genomic analyses tentatively indicate seven functionally distinct organelles distributed among over 40 genera of bacteria. Functional studies conducted thus far are consistent with the idea that polyhedral organelles act as microcompartments that enhance metabolic processes by selectively concentrating specific metabolites. Relatively little is known about how this is achieved at the molecular level. Possible mechanisms include regulation of enzyme activity or efficiency, substrate channeling, a selectively permeable protein shell, and/or differential solubility of metabolites within the organelle. Given their complexity and distinctive structure, it would not be surprising if aspects of their biochemical mechanism are unique. Therefore, the unusual structure of polyhedral organelles raises intriguing questions about their assembly, turnover, and molecular evolution, very little of which is understood.

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Year:  2006        PMID: 16525780     DOI: 10.1007/s00253-005-0295-0

Source DB:  PubMed          Journal:  Appl Microbiol Biotechnol        ISSN: 0175-7598            Impact factor:   4.813


  65 in total

1.  Elucidating essential role of conserved carboxysomal protein CcmN reveals common feature of bacterial microcompartment assembly.

Authors:  James N Kinney; Annette Salmeen; Fei Cai; Cheryl A Kerfeld
Journal:  J Biol Chem       Date:  2012-03-29       Impact factor: 5.157

2.  Crystallographic insights into the pore structures and mechanisms of the EutL and EutM shell proteins of the ethanolamine-utilizing microcompartment of Escherichia coli.

Authors:  Mihoko Takenoya; Kiel Nikolakakis; Martin Sagermann
Journal:  J Bacteriol       Date:  2010-09-17       Impact factor: 3.490

3.  Addressing microbial organelles: a short peptide directs enzymes to the interior.

Authors:  Sabine Heinhorst; Gordon C Cannon
Journal:  Proc Natl Acad Sci U S A       Date:  2010-04-16       Impact factor: 11.205

4.  Short N-terminal sequences package proteins into bacterial microcompartments.

Authors:  Chenguang Fan; Shouqiang Cheng; Yu Liu; Cristina M Escobar; Christopher S Crowley; Robert E Jefferson; Todd O Yeates; Thomas A Bobik
Journal:  Proc Natl Acad Sci U S A       Date:  2010-03-22       Impact factor: 11.205

5.  Cobinamide production of hydrogen in a homogeneous aqueous photochemical system, and assembly and photoreduction in a (βα)8 protein.

Authors:  Wesley D Robertson; Adonis M Bovell; Kurt Warncke
Journal:  J Biol Inorg Chem       Date:  2013-06-27       Impact factor: 3.358

6.  Characterization of the carboxysomal carbonic anhydrase CsoSCA from Halothiobacillus neapolitanus.

Authors:  Sabine Heinhorst; Eric B Williams; Fei Cai; C Daniel Murin; Jessup M Shively; Gordon C Cannon
Journal:  J Bacteriol       Date:  2006-09-29       Impact factor: 3.490

7.  The carboxysome shell is permeable to protons.

Authors:  Balaraj B Menon; Sabine Heinhorst; Jessup M Shively; Gordon C Cannon
Journal:  J Bacteriol       Date:  2010-09-24       Impact factor: 3.490

8.  Preliminary structural investigations of the Eut-L shell protein of the ethanolamine ammonia-lyase metabolosome of Escherichia coli.

Authors:  Kiel Nikolakakis; Akashi Ohtaki; Keith Newton; Arkadiusz Chworos; Martin Sagermann
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2009-01-31

9.  The C-terminal peptide of Aquifex aeolicus riboflavin synthase directs encapsulation of native and foreign guests by a cage-forming lumazine synthase.

Authors:  Yusuke Azuma; Reinhard Zschoche; Donald Hilvert
Journal:  J Biol Chem       Date:  2017-05-17       Impact factor: 5.157

10.  β-Carboxysomal proteins assemble into highly organized structures in Nicotiana chloroplasts.

Authors:  Myat T Lin; Alessandro Occhialini; P John Andralojc; Jean Devonshire; Kevin M Hines; Martin A J Parry; Maureen R Hanson
Journal:  Plant J       Date:  2014-06-09       Impact factor: 6.417

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