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Article ; Online: Ceruloplasmin as a source of Cu for a fungal pathogen.

Besold, Angelique N / Shanbhag, Vinit / Petris, Michael J / Culotta, Valeria C

2021 Volume 219, Page(s) 111424

Abstract: Copper is an essential metal for virtually all organisms, yet little is known about the extracellular sources of this micronutrient. In serum, the most abundant extracellular Cu-binding molecule is the multi‑copper oxidase ceruloplasmin (Cp). Cp levels ... ...

Abstract	Copper is an essential metal for virtually all organisms, yet little is known about the extracellular sources of this micronutrient. In serum, the most abundant extracellular Cu-binding molecule is the multi‑copper oxidase ceruloplasmin (Cp). Cp levels increase during infection and inflammation, and pathogens can be exposed to high Cp at sites of infection. It is not known whether Cp might serve as a Cu source for microbial pathogens and we tested this using the opportunistic fungal pathogen Candida albicans. We find that C. albicans can use whole serum as a Cu source and that this Cu is sensed by the transcription factor protein Mac1. Mac1 activates expression of Mn-SOD3 superoxide dismutase and represses Cu/Zn-SOD1 during Cu starvation and both responses are regulated by serum Cu. We also show that purified human Cp can act as a sole source of Cu for the fungus and likewise modulates the Mac1 Cu stress response. To investigate whether Cp is a Cu source in serum, we compared the ability of C. albicans to use serum from wild type versus Cp
MeSH term(s)	Animals ; Candida albicans/metabolism ; Candidiasis/metabolism ; Ceruloplasmin/metabolism ; Copper/blood ; Copper/metabolism ; Female ; Fungal Proteins/metabolism ; Humans ; Male ; Mice ; Nuclear Proteins/metabolism ; Superoxide Dismutase/metabolism ; Superoxide Dismutase-1/metabolism ; Transcription Factors/metabolism
Chemical Substances	Fungal Proteins ; Nuclear Proteins ; Transcription Factors ; Copper (789U1901C5) ; Superoxide Dismutase (EC 1.15.1.1) ; Superoxide Dismutase-1 (EC 1.15.1.1) ; Ceruloplasmin (EC 1.16.3.1)
Language	English
Publishing date	2021-03-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	162843-4
ISSN	1873-3344 ; 0162-0134
ISSN (online)	1873-3344
ISSN	0162-0134
DOI	10.1016/j.jinorgbio.2021.111424
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Article ; Online: Cdc42 regulates reactive oxygen species production in the pathogenic yeast Candida albicans.

Kowalewski, Griffin P / Wildeman, Asia S / Bogliolo, Stéphanie / Besold, Angelique N / Bassilana, Martine / Culotta, Valeria C

The Journal of biological chemistry

2021 Volume 297, Issue 2, Page(s) 100917

Abstract: Across eukaryotes, Rho GTPases such as Rac and Cdc42 play important roles in establishing cell polarity, which is a key feature of cell growth. In mammals and filamentous fungi, Rac targets large protein complexes containing NADPH oxidases (NOX) that ... ...

Abstract	Across eukaryotes, Rho GTPases such as Rac and Cdc42 play important roles in establishing cell polarity, which is a key feature of cell growth. In mammals and filamentous fungi, Rac targets large protein complexes containing NADPH oxidases (NOX) that produce reactive oxygen species (ROS). In comparison, Rho GTPases of unicellular eukaryotes were believed to signal cell polarity without ROS, and it was unclear whether Rho GTPases were required for ROS production in these organisms. We document here the first example of Rho GTPase-mediated post-transcriptional control of ROS in a unicellular microbe. Specifically, Cdc42 is required for ROS production by the NOX Fre8 of the opportunistic fungal pathogen Candida albicans. During morphogenesis to a hyphal form, a filamentous growth state, C. albicans FRE8 mRNA is induced, which leads to a burst in ROS. Fre8-ROS is also induced during morphogenesis when FRE8 is driven by an ectopic promoter; hence, Fre8 ROS production is in addition controlled at the post-transcriptional level. Using fluorescently tagged Fre8, we observe that the majority of the protein is associated with the vacuolar system. Interestingly, much of Fre8 in the vacuolar system appears inactive, and Fre8-induced ROS is only produced at sites near the hyphal tip, where Cdc42 is also localized during morphogenesis. We observe that Cdc42 is necessary to activate Fre8-mediated ROS production during morphogenesis. Cdc42 regulation of Fre8 occurs without the large NOX protein complexes typical of higher eukaryotes and therefore represents a novel form of ROS control by Rho GTPases.
MeSH term(s)	Candida albicans/isolation & purification ; Candida albicans/pathogenicity ; Candidiasis/metabolism ; Candidiasis/microbiology ; Candidiasis/pathology ; Cell Polarity ; Fungal Proteins/metabolism ; Hyphae/metabolism ; Morphogenesis ; Reactive Oxygen Species/metabolism ; cdc42 GTP-Binding Protein/metabolism
Chemical Substances	Fungal Proteins ; Reactive Oxygen Species ; cdc42 GTP-Binding Protein (EC 3.6.5.2)
Language	English
Publishing date	2021-06-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2021.100917
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Article ; Online: The Yin and Yang of copper during infection.

Besold, Angelique N / Culbertson, Edward M / Culotta, Valeria C

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry

2016 Volume 21, Issue 2, Page(s) 137–144

Abstract: Copper is an essential micronutrient for both pathogens and the animal hosts they infect. However, copper can also be toxic in cells due to its redox properties and ability to disrupt active sites of metalloproteins, such as Fe-S enzymes. Through these ... ...

Abstract	Copper is an essential micronutrient for both pathogens and the animal hosts they infect. However, copper can also be toxic in cells due to its redox properties and ability to disrupt active sites of metalloproteins, such as Fe-S enzymes. Through these toxic properties, copper is an effective antimicrobial agent and an emerging concept in innate immunity is that the animal host intentionally exploits copper toxicity in antimicrobial weaponry. In particular, macrophages can attack invading microbes with high copper and this metal is also elevated at sites of lung infection. In addition, copper levels in serum rise during infection with a wide array of pathogens. To defend against this toxic copper, the microbial intruder is equipped with a battery of copper detoxification defenses that promote survival in the host, including copper exporting ATPases and copper binding metallothioneins. However, it is important to remember that copper is also an essential nutrient for microbial pathogens and serves as important cofactor for enzymes such as cytochrome c oxidase for respiration, superoxide dismutase for anti-oxidant defense and multi-copper oxidases that act on metals and organic substrates. We therefore posit that the animal host can also thwart pathogen growth by limiting their copper nutrients, similar to the well-documented nutritional immunity effects for starving microbes of essential zinc, manganese and iron micronutrients. This review provides both sides of the copper story and evaluates how the host can exploit either copper-the-toxin or copper-the-nutrient in antimicrobial tactics at the host-pathogen battleground.
MeSH term(s)	Animals ; Bacterial Infections/metabolism ; Ceruloplasmin/metabolism ; Copper/blood ; Copper/metabolism ; Humans ; Mycoses/metabolism ; Mycoses/microbiology
Chemical Substances	Copper (789U1901C5) ; Ceruloplasmin (EC 1.16.3.1)
Language	English
Publishing date	2016-01-20
Publishing country	Germany
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1464026-0
ISSN	1432-1327 ; 0949-8257
ISSN (online)	1432-1327
ISSN	0949-8257
DOI	10.1007/s00775-016-1335-1
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Article ; Online: Neural Zinc Finger Factor/Myelin Transcription Factor Proteins: Metal Binding, Fold, and Function.

Besold, Angelique N / Michel, Sarah L J

Biochemistry

2015 Volume 54, Issue 29, Page(s) 4443–4452

Abstract: Zinc finger (ZF) proteins make up a large family of metalloproteins that contain discrete domains with amino acid ligands (cysteine and histidine) that serve to coordinate zinc in a tetrahedral geometry. Upon zinc coordination, the domains adopt three- ... ...

Abstract	Zinc finger (ZF) proteins make up a large family of metalloproteins that contain discrete domains with amino acid ligands (cysteine and histidine) that serve to coordinate zinc in a tetrahedral geometry. Upon zinc coordination, the domains adopt three-dimensional structure. The most well-studied ZFs are the "classical" ZFs, which use a Cys2His2 motif to bind zinc and adopt an antiparallel β sheet/α helical fold. In addition to the classical ZF class, at least 13 other ZF classes, collectively termed nonclassical ZFs, have been identified. These other classes are distinguished by the combination and order of the cysteine and histidine ligands within each domain, the spacing between each ligand (i.e., number and type of amino acid), and the structural architecture that the domain adopts in the presence of zinc. One class of nonclassical ZFs, the neural zinc finger/myelin transcription factor (NZF/MyT) class, contains ZF domains with a Cys2His2Cys ligand set, adopts a fold that consists of a series of loops in the presence of zinc, and functions as transcription factors by binding to and regulating genes that are critical for the development of the central nervous system. This Current Topic focuses on our understanding of the NZF/MyT class of nonclassical ZFs and presents current hypotheses regarding this class' unique mechanism of metal-mediated folding and function.
MeSH term(s)	Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Cobalt/chemistry ; Conserved Sequence ; Humans ; Molecular Sequence Data ; Myelin Proteins/chemistry ; Myelin Proteins/physiology ; Nerve Tissue Proteins/chemistry ; Nerve Tissue Proteins/physiology ; Protein Binding ; Transcription Factors/chemistry ; Transcription Factors/physiology ; Zinc/chemistry ; Zinc Fingers
Chemical Substances	Myelin Proteins ; Nerve Tissue Proteins ; Transcription Factors ; Cobalt (3G0H8C9362) ; Zinc (J41CSQ7QDS)
Language	English
Publishing date	2015-07-28
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/bi501371a
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Article: Neural Zinc Finger Factor/Myelin Transcription Factor Proteins: Metal Binding, Fold, and Function

Besold, Angelique N / Michel Sarah L. J

Biochemistry. 2015 July 28, v. 54, no. 29

2015

Abstract	Zinc finger (ZF) proteins make up a large family of metalloproteins that contain discrete domains with amino acid ligands (cysteine and histidine) that serve to coordinate zinc in a tetrahedral geometry. Upon zinc coordination, the domains adopt three-dimensional structure. The most well-studied ZFs are the âclassicalâ ZFs, which use a CysâHisâ motif to bind zinc and adopt an antiparallel Î² sheet/Î± helical fold. In addition to the classical ZF class, at least 13 other ZF classes, collectively termed nonclassical ZFs, have been identified. These other classes are distinguished by the combination and order of the cysteine and histidine ligands within each domain, the spacing between each ligand (i.e., number and type of amino acid), and the structural architecture that the domain adopts in the presence of zinc. One class of nonclassical ZFs, the neural zinc finger/myelin transcription factor (NZF/MyT) class, contains ZF domains with a CysâHisâCys ligand set, adopts a fold that consists of a series of loops in the presence of zinc, and functions as transcription factors by binding to and regulating genes that are critical for the development of the central nervous system. This Current Topic focuses on our understanding of the NZF/MyT class of nonclassical ZFs and presents current hypotheses regarding this classâ unique mechanism of metal-mediated folding and function.
Keywords	cysteine ; genes ; geometry ; histidine ; ligands ; metalloproteins ; myelin sheath ; neurodevelopment ; transcription factors ; zinc ; zinc finger motif
Language	English
Dates of publication	2015-0728
Size	p. 4443-4452.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021%2Fbi501371a
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: A role for hydrogen bonding in DNA recognition by the non-classical CCHHC type zinc finger, NZF-1.

Besold, Angelique N / Amick, Deborah L / Michel, Sarah L J

Molecular bioSystems

2014 Volume 10, Issue 7, Page(s) 1753–1756

Abstract: The non-classical zinc finger protein, Neural Zinc Finger Factor-1, contains six Cys2His2Cys domains. All three cysteines and the second histidine directly bind Zn(II). Using a combination of mutagenesis, metal coordination and DNA binding studies, we ... ...

Abstract	The non-classical zinc finger protein, Neural Zinc Finger Factor-1, contains six Cys2His2Cys domains. All three cysteines and the second histidine directly bind Zn(II). Using a combination of mutagenesis, metal coordination and DNA binding studies, we report that the first histidine is involved in a functionally important hydrogen bonding interaction.
MeSH term(s)	Animals ; Binding Sites ; Cysteine/metabolism ; DNA/metabolism ; Histidine/metabolism ; Humans ; Hydrogen Bonding ; Models, Molecular ; Mutation ; Nerve Tissue Proteins/chemistry ; Nerve Tissue Proteins/metabolism ; Transcription Factors/chemistry ; Transcription Factors/metabolism ; Zinc Fingers
Chemical Substances	MYT1L protein, human ; Nerve Tissue Proteins ; Transcription Factors ; Histidine (4QD397987E) ; DNA (9007-49-2) ; Cysteine (K848JZ4886)
Language	English
Publishing date	2014-05-13
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2188635-0
ISSN	1742-2051 ; 1742-206X
ISSN (online)	1742-2051
ISSN	1742-206X
DOI	10.1039/c4mb00246f
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Article ; Online: Switching metal ion coordination and DNA Recognition in a Tandem CCHHC-type zinc finger peptide.

Besold, Angelique N / Oluyadi, Abdulafeez A / Michel, Sarah L J

Inorganic chemistry

2013 Volume 52, Issue 8, Page(s) 4721–4728

Abstract: Neural Zinc Finger Factor-1 (NZF-1) and Myelin Transcription Factor 1 (MyT1) are two homologous nonclassical zinc finger (ZF) proteins that are involved in the development of the central nervous system (CNS). Both NZF-1 and MyT1 contain multiple ZF ... ...

Abstract	Neural Zinc Finger Factor-1 (NZF-1) and Myelin Transcription Factor 1 (MyT1) are two homologous nonclassical zinc finger (ZF) proteins that are involved in the development of the central nervous system (CNS). Both NZF-1 and MyT1 contain multiple ZF domains, each of which contains an absolutely conserved Cys2His2Cys motif. All three cysteines and the second histidine have been shown to coordinate Zn(II); however, the role of the first histidine remains unresolved. Using a functional form of NZF-1 that contains two ZF domains (NZF-1-F2F3), mutant proteins in which each histidine was sequentially mutated to a phenylalanine were prepared to determine the role(s) of the histidine residues in DNA recognition. When the first histidine is mutated, the protein binds Zn(II) in an analogous manner to the native protein. Surprisingly, this mutant does not bind to target DNA (β-RAR), suggesting that the noncoordinating histidine is critical for sequence selective DNA recognition. The first histidine will coordinate Zn(II) when the second histidine is mutated; however, the overall fold of the protein is perturbed leading to abrogation of DNA binding. NZF-1-F2F3 selectively binds to a specific DNA target sequence (from β-RAR) with high affinity (nM); while its homologue MyT1 (MyT1-F2F3), which is 92% identical to NZF-1-F2F3, binds to this same DNA sequence nonspecifically. A single, nonconserved amino acid residue in NZF-1-F2F3 is shown to be responsible for this high affinity DNA binding to β-RAR. When this residue (arginine) is engineered into the MyT1-F2F3 sequence, the affinity for β-RAR DNA increases.
MeSH term(s)	Amino Acid Sequence ; Animals ; Binding Sites ; Cobalt/metabolism ; DNA/chemistry ; DNA/metabolism ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Histidine/chemistry ; Histidine/genetics ; Histidine/metabolism ; Metals/metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nerve Tissue Proteins/chemistry ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Peptides/chemistry ; Peptides/genetics ; Protein Binding ; Rats ; Sequence Alignment ; Trans-Activators/chemistry ; Trans-Activators/genetics ; Trans-Activators/metabolism ; Transcription Factors/chemistry ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Zinc/metabolism ; Zinc Fingers
Chemical Substances	DNA-Binding Proteins ; Metals ; Myt1 protein, rat ; Myt1l protein, rat ; Nerve Tissue Proteins ; Peptides ; Trans-Activators ; Transcription Factors ; Cobalt (3G0H8C9362) ; Histidine (4QD397987E) ; DNA (9007-49-2) ; Zinc (J41CSQ7QDS)
Language	English
Publishing date	2013-03-22
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	1484438-2
ISSN	1520-510X ; 0020-1669
ISSN (online)	1520-510X
ISSN	0020-1669
DOI	10.1021/ic4003516
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Article ; Online: Cysteine and histidine shuffling: mixing and matching cysteine and histidine residues in zinc finger proteins to afford different folds and function.

Michalek, Jamie L / Besold, Angelique N / Michel, Sarah L J

Dalton transactions (Cambridge, England : 2003)

2011 Volume 40, Issue 47, Page(s) 12619–12632

Abstract: Zinc finger proteins utilize zinc for structural purposes: zinc binds to a combination of cysteine and histidine ligands in a tetrahedral coordination geometry facilitating protein folding and function. While much is known about the classical zinc finger ...

Abstract	Zinc finger proteins utilize zinc for structural purposes: zinc binds to a combination of cysteine and histidine ligands in a tetrahedral coordination geometry facilitating protein folding and function. While much is known about the classical zinc finger proteins, which utilize a Cys(2)His(2) ligand set to coordinate zinc and fold into an anti-parallel beta sheet/alpha helical fold, there are thirteen other families of 'non-classical' zinc finger proteins for which relationships between metal coordination and protein structure/function are less defined. This 'Perspective' article focuses on two classes of these non-classical zinc finger proteins: Cys(3)His type zinc finger proteins and Cys(2)His(2)Cys type zinc finger proteins. These proteins bind zinc in a tetrahedral geometry, like the classical zinc finger proteins, yet they adopt completely different folds and target different oligonucleotides. Our current understanding of the relationships between ligand set, metal ion, fold and function for these non-classical zinc fingers is discussed.
MeSH term(s)	Amino Acid Sequence ; Cysteine/chemistry ; Histidine/chemistry ; Molecular Sequence Data ; Oxidation-Reduction ; Protein Folding ; Protein Structure, Secondary ; Proteins/chemistry ; Sequence Alignment ; Zinc/chemistry ; Zinc Fingers
Chemical Substances	Proteins ; Histidine (4QD397987E) ; Zinc (J41CSQ7QDS) ; Cysteine (K848JZ4886)
Language	English
Publishing date	2011-12-21
Publishing country	England
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1472887-4
ISSN	1477-9234 ; 1364-5447 ; 0300-9246 ; 1477-9226
ISSN (online)	1477-9234 ; 1364-5447
ISSN	0300-9246 ; 1477-9226
DOI	10.1039/c1dt11071c
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Article ; Online: Role of Calprotectin in Withholding Zinc and Copper from Candida albicans.

Besold, Angelique N / Gilston, Benjamin A / Radin, Jana N / Ramsoomair, Christian / Culbertson, Edward M / Li, Cissy X / Cormack, Brendan P / Chazin, Walter J / Kehl-Fie, Thomas E / Culotta, Valeria C

Infection and immunity

2018 Volume 86, Issue 2

Abstract: The opportunistic fungal ... ...

Abstract	The opportunistic fungal pathogen
MeSH term(s)	Animals ; Candida albicans/drug effects ; Candida albicans/growth & development ; Candida albicans/metabolism ; Copper/metabolism ; Fungal Proteins/metabolism ; Homeostasis/drug effects ; Leukocyte L1 Antigen Complex/pharmacology ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Zinc/metabolism
Chemical Substances	Fungal Proteins ; Leukocyte L1 Antigen Complex ; Copper (789U1901C5) ; Zinc (J41CSQ7QDS)
Language	English
Publishing date	2018-01-22
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	218698-6
ISSN	1098-5522 ; 0019-9567
ISSN (online)	1098-5522
ISSN	0019-9567
DOI	10.1128/IAI.00779-17
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Article ; Online: Revisiting and re-engineering the classical zinc finger peptide: consensus peptide-1 (CP-1).

Besold, Angelique N / Widger, Leland R / Namuswe, Frances / Michalek, Jamie L / Michel, Sarah L J / Goldberg, David P

Molecular bioSystems

2016 Volume 12, Issue 4, Page(s) 1183–1193

Abstract: Zinc plays key structural and catalytic roles in biology. Structural zinc sites are often referred to as zinc finger (ZF) sites, and the classical ZF contains a Cys2His2 motif that is involved in coordinating Zn(II). An optimized Cys2His2 ZF, named ... ...

Abstract	Zinc plays key structural and catalytic roles in biology. Structural zinc sites are often referred to as zinc finger (ZF) sites, and the classical ZF contains a Cys2His2 motif that is involved in coordinating Zn(II). An optimized Cys2His2 ZF, named consensus peptide 1 (CP-1), was identified more than 20 years ago using a limited set of sequenced proteins. We have reexamined the CP-1 sequence, using our current, much larger database of sequenced proteins that have been identified from high-throughput sequencing methods, and found the sequence to be largely unchanged. The CCHH ligand set of CP-1 was then altered to a CAHH motif to impart hydrolytic activity. This ligand set mimics the His2Cys ligand set of peptide deformylase (PDF), a hydrolytically active M(II)-centered (M = Zn or Fe) protein. The resultant peptide [CP-1(CAHH)] was evaluated for its ability to coordinate Zn(II) and Co(II) ions, adopt secondary structure, and promote hydrolysis. CP-1(CAHH) was found to coordinate Co(II) and Zn(II) and a pentacoordinate geometry for Co(II)-CP-1(CAHH) was implicated from UV-vis data. This suggests a His2Cys(H2O)2 environment at the metal center. The Zn(II)-bound CP-1(CAHH) was shown to adopt partial secondary structure by 1-D (1)H NMR spectroscopy. Both Zn(II)-CP-1(CAHH) and Co(II)-CP-1(CAHH) show good hydrolytic activity toward the test substrate 4-nitrophenyl acetate, exhibiting faster rates than most active synthetic Zn(II) complexes.
MeSH term(s)	Amino Acid Sequence ; Conserved Sequence ; Copper/chemistry ; Hydrolysis ; Ions/chemistry ; Metals/chemistry ; Oligopeptides/chemistry ; Peptides/chemistry ; Position-Specific Scoring Matrices ; Zinc/chemistry ; Zinc Fingers
Chemical Substances	CP-1 peptide ; Ions ; Metals ; Oligopeptides ; Peptides ; Copper (789U1901C5) ; Zinc (J41CSQ7QDS)
Language	English
Publishing date	2016-04
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2188635-0
ISSN	1742-2051 ; 1742-206X
ISSN (online)	1742-2051
ISSN	1742-206X
DOI	10.1039/c5mb00796h
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