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Article ; Online: Targeting APEX2 to the mRNA encoding fatty acid synthase β in yeast identifies interacting proteins that control its abundance in the cell cycle.

Blank, Heidi M / Griffith, Wendell P / Polymenis, Michael

2023 Volume 34, Issue 13, Page(s) br20

Abstract: Profiling the repertoire of proteins associated with a given mRNA during the cell cycle is unstudied. Furthermore, it is easier to ask and answer what mRNAs a specific protein might bind to than the other way around. Here, we implemented an RNA-centric ... ...

Abstract	Profiling the repertoire of proteins associated with a given mRNA during the cell cycle is unstudied. Furthermore, it is easier to ask and answer what mRNAs a specific protein might bind to than the other way around. Here, we implemented an RNA-centric proximity labeling technology at different points in the cell cycle in highly synchronous yeast cultures. To understand how the abundance of
MeSH term(s)	Saccharomyces cerevisiae/metabolism ; RNA, Messenger/genetics ; Fatty Acid Synthases/genetics ; Fatty Acid Synthases/metabolism ; Cell Cycle ; Cell Division
Chemical Substances	RNA, Messenger ; Fatty Acid Synthases (EC 2.3.1.85)
Language	English
Publishing date	2023-10-04
Publishing country	United States
Document type	Journal Article
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E23-05-0166
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Article ; Online: Dietary Supplementation with 23-Hydroxy Ursolic Acid Reduces the Severity and Incidence of Acute Experimental Autoimmune Encephalomyelitis (EAE) in a Murine Model of Multiple Sclerosis.

Asmis, Reto / Medrano, Megan T / Chase Huizar, Carol / Griffith, Wendell P / Forsthuber, Thomas G

Nutrients

2024 Volume 16, Issue 3

Abstract: 23-Hydroxy ursolic acid (23-OH UA) is a potent atheroprotective and anti-obesogenic phytochemical, with anti-inflammatory and inflammation-resolving properties. In this study, we examined whether dietary 23-OH UA protects mice against the acute onset and ...

Abstract	23-Hydroxy ursolic acid (23-OH UA) is a potent atheroprotective and anti-obesogenic phytochemical, with anti-inflammatory and inflammation-resolving properties. In this study, we examined whether dietary 23-OH UA protects mice against the acute onset and progression of experimental autoimmune encephalomyelitis (EAE), a mouse model of multiple sclerosis (MS). Female C57BL/6 mice were fed either a defined low-calorie maintenance diet (MD) or an MD supplemented with 0.2% wgt/wgt 23-OH UA for 5 weeks prior to actively inducing EAE and during the 30 days post-immunization. We observed no difference in the onset of EAE between the groups of mice, but ataxia and EAE disease severity were suppressed by 52% and 48%, respectively, and disease incidence was reduced by over 49% in mice that received 23-OH UA in their diet. Furthermore, disease-associated weight loss was strikingly ameliorated in 23-OH UA-fed mice. ELISPOT analysis showed no significant differences in frequencies of T cells producing IL-17 or IFN-γ between 23-OH UA-fed mice and control mice, suggesting that 23-OH UA does not appear to regulate peripheral T cell responses. In summary, our findings in EAE mice strongly suggest that dietary 23-OH UA may represent an effective oral adjunct therapy for the prevention and treatment of relapsing-remitting MS.
MeSH term(s)	Female ; Mice ; Animals ; Encephalomyelitis, Autoimmune, Experimental/drug therapy ; Multiple Sclerosis/drug therapy ; Ursolic Acid ; Disease Models, Animal ; Incidence ; Mice, Inbred C57BL ; Dietary Supplements
Chemical Substances	Ursolic Acid (P3M2575F3F)
Language	English
Publishing date	2024-01-25
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2518386-2
ISSN	2072-6643 ; 2072-6643
ISSN (online)	2072-6643
ISSN	2072-6643
DOI	10.3390/nu16030348
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Article ; Online: Formation of Monofluorinated Radical Cofactor in Galactose Oxidase through Copper-Mediated C-F Bond Scission.

Li, Jiasong / Davis, Ian / Griffith, Wendell P / Liu, Aimin

Journal of the American Chemical Society

2020 Volume 142, Issue 44, Page(s) 18753–18757

Abstract: Galactose oxidase (GAO) contains a Cu(II)-ligand radical cofactor. The cofactor, which is autocatalytically generated through the oxidation of the copper, consists of a cysteine-tyrosine radical (Cys- ... ...

Abstract	Galactose oxidase (GAO) contains a Cu(II)-ligand radical cofactor. The cofactor, which is autocatalytically generated through the oxidation of the copper, consists of a cysteine-tyrosine radical (Cys-Tyr
MeSH term(s)	Carbon/chemistry ; Catalysis ; Copper/chemistry ; Crystallography, X-Ray ; Directed Molecular Evolution ; Electron Spin Resonance Spectroscopy ; Fluorine/chemistry ; Free Radicals/chemistry ; Galactose Oxidase/chemistry ; Galactose Oxidase/genetics ; Galactose Oxidase/metabolism ; Kinetics ; Ligands ; Mutagenesis, Site-Directed ; Oxidation-Reduction ; Protein Structure, Tertiary ; Tyrosine/analogs & derivatives ; Tyrosine/chemistry ; Tyrosine/metabolism
Chemical Substances	Free Radicals ; Ligands ; tyrosine radical ; Fluorine (284SYP0193) ; 3,5-difluorotyrosine (369-96-0) ; Tyrosine (42HK56048U) ; Carbon (7440-44-0) ; Copper (789U1901C5) ; Galactose Oxidase (EC 1.1.3.9)
Language	English
Publishing date	2020-10-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.0c08992
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Article: Formation of Monofluorinated Radical Cofactor in Galactose Oxidase through Copper-Mediated C–F Bond Scission

Li, Jiasong / Davis, Ian / Griffith, Wendell P / Liu, Aimin

Journal of the American Chemical Society. 2020 Oct. 22, v. 142, no. 44

2020

Abstract	Galactose oxidase (GAO) contains a Cu(II)-ligand radical cofactor. The cofactor, which is autocatalytically generated through the oxidation of the copper, consists of a cysteine-tyrosine radical (Cys-Tyr•) as a copper ligand. The formation of the cross-linked thioether bond is accompanied by a C–H bond scission on Tyr272 with few details known thus far. Here, we report the genetic incorporation of 3,5-dichlorotyrosine (Cl₂-Tyr) and 3,5-difluorotyrosine (F₂-Tyr) to replace Tyr272 in the GAOⱽ previously optimized for expression through directed evolution. The proteins with an unnatural tyrosine residue are catalytically competent. We determined the high-resolution crystal structures of the GAOⱽ, Cl₂-Tyr272, and F₂-Tyr272 incorporated variants at 1.48, 1.23, and 1.80 Å resolution, respectively. The structural data showed only one halogen remained in the cofactor, indicating that an oxidative carbon-chlorine/fluorine bond scission has occurred during the autocatalytic process of cofactor biogenesis. Using hydroxyurea as a radical scavenger, the spin-coupled hidden Cu(II) was observed by EPR spectroscopy. Thus, the structurally defined catalytic center with genetic unnatural tyrosine substitution is in the radical containing form as in the wild-type, i.e., Cu(II)-(Cl-Tyr•-Cys) or Cu(II)-(F-Tyr•-Cys). These findings illustrate a previously unobserved C–F/C–Cl bond cleavage in biology mediated by a mononuclear copper center.
Keywords	biogenesis ; cleavage (chemistry) ; copper ; crosslinking ; directed evolution ; electron paramagnetic resonance spectroscopy ; galactose oxidase ; hydroxyurea ; ligands ; oxidation ; tyrosine
Language	English
Dates of publication	2020-1022
Size	p. 18753-18757.
Publishing place	American Chemical Society
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.0c08992
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Article ; Online: Characterization of the nonheme iron center of cysteamine dioxygenase and its interaction with substrates.

Wang, Yifan / Davis, Ian / Chan, Yan / Naik, Sunil G / Griffith, Wendell P / Liu, Aimin

The Journal of biological chemistry

2020 Volume 295, Issue 33, Page(s) 11789–11802

Abstract: Cysteamine dioxygenase (ADO) has been reported to exhibit two distinct biological functions with a nonheme iron center. It catalyzes oxidation of both cysteamine in sulfur metabolism and N-terminal cysteine-containing proteins or peptides, such as ... ...

Abstract	Cysteamine dioxygenase (ADO) has been reported to exhibit two distinct biological functions with a nonheme iron center. It catalyzes oxidation of both cysteamine in sulfur metabolism and N-terminal cysteine-containing proteins or peptides, such as regulator of G protein signaling 5 (RGS5). It thereby preserves oxygen homeostasis in a variety of physiological processes. However, little is known about its catalytic center and how it interacts with these two types of primary substrates in addition to O
MeSH term(s)	Animals ; Catalytic Domain ; Cysteamine/metabolism ; Dioxygenases/chemistry ; Dioxygenases/metabolism ; Humans ; Mice ; Models, Molecular ; Oxygen/metabolism ; Peptides/metabolism ; Protein Binding ; RGS Proteins/metabolism ; Substrate Specificity
Chemical Substances	Peptides ; RGS Proteins ; RGS5 protein, human ; Cysteamine (5UX2SD1KE2) ; Dioxygenases (EC 1.13.11.-) ; cysteamine dioxygenase (EC 1.13.11.19) ; Oxygen (S88TT14065)
Language	English
Publishing date	2020-06-28
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA120.013915
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Article ; Online: Hormone glucagon: electrooxidation and determination at carbon nanotubes.

Karra, Sushma / Griffith, Wendell P / Kennedy, Robert T / Gorski, Waldemar

The Analyst

2016 Volume 141, Issue 8, Page(s) 2405–2411

Abstract: The oxidation of glucagon, which is one of the key hormones in glucose homeostasis, was studied at electrodes modified with carbon nanotubes (CNT) that were dispersed in a polysaccharide adhesive chitosan (CHIT). Such electrodes displayed improved ... ...

Abstract	The oxidation of glucagon, which is one of the key hormones in glucose homeostasis, was studied at electrodes modified with carbon nanotubes (CNT) that were dispersed in a polysaccharide adhesive chitosan (CHIT). Such electrodes displayed improved resistance to fouling, which allowed for the investigation of both the electrolysis/mass spectrometry and electroanalysis of glucagon. The off-line electrospray ionization and tandem mass spectrometric analyses showed that the -4 Da mass change to glucagon upon electrolysis at CNT was due to the electrooxidation of its tryptophan (W25) and dityrosine (Y10, Y13) residues. The methionine residue of glucagon did not contribute to its oxidation. The amperometric determination of glucagon yielded the limit of detection equal to ∼20 nM (E = 0.800 V, pH 7.40, S/N = 3), sensitivity of 0.46 A M(-1) cm(-2), linear dynamic range up to 2.0 μM (R(2) = 0.998), response time <5 s, and good signal stability. Free tryptophan and tyrosine yielded comparable analytical figures of merit. The direct amperometric determination of unlabeled glucagon at CHIT-CNT electrodes is the first example of a rapid alternative to the complex analytical assays of this peptide.
MeSH term(s)	Amino Acid Sequence ; Amino Acids/chemistry ; Chitosan/chemistry ; Electrochemistry/instrumentation ; Electrochemistry/methods ; Electrodes ; Glucagon/chemistry ; Mass Spectrometry ; Nanotubes, Carbon/chemistry ; Oxidation-Reduction
Chemical Substances	Amino Acids ; Nanotubes, Carbon ; Glucagon (9007-92-5) ; Chitosan (9012-76-4)
Language	English
Publishing date	2016-04-21
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	210747-8
ISSN	1364-5528 ; 0003-2654
ISSN (online)	1364-5528
ISSN	0003-2654
DOI	10.1039/c5an02636a
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Article: Biocatalytic Carbon-Hydrogen and Carbon-Fluorine Bond Cleavage through Hydroxylation Promoted by a Histidyl-Ligated Heme Enzyme.

Wang, Yifan / Davis, Ian / Shin, Inchul / Wherritt, Daniel J / Griffith, Wendell P / Dornevil, Kednerlin / Colabroy, Keri L / Liu, Aimin

ACS catalysis

2019 Volume 9, Issue 6, Page(s) 4764–4776

Abstract: LmbB2 is a peroxygenase-like enzyme that hydroxylates L-tyrosine to L-3,4-dihydroxyphenylalanine (DOPA) in the presence of hydrogen peroxide. However, its heme cofactor is ligated by a proximal histidine, not cysteine. We show that LmbB2 can oxidize L- ... ...

Abstract	LmbB2 is a peroxygenase-like enzyme that hydroxylates L-tyrosine to L-3,4-dihydroxyphenylalanine (DOPA) in the presence of hydrogen peroxide. However, its heme cofactor is ligated by a proximal histidine, not cysteine. We show that LmbB2 can oxidize L-tyrosine analogs with ring-deactivated substituents such as 3-nitro-, fluoro-, chloro-, iodo-L-tyrosine. We also found that the 4-hydroxyl group of the substrate is essential for reacting with the heme-based oxidant and activating the aromatic C-H bond. The most interesting observation of this study was obtained with 3-fluoro-L-tyrosine as a substrate and mechanistic probe. The LmbB2-mediated catalytic reaction yielded two hydroxylated products with comparable populations,
Language	English
Publishing date	2019-04-11
Publishing country	United States
Document type	Journal Article
ISSN	2155-5435
ISSN	2155-5435
DOI	10.1021/acscatal.9b00231
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Article ; Online: Chemical synthesis of 7α-hydroxypregnenolone, a neuroactive steroid that stimulates locomotor activity.

Yoshimoto, Francis K / Arman, Hadi D / Griffith, Wendell P / Yan, Fangzhi / Wherritt, Daniel J

Steroids

2017 Volume 128, Page(s) 50–57

Abstract: 7α-Hydroxypregnenolone is an endogenous neuroactive steroid that stimulates locomotor activity. A synthesis of 7α-hydroxypregnenolone from pregnenolone, which takes advantage of an orthogonal protecting group strategy, is described. In detail, the C7- ... ...

Abstract	7α-Hydroxypregnenolone is an endogenous neuroactive steroid that stimulates locomotor activity. A synthesis of 7α-hydroxypregnenolone from pregnenolone, which takes advantage of an orthogonal protecting group strategy, is described. In detail, the C7-position was oxidized with CrO
MeSH term(s)	17-alpha-Hydroxypregnenolone/analogs & derivatives ; 17-alpha-Hydroxypregnenolone/chemical synthesis ; 17-alpha-Hydroxypregnenolone/therapeutic use ; Benzoates/chemistry ; Brain/drug effects ; Brain/physiology ; Humans ; Locomotion/drug effects ; Melatonin/metabolism ; Steroids/chemical synthesis ; Steroids/therapeutic use
Chemical Substances	7-hydroxypregnenolone ; Benzoates ; Steroids ; 17-alpha-Hydroxypregnenolone (387-79-1) ; peroxybenzoic acid (C0EZ97V99I) ; Melatonin (JL5DK93RCL)
Language	English
Publishing date	2017-10-20
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	80312-1
ISSN	1878-5867 ; 0039-128X
ISSN (online)	1878-5867
ISSN	0039-128X
DOI	10.1016/j.steroids.2017.10.004
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Article: Protein conformational heterogeneity as a binding catalyst: ESI-MS study of hemoglobin H formation.

Griffith, Wendell P / Kaltashov, Igor A

Biochemistry

2007 Volume 46, Issue 7, Page(s) 2020–2026

Abstract: Our previous studies of hemoglobin tetramer assembly in vitro suggested that the initial step in the oligomerization process, which ultimately dictates the high fidelity of the heterotetramer (alpha*beta*)2 assembly, is the binding of a flexible heme- ... ...

Abstract	Our previous studies of hemoglobin tetramer assembly in vitro suggested that the initial step in the oligomerization process, which ultimately dictates the high fidelity of the heterotetramer (alphabeta)2 assembly, is the binding of a flexible heme-free beta-globin chain to a highly ordered heme-bound alpha-globin. In this work, we extend these studies to investigate formation of the homotetrameric hemoglobin H, whose formation in vivo is a well-documented clinical consequence of significant overexpression of beta-globin in alpha-thalassemic disorders. Upon reconstitution of the isolated beta-globin with excess heme, the predominant species in the ESI mass spectrum corresponds to the homotetramer beta4, alongside homodimeric species and monomeric beta-globin chains in both apo and holo forms. The assembly process of the hemoglobin H homotetramer apparently follows a scenario similar to that of a normal heterodimeric hemoglobin (alphabeta)2 species, with the asymmetric binding event between compact and flexible polypeptide chains being the initial step. The extreme importance of large-scale chain dynamics and conformational heterogeneity for the protein assembly process is highlighted by the inability of highly structured alpha-globins to undergo ordered oligomerization to form dimers and tetramers as opposed to indiscriminate aggregation.
MeSH term(s)	Animals ; Apoproteins/chemistry ; Cattle ; Globins/chemistry ; Hemoglobin H/chemistry ; Protein Binding ; Protein Conformation ; Solutions ; Spectrometry, Mass, Electrospray Ionization
Chemical Substances	Apoproteins ; Solutions ; Globins (9004-22-2) ; Hemoglobin H (9034-79-1)
Language	English
Publishing date	2007-02-20
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/bi062032q
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Article ; Online: Cofactor Biogenesis in Cysteamine Dioxygenase: C-F Bond Cleavage with Genetically Incorporated Unnatural Tyrosine.

Wang, Yifan / Griffith, Wendell P / Li, Jiasong / Koto, Teruaki / Wherritt, Daniel J / Fritz, Elizabeth / Liu, Aimin

Angewandte Chemie (International ed. in English)

2018 Volume 57, Issue 27, Page(s) 8149–8153

Abstract: Cysteamine dioxygenase (ADO) is a thiol dioxygenase whose study has been stagnated by the ambiguity as to whether or not it possesses an anticipated protein-derived cofactor. Reported herein is the discovery and elucidation of a Cys-Tyr cofactor in human ...

Abstract	Cysteamine dioxygenase (ADO) is a thiol dioxygenase whose study has been stagnated by the ambiguity as to whether or not it possesses an anticipated protein-derived cofactor. Reported herein is the discovery and elucidation of a Cys-Tyr cofactor in human ADO, crosslinked between Cys220 and Tyr222 through a thioether (C-S) bond. By genetically incorporating an unnatural amino acid, 3,5-difluoro-tyrosine (F
MeSH term(s)	Amino Acid Motifs ; Carbon/chemistry ; Catalytic Domain ; Cysteine/chemistry ; Cysteine/metabolism ; Cysteine Dioxygenase/chemistry ; Cysteine Dioxygenase/metabolism ; Dioxygenases/chemistry ; Dioxygenases/metabolism ; Fluorine/chemistry ; Humans ; Nuclear Magnetic Resonance, Biomolecular ; Oxidation-Reduction ; Protein Structure, Tertiary ; Tyrosine/chemistry ; Tyrosine/metabolism
Chemical Substances	Fluorine (284SYP0193) ; Tyrosine (42HK56048U) ; Carbon (7440-44-0) ; Dioxygenases (EC 1.13.11.-) ; cysteamine dioxygenase (EC 1.13.11.19) ; Cysteine Dioxygenase (EC 1.13.11.20) ; Cysteine (K848JZ4886)
Language	English
Publishing date	2018-06-05
Publishing country	Germany
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2011836-3
ISSN	1521-3773 ; 1433-7851
ISSN (online)	1521-3773
ISSN	1433-7851
DOI	10.1002/anie.201803907
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