Ubiquitin-Like Protein $\mathrm{SAMP1}$ and $\mathrm{JAMM/MPN+}$ Metalloprotease $\mathrm{HvJAMM1}$ Constitute a System for Reversible Regulation of Metabolic Enzyme Activity in Archaea

Cao, Shiyun; Hepowit, Nathaniel; Maupin-Furlow, Julie A.

doi:10.1371/journal.pone.0128399

Ubiquitin-Like Protein $$\mathrm{SAMP1}$$ and $$\mathrm{JAMM/MPN+}$$ Metalloprotease $$\mathrm{HvJAMM1}$$ Constitute a System for Reversible Regulation of Metabolic Enzyme Activity in Archaea

Journal Article · Tue May 26 04:00:00 EDT 2015 · PLoS ONE

DOI:https://doi.org/10.1371/journal.pone.0128399· OSTI ID:1904666

Cao, Shiyun ^[1]; Hepowit, Nathaniel ^[2]; Maupin-Furlow, Julie A. ^[2]

University of Florida, Gainesville, FL (United States); Univ. of Florida, Gainesville, FL (United States)
University of Florida, Gainesville, FL (United States)

Ubiquitin/ubiquitin-like (Ub/Ubl) proteins are involved in diverse cellular processes by their covalent linkage to P1) and a JAMM/MPN+ metalloprotease (HvJAMM1). Molybdopterin (MPT) synthasprotein substrates. Here, we provide evidence for a post-translational modification system that regulates enzyme activity which is composed of an archaeal Ubl protein (SAMe activity was found to be inhibited by covalent linkage of SAMP1 to the large subunit (MoaE) of MPT synthase. HvJAMM1 was shown to cleave the covalently linked inactive form of SAMP1-MoaE to the free functional individual SAMP1 and MoaE subunits of MPT synthase, suggesting reactivation of MPT synthase by this metalloprotease. Overall, this study provides new insight into the broad idea that Ub/Ubl modification is a post-translational process that can directly and reversibly regulate the activity of metabolic enzymes. In particular, we show that Ub/Ubl linkages on the active site residues of an enzyme (MPT synthase) can inhibit its catalytic activity and that the enzyme can be reactivated through cleavage by a JAMM/MPN+ metalloprotease.

View Accepted Manuscript (DOE)

Research Organization:: University of Florida, Gainesville, FL (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences & Biosciences Division (CSGB); National Institutes of Health (NIH)

Grant/Contract Number:: FG02-05ER15650

OSTI ID:: 1904666

Journal Information:: PLoS ONE, Journal Name: PLoS ONE Journal Issue: 5 Vol. 10; ISSN 1932-6203

Publisher:: Public Library of ScienceCopyright Statement

Country of Publication:: United States

Language:: English

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Ubiquitin-Like Protein $$\mathrm{SAMP1}$$ and $$\mathrm{JAMM/MPN+}$$ Metalloprotease $$\mathrm{HvJAMM1}$$ Constitute a System for Reversible Regulation of Metabolic Enzyme Activity in Archaea

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