Article
Biology
Markus Sutter, Cheryl A. Kerfeld
Summary: Bacterial microcompartments (BMCs) are protein-based organelles with unique shell proteins and selective permeability. We have developed a webserver tool using HMM profiles to analyze and categorize BMCs, providing users with information and a reference database.
Review
Microbiology
Jessica M. Ochoa, Todd O. Yeates
Summary: Bacterial microcompartments are organelle-like structures composed entirely of proteins that enhance metabolic functions. Recent studies have highlighted nuanced variations in microcompartment shell proteins, showing how variation and specialization enable complex molecular machine construction. Engineering synthetic miniaturized microcompartment shells provides additional frameworks for dissecting principles of microcompartment structure and assembly.
CURRENT OPINION IN MICROBIOLOGY
(2021)
Article
Multidisciplinary Sciences
Daniel S. Trettel, Chris Neale, Mingfei Zhao, S. Gnanakaran, C. Raul Gonzalez-Esquer
Summary: Bacterial microcompartments (BMCs) are protein organelles with an inner enzymatic core encased in a selectively permeable shell. It has been found that the properties of the shell affect ion permeability, which in turn influences the permeation rate of substrates.
SCIENTIFIC REPORTS
(2023)
Review
Environmental Sciences
Daniel A. Raba, Cheryl A. Kerfeld
Summary: The application of nanotechnology to plants, known as phytonanotechnology, has the potential to revolutionize plant research and agricultural production, improving crop yield and disease resistance.
ENVIRONMENTAL MICROBIOLOGY REPORTS
(2022)
Review
Microbiology
Matthew R. Melnicki, Markus Sutter, Cheryl A. Kerfeld
Summary: Bacterial microcompartments (BMCs) are self-assembling prokaryotic organelles that encapsulate enzymes within a polyhedral protein shell. The shells are composed of distinct domains forming pentagonal and hexagonal building blocks. Recent phylogenomic surveys have revealed specific structural features of BMCs' building blocks, suggesting distinct functional roles across diverse BMC families.
CURRENT OPINION IN MICROBIOLOGY
(2021)
Article
Biochemistry & Molecular Biology
Daniel S. Trettel, William Resager, Beatrix M. Ueberheide, Conor C. Jenkins, Wade C. Winkler
Summary: Bacterial microcompartments (BMCs) are structures found in bacteria that are used for various metabolic purposes. By using chemical probes, the structure of a native BMC was observed, revealing that the shell layer is more dynamic than previously thought. Analysis of cross-linking chemical probes showed a complex multivalent network among cargo proteins, supporting the idea that biomolecular condensation drives interactions between cargo and shell proteins before encapsulation.
Review
Biochemistry & Molecular Biology
Andrew M. Stewart, Katie L. Stewart, Todd O. Yeates, Thomas A. Bobik
Summary: Bacterial microcompartments (MCPs) are large and diverse proteinaceous organelles that compartmentalize metabolic pathways and sequester toxic or volatile intermediates. Recent studies have expanded our understanding of MCP diversity, structure, function, and potential applications, revealing new types of MCPs and their associations with human disease. Structural studies have provided new insights into MCP assembly and mechanisms, while biotechnology applications are utilizing MCP principles for nanobioreactors, nanocontainers, and molecular scaffolds.
TRENDS IN BIOCHEMICAL SCIENCES
(2021)
Review
Microbiology
Markus Sutter, Cheryl A. Kerfeld, Kathleen M. Scott
Summary: Carboxysomes are proteinaceous microcompartments responsible for a significant amount of CO2 fixation on Earth. They facilitate CO2 fixation by concentrating it in cells and converting HCO3- to CO2. The structural components and genetic context of atypical carboxysomes are described in this review.
FRONTIERS IN MICROBIOLOGY
(2022)
Article
Multidisciplinary Sciences
Markus Sutter, Matthew R. Melnicki, Frederik Schulz, Tanja Woyke, Cheryl A. Kerfeld
Summary: Bacterial microcompartments (BMCs) are organelles made up of a selectively permeable shell where specific metabolic reactions occur separate from the cytoplasm. A recent study has shown a twenty-fold increase in the number of identified BMC loci since 2014, along with a doubling of distinct BMC types. These new BMC types broaden the range of compartmentalized catalysis and hint at more BMC biochemistry yet to be discovered.
NATURE COMMUNICATIONS
(2021)
Review
Microbiology
Thomas A. Bobik, Andrew M. Stewart
Summary: Bacterial microcompartments are organelles that are widespread and play important roles in the environment, with a selectively permeable protein shell mediating the movement of substrates, products, and cofactors. Current knowledge of selective transport across these protein shells, including mechanisms, regulation, and unanswered questions, is discussed here.
CURRENT OPINION IN MICROBIOLOGY
(2021)
Article
Multidisciplinary Sciences
Jessica M. Ochoa, Kaylie Bair, Thomas Holton, Thomas A. Bobik, Todd O. Yeates
Summary: Bacterial microcompartments are organelle-like structures made of proteins, carrying out specialized metabolic functions in various bacteria. The MCPdb database categorizes and organizes known microcompartment protein structures and their larger assemblies, serving as a growing resource for scientists interested in understanding these protein-based metabolic organelles in bacteria.
Article
Biochemical Research Methods
Taiyu Chen, Yi Fang, Qiuyao Jiang, Gregory F. Dykes, Yongjun Lin, G. Dean Price, Benedict M. Long, Lu-Ning Liu
Summary: The carboxysome is an important prokaryotic organelle involved in carbon fixation. This study successfully engineered alpha-carboxysomes and found that incorporating certain components can enhance their CO2 fixation activities. Additionally, the structure of carboxysomes can be modified through different expression systems.
ACS SYNTHETIC BIOLOGY
(2022)
Article
Biochemistry & Molecular Biology
Sasha L. Evans, Monsour M. J. Al-Hazeem, Daniel Mann, Nicolas Smetacek, Andrew J. Beavil, Yaqi Sun, Taiyu Chen, Gregory F. Dykes, Lu-Ning Liu, Julien R. C. Bergeron
Summary: This study characterizes a native α-carboxysome from a marine cyanobacterium using single-particle cryoelectron microscopy. The structure of its RuBisCO enzyme was determined, and low-resolution maps of its icosahedral shell and concentric interior organization were obtained. By integrating modeling approaches, a complete atomic model of an intact carboxysome was proposed, providing insight into its organization and assembly, and highlighting its potential in synthetic biology for biotechnological applications.
Review
Biochemistry & Molecular Biology
Lu-Ning Liu
Summary: Carboxysomes are bacterial microcompartments that encapsulate the primary CO2-fixing enzyme Rubisco within a virus-like protein shell. They play a central role in CO2 fixation in bacteria by providing elevated levels of CO2 to maximize carboxylation. Recent research has provided new insights into the assembly and functional maintenance of carboxysomes in bacteria and has explored their potential applications in synthetic biology.
TRENDS IN MICROBIOLOGY
(2022)
Article
Chemistry, Multidisciplinary
Yaohua Li, Nolan W. Kennedy, Siyu Li, Carolyn E. Mills, Danielle Tullman-Ercek, Monica Olvera de la Cruz
Summary: Bacterial microcompartments compartmentalize enzymes for chemical and energy production, aiding bacterial survival in hostile environments. Mutations can alter protein preferred angles and interaction strengths, modifying assembled morphologies. These findings offer insight into controlled protein assembly and principles for designing microcompartments for various applications.
ACS CENTRAL SCIENCE
(2021)