Genetic Analysis of the Protein Shell of the Microcompartments Involved in Coenzyme B12-Dependent 1,2-Propanediol Degradation by Salmonella

Cheng, Shouqiang; Sinha, Sharmistha; Fan, Chenguang; Liu, Yu; Bobik, Thomas A.

doi:10.1128/jb.01473-10

Cited by 104Bacterial Genetics and BiotechnologyMicrobial metabolism and enzyme functionMicrobial Metabolic Engineering and Bioproduction

Genetic Analysis of the Protein Shell of the Microcompartments Involved in Coenzyme B12-Dependent 1,2-Propanediol Degradation by Salmonella

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Cheng, Shouqiang, Sinha, Sharmistha, Fan, Chenguang, Liu, Yu, Bobik, Thomas A.·2011·Journal of Bacteriology

DOI 10.1128/jb.01473-10PMC PMC3067621

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Abstract

Hundreds of bacterial species use microcompartments (MCPs) to optimize metabolic pathways that have toxic or volatile intermediates. MCPs consist of a protein shell encapsulating specific metabolic enzymes. In Salmonella, an MCP is used for 1,2-propanediol utilization (Pdu MCP). The shell of this MCP is composed of eight different types of polypeptides, but their specific functions are uncertain. Here, we individually deleted the eight genes encoding the shell proteins of the Pdu MCP. The effects of each mutation on 1,2-PD degradation and MCP structure were determined by electron microscopy and growth studies. Deletion of the pduBB', pduJ, or pduN gene severely impaired MCP formation, and the observed defects were consistent with roles as facet, edge, or vertex protein, respectively. Metabolite measurements showed that pduA, pduBB', pduJ, or pduN deletion mutants accumulated propionaldehyde to toxic levels during 1,2-PD catabolism, indicating that the integrity of the shell was disrupted. Deletion of the pduK, pduT, or pduU gene did not substantially affect MCP structure or propionaldehyde accumulation, suggesting they are nonessential to MCP formation. However, the pduU or pduT deletion mutants grew more slowly than the wild type on 1,2-PD at saturating B(12), indicating that they are needed for maximal activity of the 1,2-PD degradative enzymes encased within the MCP shell. Considering recent crystallography studies, this suggests that PduT and PduU may mediate the transport of enzyme substrates/cofactors across the MCP shell. Interestingly, a pduK deletion caused MCP aggregation, suggesting a role in the spatial organization of MCP within the cytoplasm or perhaps in segregation at cell division.

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A complex of 22 enzymes is linked to degradation of 1,2-propanediol to non-equimolar levels of 1-propanol or propionic acid, with propionaldehyde as an intermediate.
“A complex of 22 enzymes has been shown to be linked to the degradation of 1,2-propanediol to non-equimolar levels of 1-propanol (reduced) or propionic acid (oxidized), with propionaldehyde as an intermediate in the reaction [70,71].”
From Dynamic succession of microbiota during ensiling of whole plant corn following inoculation with Lactobacillus buchneri and Lactobacillus hilgardii alone or in combination. (2019) · cites this paper as [71]

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Authors: Cheng, S., Sinha, S., Fan, C., Liu, Y., & Bobik, T. A.
Affiliations: Iowa State University (US)
University of California, Berkeley (US)
Corresponding author: Bobik, Thomas A.
ORCID: Cheng, Shouqiang
Sinha, Sharmistha
Fan, Chenguang
Liu, Yu
Bobik, Thomas A.
Venue: Journal of Bacteriology
Publisher: American Society for Microbiology
Published: 2011-03-15
Volume: 193
Issue: 6
Pages: 1385-1392
ISSN: 0021-9193 (ISSN-L)
1098-5530
DOI: 10.1128/jb.01473-10
PMC: PMC3067621
OpenAlex: W2126957790
Cited by: 104
References: 61
Citations by year: 2026: 8 · 2025: 6 · 2024: 7 · 2023: 6 · 2022: 11 · 2021: 7 · 2020: 12 · 2019: 5 · 2018: 4 · 2017: 8 · 2016: 3 · 2015: 6 · 2014: 10 · 2013: 5 · 2012: 6
FWCI: 4.19
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Journal of Bacteriology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Science Foundation
Iowa State University
National Institutes of Health
National Institute of Allergy and Infectious Diseases (R01AI081146, AI081146)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial Metabolic Engineering and Bioproduction
Keywords: microcompartments, protein shell, coenzyme B12, Salmonella
MeSH terms: Aldehydes, Bacterial Proteins, Cobamides, Microscopy, Electron, Salmonella typhimurium, Organelles, Gene Deletion, Propylene Glycol

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Genetic Analysis of the Protein Shell of the Microcompartments Involved in Coenzyme B12-Dependent 1,2-Propanediol Degradation by Salmonella

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