Polyhedral organelles compartmenting bacterial metabolic processes

被引:93
作者
Bobik, TA [1 ]
机构
[1] Iowa State Univ, Dept Biochem Biophys & Mol Biol, Ames, IA 50011 USA
关键词
D O I
10.1007/s00253-005-0295-0
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
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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页码:517 / 525
页数:9
相关论文
共 67 条
[31]   SALMONELLA-TYPHIMURIUM SYNTHESIZES COBALAMIN (VITAMIN-B12) DENOVO UNDER ANAEROBIC GROWTH-CONDITIONS [J].
JETER, RM ;
OLIVERA, BM ;
ROTH, JR .
JOURNAL OF BACTERIOLOGY, 1984, 159 (01) :206-213
[32]   Functional genomic, biochemical, and genetic characterization of the Salmonella pduO gene, an ATP:cob(I)alamin adenosyltransferase gene [J].
Johnson, CLV ;
Pechonick, E ;
Park, SD ;
Havemann, GD ;
Leal, NA ;
Bobik, TA .
JOURNAL OF BACTERIOLOGY, 2001, 183 (05) :1577-1584
[33]   Purification and initial characterization of the Salmonella enterica PduO ATP:cob(I)alamin adenosyltransferase [J].
Johnson, CLV ;
Buszko, ML ;
Bobik, TA .
JOURNAL OF BACTERIOLOGY, 2004, 186 (23) :7881-7887
[34]   Acclimation of photosynthetic microorganisms to changing ambient CO2 concentration [J].
Kaplan, A ;
Helman, Y ;
Tchernov, D ;
Reinhold, L .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (09) :4817-4818
[35]   CO2 concentrating mechanisms in photosynthetic microorganisms [J].
Kaplan, A ;
Reinhold, L .
ANNUAL REVIEW OF PLANT PHYSIOLOGY AND PLANT MOLECULAR BIOLOGY, 1999, 50 :539-+
[36]   ANALYSIS OF HIGH CO2 REQUIRING MUTANTS INDICATES A CENTRAL ROLE FOR THE 5' FLANKING REGION OF RBC AND FOR THE CARBOXYSOMES IN CYANOBACTERIAL PHOTOSYNTHESIS [J].
KAPLAN, A .
CANADIAN JOURNAL OF BOTANY-REVUE CANADIENNE DE BOTANIQUE, 1990, 68 (06) :1303-1310
[37]   Protein structures forming the shell of primitive bacterial organelles [J].
Kerfeld, CA ;
Sawaya, MR ;
Tanaka, S ;
Nguyen, CV ;
Phillips, M ;
Beeby, M ;
Yeates, TO .
SCIENCE, 2005, 309 (5736) :936-938
[38]   The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes five homologues of carboxysome shell proteins [J].
Kofoid, E ;
Rappleye, C ;
Stojiljkovic, I ;
Roth, J .
JOURNAL OF BACTERIOLOGY, 1999, 181 (17) :5317-5329
[39]   PduP is a coenzyme-a-acylating propionaldehyde dehydrogenase associated with the polyhedral bodies involved in B12-dependent 1,2-propanediol degradation by Salmonella enterica serovar Typhimurium LT2 [J].
Leal, NA ;
Havemann, GD ;
Bobik, TA .
ARCHIVES OF MICROBIOLOGY, 2003, 180 (05) :353-361
[40]   HIGH CO2 REQUIRING MUTANT OF ANACYSTIS-NIDULANS R2 [J].
MARCUS, Y ;
SCHWARZ, R ;
FRIEDBERG, D ;
KAPLAN, A .
PLANT PHYSIOLOGY, 1986, 82 (02) :610-612