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Title: Glycyl Radical Enzyme-Associated Microcompartments: Redox-Replete Bacterial Organelles

Abstract

ABSTRACT An increasing number of microbes are being identified that organize catabolic pathways within self-assembling proteinaceous structures known as bacterial microcompartments (BMCs). Most BMCs are characterized by their singular substrate specificity and commonly employ B 12 -dependent radical mechanisms. In contrast, a less-well-known BMC type utilizes the B 12 -independent radical chemistry of glycyl radical enzymes (GREs). Unlike B 12 -dependent enzymes, GREs require an activating enzyme (AE) as well as an external source of electrons to generate an adenosyl radical and form their catalytic glycyl radical. Organisms encoding these glycyl radical enzyme-associated microcompartments (GRMs) confront the challenge of coordinating the activation and maintenance of their GREs with the assembly of a multienzyme core that is encapsulated in a protein shell. The GRMs appear to enlist redox proteins to either generate reductants internally or facilitate the transfer of electrons from the cytosol across the shell. Despite this relative complexity, GRMs are one of the most widespread types of BMC, with distinct subtypes to catabolize different substrates. Moreover, they are encoded by many prominent gut-associated and pathogenic bacteria. In this review, we will focus on the diversity, function, and physiological importance of GRMs, with particular attention given to their associated andmore » enigmatic redox proteins.« less

Authors:
ORCiD logo; ORCiD logo; ORCiD logo;
Publication Date:
Sponsoring Org.:
USDOE
OSTI Identifier:
1489729
Grant/Contract Number:  
FG02-91ER20021
Resource Type:
Journal Article: Published Article
Journal Name:
mBio (Online)
Additional Journal Information:
Journal Name: mBio (Online) Journal Volume: 10 Journal Issue: 1; Journal ID: ISSN 2150-7511
Publisher:
American Society for Microbiology
Country of Publication:
United States
Language:
English

Citation Formats

Ferlez, Bryan, Sutter, Markus, Kerfeld, Cheryl A., and Garsin, ed., Danielle A. Glycyl Radical Enzyme-Associated Microcompartments: Redox-Replete Bacterial Organelles. United States: N. p., 2019. Web. doi:10.1128/mBio.02327-18.
Ferlez, Bryan, Sutter, Markus, Kerfeld, Cheryl A., & Garsin, ed., Danielle A. Glycyl Radical Enzyme-Associated Microcompartments: Redox-Replete Bacterial Organelles. United States. doi:10.1128/mBio.02327-18.
Ferlez, Bryan, Sutter, Markus, Kerfeld, Cheryl A., and Garsin, ed., Danielle A. Tue . "Glycyl Radical Enzyme-Associated Microcompartments: Redox-Replete Bacterial Organelles". United States. doi:10.1128/mBio.02327-18.
@article{osti_1489729,
title = {Glycyl Radical Enzyme-Associated Microcompartments: Redox-Replete Bacterial Organelles},
author = {Ferlez, Bryan and Sutter, Markus and Kerfeld, Cheryl A. and Garsin, ed., Danielle A.},
abstractNote = {ABSTRACT An increasing number of microbes are being identified that organize catabolic pathways within self-assembling proteinaceous structures known as bacterial microcompartments (BMCs). Most BMCs are characterized by their singular substrate specificity and commonly employ B 12 -dependent radical mechanisms. In contrast, a less-well-known BMC type utilizes the B 12 -independent radical chemistry of glycyl radical enzymes (GREs). Unlike B 12 -dependent enzymes, GREs require an activating enzyme (AE) as well as an external source of electrons to generate an adenosyl radical and form their catalytic glycyl radical. Organisms encoding these glycyl radical enzyme-associated microcompartments (GRMs) confront the challenge of coordinating the activation and maintenance of their GREs with the assembly of a multienzyme core that is encapsulated in a protein shell. The GRMs appear to enlist redox proteins to either generate reductants internally or facilitate the transfer of electrons from the cytosol across the shell. Despite this relative complexity, GRMs are one of the most widespread types of BMC, with distinct subtypes to catabolize different substrates. Moreover, they are encoded by many prominent gut-associated and pathogenic bacteria. In this review, we will focus on the diversity, function, and physiological importance of GRMs, with particular attention given to their associated and enigmatic redox proteins.},
doi = {10.1128/mBio.02327-18},
journal = {mBio (Online)},
number = 1,
volume = 10,
place = {United States},
year = {Tue Jan 08 00:00:00 EST 2019},
month = {Tue Jan 08 00:00:00 EST 2019}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record at 10.1128/mBio.02327-18

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Works referenced in this record:

Biochemistry of coenzyme B12-dependent glycerol and diol dehydratases and organization of the encoding genes
journal, December 1998