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

Journal Article · · mBio
ORCiD logo [1]; ORCiD logo [2]; ORCiD logo [3];
  1. MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, Michigan, USA
  2. MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, Michigan, USA, Environmental Genomics and Systems Biology and Molecular Biophysics and Integrated Bioimaging Divisions, Lawrence Berkeley National Laboratory, Berkeley, California, USA
  3. MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, Michigan, USA, Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan, USA, Environmental Genomics and Systems Biology and Molecular Biophysics and Integrated Bioimaging Divisions, Lawrence Berkeley National Laboratory, Berkeley, California, USA

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 B12-dependent radical mechanisms. In contrast, a less-well-known BMC type utilizes the B12-independent radical chemistry of glycyl radical enzymes (GREs). Unlike B12-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.

Research Organization:
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States); Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Laboratory
Sponsoring Organization:
National Institutes of Health (NIH); USDOE Office of Science (SC), Basic Energy Sciences (BES)
Grant/Contract Number:
FG02-91ER20021; AC02-05CH11231; R01 AI114975-05
OSTI ID:
1489729
Alternate ID(s):
OSTI ID: 1591803; OSTI ID: 1607876
Journal Information:
mBio, Journal Name: mBio Vol. 10 Journal Issue: 1; ISSN 2161-2129
Publisher:
American Society for MicrobiologyCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 21 works
Citation information provided by
Web of Science

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