Genetic analysis around aminoalcohol dehydrogenase gene of Rhodococcus erythropolis MAK154: a putative GntR transcription factor in transcriptional regulation

Urano, Nobuyuki; Kataoka, Michihiko; Ishige, Takeru; Kita, Shinji; Sakamoto, Keiji; Shimizu, Sakayu

doi:10.1007/s00253-010-2924-5

Cited by 20 publications

(20 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…and Mycobacterium spp. microcompartment) has been linked to aminoalcohol or aminoketone metabolism 91 . However, only one of the putatively encapsulated enzymes of RMM has been characterized, the L-1-amino-2-propanol dehydrogenase 92 .…”

Section: The Functional Diversity Of Bmcsmentioning

confidence: 99%

Bacterial microcompartments

et al. 2018

View full text Add to dashboard Cite

Bacterial microcompartments (BMCs) are self-assembling organelles that consist of an enzymatic core that is encapsulated by a selectively permeable protein shell. The potential to form BMCs is widespread, found across the Kingdom Bacteria. BMCs have crucial roles in carbon dioxide fixation in autotrophs and the catabolism of organic substrates in heterotrophs. They contribute to the metabolic versatility of bacteria, providing a competitive advantage in specific environmental niches. Although BMCs were first visualized more than sixty years ago, it is mainly in the last decade that progress has been made in understanding their metabolic diversity and the structural basis of their assembly and function. This progress has not only heightened our understanding of their role in microbial metabolism but it is also beginning to enable their use in a variety of applications in synthetic biology. In this Review, we focus on recent insights into the structure, assembly, diversity and function of BMCs.

show abstract

Section: The Functional Diversity Of Bmcsmentioning

confidence: 99%

Bacterial microcompartments

et al. 2018

View full text Add to dashboard Cite

show abstract

“…Encoded enzymes that have not been catalytically characterized, but from sequence homology, the operon includes a class III aminotransferase, an aldehydealcohol dehydrogenase, and a protein with distant homology to aminoglycoside phosphotransferases. This operon can be induced in Rhodococcus by the addition of 1-amino-2-propanol (24). Together, this suggests that the initial substrate is either 1-amino-2-propanol, and/or a small amino alcohol, or a closely related metabolite.…”

mentioning

confidence: 90%

A Complete Structural Inventory of the Mycobacterial Microcompartment Shell Proteins Constrains Models of Global Architecture and Transport

Mallette

Kimber

2017

Journal of Biological Chemistry

View full text Add to dashboard Cite

Bacterial microcompartments are bacterial analogs of eukaryotic organelles in that they spatially segregate aspects of cellular metabolism, but they do so by building not a lipid membrane but a thin polyhedral protein shell. Although multiple shell protein structures are known for several microcompartment types, additional uncharacterized components complicate systematic investigations of shell architecture. We report here the structures of all four proteins proposed to form the shell of an uncharacterized microcompartment designated the Rhodococcus and Mycobacterium microcompartment (RMM), which, along with crystal interactions and docking studies, suggests possible models for the particle's vertex and edge organization. MSM0272 is a typical hexameric β-sandwich shell protein thought to form the bulk of the facet. MSM0273 is a pentameric β-barrel shell protein that likely plugs the vertex of the particle. MSM0271 is an unusual double-ringed bacterial microcompartment shell protein whose rings are organized in an offset position relative to all known related proteins. MSM0275 is related to MSM0271 but self-organizes as linear strips that may line the facet edge; here, the presence of a novel extendable loop may help ameliorate poor packing geometry of the rigid main particle at the angled edges. In contrast to previously characterized homologs, both of these proteins show closed pores at both ends. This suggests a model where key interactions at the vertex and edges are mediated at the inner layer of the shell by MSM0271 (encircling MSM0273) and MSM0275, and the facet is built from MSM0272 hexamers tiling in the outer layer of the shell.

show abstract

“…BMC-shell encoding genes are present in more than 400 sequenced bacterial genomes; and the encoded proteins are associated with enzymes involved in at least eight different metabolic pathways [7], [8], [9]. A subset of BMCs, called carboxysomes, plays an important role in CO 2 fixation [10], [11].…”

Section: Introductionmentioning

confidence: 99%

Engineered Protein Nano-Compartments for Targeted Enzyme Localization

et al. 2012

View full text Add to dashboard Cite

Compartmentalized co-localization of enzymes and their substrates represents an attractive approach for multi-enzymatic synthesis in engineered cells and biocatalysis. Sequestration of enzymes and substrates would greatly increase reaction efficiency while also protecting engineered host cells from potentially toxic reaction intermediates. Several bacteria form protein-based polyhedral microcompartments which sequester functionally related enzymes and regulate their access to substrates and other small metabolites. Such bacterial microcompartments may be engineered into protein-based nano-bioreactors, provided that they can be assembled in a non-native host cell, and that heterologous enzymes and substrates can be targeted into the engineered compartments. Here, we report that recombinant expression of Salmonella enterica ethanolamine utilization ( eut ) bacterial microcompartment shell proteins in E. coli results in the formation of polyhedral protein shells. Purified recombinant shells are morphologically similar to the native Eut microcompartments purified from S. enterica . Surprisingly, recombinant expression of only one of the shell proteins (EutS) is sufficient and necessary for creating properly delimited compartments. Co-expression with EutS also facilitates the encapsulation of EGFP fused with a putative Eut shell-targeting signal sequence. We also demonstrate the functional localization of a heterologous enzyme (β-galactosidase) targeted to the recombinant shells. Together our results provide proof-of-concept for the engineering of protein nano-compartments for biosynthesis and biocatalysis.

show abstract

Genetic analysis around aminoalcohol dehydrogenase gene of Rhodococcus erythropolis MAK154: a putative GntR transcription factor in transcriptional regulation

Cited by 20 publications

References 27 publications

Bacterial microcompartments

Bacterial microcompartments

A Complete Structural Inventory of the Mycobacterial Microcompartment Shell Proteins Constrains Models of Global Architecture and Transport

Engineered Protein Nano-Compartments for Targeted Enzyme Localization

Contact Info

Product

Resources

About