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Article: Purification and refolding protocol for cold-active recombinant esterase AaSGNH1 from Aphanizomenon flos-aquae expressed as insoluble inclusion bodies

Knepp, Zachary J. / Ghaner, Ashlea / Root, Kyle T.

Preparative biochemistry & biotechnology. 2022 Apr. 1, v. 52, no. 4

2022

Abstract: Microbial esterases are a highly desirable tool for numerous biosynthetic and biotechnological applications requiring ester bond cleavage. Once identified, microbial esterases are often produced recombinantly in Escherichia coli to enhance yield and ease ...

Abstract	Microbial esterases are a highly desirable tool for numerous biosynthetic and biotechnological applications requiring ester bond cleavage. Once identified, microbial esterases are often produced recombinantly in Escherichia coli to enhance yield and ease of purification. In this study a polyhistidine-tagged SGNH esterase gene (AaSGNH1), originating from the cyanobacterium Aphanizomenon flos-aquae, was cloned into an over-expression plasmid and expressed in BL21(DE3) cells. The recombinant esterase enzyme was produced as inactive inclusion bodies which were insoluble in 8 M urea but readily solubilized by the detergent Empigen BB®. Crucially, the procurement of active enzyme required controlled removal of detergent during column chromatography and dialysis steps. The refolded esterase was characterized with respect to its ability to catalyze the cleavage of p-nitrophenol esters of different chain lengths (C2, C8, C16). In addition, the temperature and pH optima were determined and it was found that the enzyme was most active at low temperatures (5–15 °C) and under alkaline conditions (pH 8–10). It was found that the kinetic properties of AaSGNH1 were remarkably similar to other SGNH esterases described thereby validating that the protein was effectively refolded. Overall, this study provides a simple strategy for isolating cold-active recombinant esterase enzyme when expressed as inclusion bodies.
Keywords	Aphanizomenon flos-aquae ; Escherichia coli ; biosynthesis ; biotechnology ; chromatography ; cleavage (chemistry) ; detergents ; dialysis ; esterases ; genes ; p-nitrophenol ; pH ; plasmids ; solubilization ; temperature ; urea
Language	English
Dates of publication	2022-0401
Size	p. 394-403.
Publishing place	Taylor & Francis
Document type	Article
ZDB-ID	1322522-4
ISSN	1532-2297 ; 1082-6068
ISSN (online)	1532-2297
ISSN	1082-6068
DOI	10.1080/10826068.2021.1952601
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Article ; Online: Purification and refolding protocol for cold-active recombinant esterase

Knepp, Zachary J / Ghaner, Ashlea / Root, Kyle T

Preparative biochemistry & biotechnology

2021 Volume 52, Issue 4, Page(s) 394–403

Abstract	Microbial esterases are a highly desirable tool for numerous biosynthetic and biotechnological applications requiring ester bond cleavage. Once identified, microbial esterases are often produced recombinantly in
MeSH term(s)	Aphanizomenon ; Cloning, Molecular ; Detergents/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Esterases/metabolism ; Inclusion Bodies/chemistry ; Recombinant Proteins ; Renal Dialysis
Chemical Substances	Detergents ; Recombinant Proteins ; Esterases (EC 3.1.-)
Language	English
Publishing date	2021-08-06
Publishing country	England
Document type	Journal Article
ZDB-ID	1322522-4
ISSN	1532-2297 ; 1082-6068
ISSN (online)	1532-2297
ISSN	1082-6068
DOI	10.1080/10826068.2021.1952601
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Article ; Online: Reconstitution of full-length human caveolin-1 into phospholipid bicelles: Validation by analytical ultracentrifugation.

Rieth, Monica D / Root, Kyle T / Glover, Kerney Jebrell

Biophysical chemistry

2020 Volume 259, Page(s) 106339

Abstract: A significant hurdle in obtaining biophysical information on membrane proteins is developing a successful strategy for their reconstitution into a suitable membrane mimic. In particular, utilization of the more 'native-like' membrane mimics such as ... ...

Abstract	A significant hurdle in obtaining biophysical information on membrane proteins is developing a successful strategy for their reconstitution into a suitable membrane mimic. In particular, utilization of the more 'native-like' membrane mimics such as bicelles is generally more challenging than simple micellar solubilization. Caveolin-1, an integral membrane protein involved in membrane curvature, endocytosis, mechano-protection, and signal transduction, has been shown to be particularly recalcitrant to standard reconstitution protocols due to its highly hydrophobic characteristics. Herein we describe a robust method to incorporate recombinantly produced full-length caveolin-1 into bicelles at levels needed for biophysical experimentation. The benchmark of successful reconstitution is the obtainment of protein in a homogeneous state; therefore, we developed a validation procedure to monitor the success of the reconstitution using analytical ultracentrifugation of density-matched bicelles. Our findings indicated that our protocol produces a very homogeneous preparation of caveolin-1 associated with bicelles, and that caveolin-1 is highly α-helical (by circular dichroism spectroscopy). We believe that this methodology will serve as a general strategy to facilitate biophysical studies on membrane proteins.
MeSH term(s)	Caveolin 1/chemistry ; Circular Dichroism ; Humans ; Lipid Bilayers/chemistry ; Phospholipids/chemistry ; Recombinant Proteins/chemistry ; Reproducibility of Results ; Spectrometry, Fluorescence ; Ultracentrifugation/methods
Chemical Substances	CAV1 protein, human ; Caveolin 1 ; Lipid Bilayers ; Phospholipids ; Recombinant Proteins
Language	English
Publishing date	2020-02-26
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	185052-0
ISSN	1873-4200 ; 0301-4622
ISSN (online)	1873-4200
ISSN	0301-4622
DOI	10.1016/j.bpc.2020.106339
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Zs.A 1147: Show issues

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Article ; Online: Secondary structure of caveolins: a mini review.

Root, Kyle T / Julien, Jeffrey A / Glover, Kerney Jebrell

Biochemical Society transactions

2019 Volume 47, Issue 5, Page(s) 1489–1498

Abstract: Caveolae are 50-100 nm invaginations found within the plasma membrane of cells. Caveolae are involved in many processes that are essential for homeostasis, most notably endocytosis, mechano-protection, and signal transduction. Within these invaginations, ...

Abstract	Caveolae are 50-100 nm invaginations found within the plasma membrane of cells. Caveolae are involved in many processes that are essential for homeostasis, most notably endocytosis, mechano-protection, and signal transduction. Within these invaginations, the most important proteins are caveolins, which in addition to participating in the aforementioned processes are structural proteins responsible for caveolae biogenesis. When caveolin is misregulated or mutated, many disease states can arise which include muscular dystrophy, cancers, and heart disease. Unlike most integral membrane proteins, caveolin does not have a transmembrane orientation; instead, it is postulated to adopt an unusual topography where both the N- and C-termini lie on the cytoplasmic side of the membrane, and the hydrophobic span adopts an intramembrane loop conformation. While knowledge concerning the biology of caveolin has progressed apace, fundamental structural information has proven more difficult to obtain. In this mini-review, we curate as well as critically assess the structural data that have been obtained on caveolins to date in order to build a robust and compelling model of the caveolin secondary structure.
MeSH term(s)	Amino Acid Sequence ; Animals ; Caveolins/chemistry ; Humans ; Protein Structure, Secondary ; Sequence Homology, Amino Acid
Chemical Substances	Caveolins
Language	English
Publishing date	2019-09-10
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/BST20190375
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Zs.A 944: Show issues

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Article: Reconstitution and spectroscopic analysis of caveolin-1 residues 62-178 reveals that proline 110 governs its structure and solvent exposure.

Root, Kyle T / Glover, Kerney Jebrell

Biochimica et biophysica acta

2016 Volume 1858, Issue 4, Page(s) 682–688

Abstract: Caveolin-1 is a membrane protein that possesses an unusual topology where both N- and C-termini are cytoplasmic as a result of a membrane-embedded turn. In particular, proline 110 has been postulated to be the linchpin of this unusual motif. Using a ... ...

Abstract	Caveolin-1 is a membrane protein that possesses an unusual topology where both N- and C-termini are cytoplasmic as a result of a membrane-embedded turn. In particular, proline 110 has been postulated to be the linchpin of this unusual motif. Using a caveolin-1 construct (residues 62-178) reconstituted into dodecylphosphocholine micelles with and without a cholesterol mimic, the changes that occurred upon P110A mutation were probed. Using far UV circular dichroism spectroscopy it was shown that cholesterol attenuated the helicity of caveolin-1, and that mutation of P110 to alanine caused a significant increase in the α-helicity of the protein. Near UV circular dichroism spectroscopy showed significant changes in structure and/or environment upon mutation that again were modulated by the presence of cholesterol. Stern-Volmer quenching and λ(max) analysis of tryptophan residues showed that the proline mutation caused W85 to become more exposed, W98 and W115 to become less exposed, and W128 showed no change. This finding provided evidence that regions proximal and far away from the proline are buried differentially upon its mutation and therefore this residue is strongly tied to maintaining the hydrophobic coverage along the caveolin-1 sequence. In the presence of cholesterol, the accessibilities of the two tryptophan residues that proceeded position 110 were altered much more significantly upon P110A mutation than the two tryptophans aft P110. Overall, this work provides strong evidence that proline 110 is critical for maintaining both the structure and hydrophobic coverage of caveolin-1 and that cholesterol also plays a significant role in modulating these parameters.
MeSH term(s)	Alanine/chemistry ; Caveolin 1/chemistry ; Caveolin 1/metabolism ; Cholesterol/chemistry ; Cholesterol/metabolism ; Circular Dichroism ; Hydrophobic and Hydrophilic Interactions ; Micelles ; Mutation ; Phosphorylcholine/analogs & derivatives ; Phosphorylcholine/chemistry ; Proline/chemistry ; Protein Structure, Secondary ; Solvents/chemistry ; Structure-Activity Relationship ; Tryptophan/chemistry
Chemical Substances	Caveolin 1 ; Micelles ; Solvents ; Phosphorylcholine (107-73-3) ; dodecylphosphocholine (53949-18-1) ; Tryptophan (8DUH1N11BX) ; Cholesterol (97C5T2UQ7J) ; Proline (9DLQ4CIU6V) ; Alanine (OF5P57N2ZX)
Language	English
Publishing date	2016-04
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamem.2016.01.007
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Uc I Zs.247: Show issues

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Article ; Online: Efficient solubilization and purification of highly insoluble membrane proteins expressed as inclusion bodies using perfluorooctanoic acid.

Plucinsky, Sarah M / Root, Kyle T / Glover, Kerney Jebrell

Protein expression and purification

2017 Volume 143, Page(s) 34–37

Abstract: The purification of membrane proteins can be challenging due to their low solubility in conventional detergents and/or chaotropic solutions. The introduction of fusion systems that promote the formation of inclusion bodies has facilitated the over- ... ...

Abstract	The purification of membrane proteins can be challenging due to their low solubility in conventional detergents and/or chaotropic solutions. The introduction of fusion systems that promote the formation of inclusion bodies has facilitated the over-expression of membrane proteins. In this protocol, we describe the use of perfluorooctanoic acid (PFOA) as an aid in the purification of highly hydrophobic membrane proteins expressed as inclusion bodies. The advantage of utilizing PFOA is threefold: first, PFOA is able to reliably solubilize inclusion bodies, second, PFOA is compatible with nickel affinity chromatography, and third, PFOA can be efficiently dialyzed away to produce a detergent free sample. To demonstrate the utility of employing PFOA, we expressed and purified a segment of the extremely hydrophobic membrane protein caveolin-1.
MeSH term(s)	Caprylates/chemistry ; Escherichia coli/metabolism ; Fluorocarbons/chemistry ; Inclusion Bodies/chemistry ; Inclusion Bodies/metabolism ; Membrane Proteins/chemistry ; Membrane Proteins/isolation & purification ; Membrane Proteins/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism ; Solubility
Chemical Substances	Caprylates ; Fluorocarbons ; Membrane Proteins ; Recombinant Proteins ; perfluorooctanoic acid (947VD76D3L)
Language	English
Publishing date	2017-10-21
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1055455-5
ISSN	1096-0279 ; 1046-5928
ISSN (online)	1096-0279
ISSN	1046-5928
DOI	10.1016/j.pep.2017.10.012
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Article ; Online: One-step site-specific S-alkylation of full-length caveolin-1: Lipidation modulates the topology of its C-terminal domain.

Julien, Jeffrey A / Rousseau, Alain / Perone, Thomas V / LaGatta, David M / Hong, Chan / Root, Kyle T / Park, Soohyung / Fuanta, René / Im, Wonpil / Glover, Kerney Jebrell

Protein science : a publication of the Protein Society

2023 Volume 32, Issue 11, Page(s) e4791

Abstract: Caveolin-1 is an integral membrane protein that is known to acquire a number of posttranslational modifications upon trafficking to the plasma membrane. In particular, caveolin-1 is palmitoylated at three cysteine residues (C133, C143, and C156) located ... ...

Abstract	Caveolin-1 is an integral membrane protein that is known to acquire a number of posttranslational modifications upon trafficking to the plasma membrane. In particular, caveolin-1 is palmitoylated at three cysteine residues (C133, C143, and C156) located within the C-terminal domain of the protein which could have structural and topological implications. Herein, a reliable preparation of full-length S-alkylated caveolin-1, which closely mimics the palmitoylation observed in vivo, is described. HPLC and ESI-LC-MS analyses verified the addition of the C16 alkyl groups to caveolin-1 constructs containing one (C133), two (C133 and C143), and three (C133, C143, and C156) cysteine residues. Circular dichroism spectroscopy analysis of the constructs revealed that S-alkylation does not significantly affect the global helicity of the protein; however, molecular dynamics simulations revealed that there were local regions where the helicity was altered positively or negatively by S-alkylation. In addition, the simulations showed that lipidation tames the topological promiscuity of the C-terminal domain, resulting in a disposition within the bilayer characterized by increased depth.
MeSH term(s)	Caveolin 1/genetics ; Caveolin 1/chemistry ; Caveolin 1/metabolism ; Cysteine/metabolism ; Membrane Proteins/chemistry ; Cell Membrane/metabolism ; Alkylation
Chemical Substances	Caveolin 1 ; Cysteine (K848JZ4886) ; Membrane Proteins
Language	English
Publishing date	2023-10-06
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	1106283-6
ISSN	1469-896X ; 0961-8368
ISSN (online)	1469-896X
ISSN	0961-8368
DOI	10.1002/pro.4791
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Zs.A 3407: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article: Recent progress in the topology, structure, and oligomerization of caveolin: a building block of caveolae.

Root, Kyle T / Plucinsky, Sarah M / Glover, Kerney Jebrell

Current topics in membranes

2015 Volume 75, Page(s) 305–336

Abstract: Caveolae are cholesterol-rich plasma membrane invaginations that are found in a plethora of cell types. They play many roles including signal transduction, endocytosis, and mechanoprotection. The most critical protein in caveolae is the integral membrane ...

Abstract	Caveolae are cholesterol-rich plasma membrane invaginations that are found in a plethora of cell types. They play many roles including signal transduction, endocytosis, and mechanoprotection. The most critical protein in caveolae is the integral membrane protein, caveolin, which has been shown to be necessary for caveolae formation, and governs the major functions attributed to caveolae. Caveolin is postulated to act as a scaffold in the high molecular weight striated coat that surrounds the caveolar bulb, stabilizing it. Caveolin interacts, both directly and indirectly, with a large number of signaling molecules, and presides over the endocytosis of molecular cargo by caveolae. However, many of the key biophysical aspects of the caveolin protein, its structure, topology, and oligomeric behavior, are just beginning to come to light. Herein is an up-to-date summary and critique of the progress that has been made in understanding caveolin on a molecular and atomic level.
MeSH term(s)	Animals ; Caveolae/chemistry ; Caveolae/metabolism ; Caveolin 1/chemistry ; Caveolin 1/metabolism ; Cholesterol/metabolism ; Endocytosis ; Humans ; Protein Multimerization ; Signal Transduction
Chemical Substances	Caveolin 1 ; Cholesterol (97C5T2UQ7J)
Language	English
Publishing date	2015
Publishing country	United States
Document type	Journal Article ; Review
ISSN	1063-5823
ISSN	1063-5823
DOI	10.1016/bs.ctm.2015.03.007
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Article ; Online: Probing the U-shaped conformation of caveolin-1 in a bilayer.

Rui, Huan / Root, Kyle T / Lee, Jinwoo / Glover, Kerney Jebrell / Im, Wonpil

Biophysical journal

2014 Volume 106, Issue 6, Page(s) 1371–1380

Abstract: Caveolin induces membrane curvature and drives the formation of caveolae that participate in many crucial cell functions such as endocytosis. The central portion of caveolin-1 contains two helices (H1 and H2) connected by a three-residue break with both ... ...

Abstract	Caveolin induces membrane curvature and drives the formation of caveolae that participate in many crucial cell functions such as endocytosis. The central portion of caveolin-1 contains two helices (H1 and H2) connected by a three-residue break with both N- and C-termini exposed to the cytoplasm. Although a U-shaped configuration is assumed based on its inaccessibility by extracellular matrix probes, caveolin structure in a bilayer remains elusive. This work aims to characterize the structure and dynamics of caveolin-1 (D82-S136; Cav182-136) in a DMPC bilayer using NMR, fluorescence emission measurements, and molecular dynamics simulations. The secondary structure of Cav182-136 from NMR chemical shift indexing analysis serves as a guideline for generating initial structural models. Fifty independent molecular dynamics simulations (100 ns each) are performed to identify its favorable conformation and orientation in the bilayer. A representative configuration was chosen from these multiple simulations and simulated for 1 μs to further explore its stability and dynamics. The results of these simulations mirror those from the tryptophan fluorescence measurements (i.e., Cav182-136 insertion depth in the bilayer), corroborate that Cav182-136 inserts in the membrane with U-shaped conformations, and show that the angle between H1 and H2 ranges from 35 to 69°, and the tilt angle of Cav182-136 is 27 ± 6°. The simulations also reveal that specific faces of H1 and H2 prefer to interact with each other and with lipid molecules, and these interactions stabilize the U-shaped conformation.
MeSH term(s)	Amino Acid Sequence ; Caveolin 1/chemistry ; Caveolin 1/metabolism ; Dimyristoylphosphatidylcholine/chemistry ; Lipid Bilayers/chemistry ; Lipid Bilayers/metabolism ; Molecular Dynamics Simulation ; Molecular Sequence Data ; Protein Binding ; Protein Structure, Tertiary
Chemical Substances	Caveolin 1 ; Lipid Bilayers ; Dimyristoylphosphatidylcholine (U86ZGC74V5)
Language	English
Publishing date	2014-03-24
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	218078-9
ISSN	1542-0086 ; 0006-3495
ISSN (online)	1542-0086
ISSN	0006-3495
DOI	10.1016/j.bpj.2014.02.005
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Zs.A 235: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Low- q Bicelles Are Mixed Micelles.

Caldwell, Tracy A / Baoukina, Svetlana / Brock, Ashton T / Oliver, Ryan C / Root, Kyle T / Krueger, Joanna K / Glover, Kerney Jebrell / Tieleman, D Peter / Columbus, Linda

The journal of physical chemistry letters

2018 Volume 9, Issue 15, Page(s) 4469–4473

Abstract: Bicelles are used in many membrane protein studies because they are thought to be more bilayer-like than micelles. We investigated the properties of "isotropic" bicelles by small-angle neutron scattering, small-angle X-ray scattering, fluorescence ... ...

Abstract	Bicelles are used in many membrane protein studies because they are thought to be more bilayer-like than micelles. We investigated the properties of "isotropic" bicelles by small-angle neutron scattering, small-angle X-ray scattering, fluorescence anisotropy, and molecular dynamics. All data suggest that bicelles with a q value below 1 deviate from the classic bicelle that contains lipids in the core and detergent in the rim. Thus not all isotropic bicelles are bilayer-like.
Language	English
Publishing date	2018-07-25
Publishing country	United States
Document type	Journal Article
ISSN	1948-7185
ISSN (online)	1948-7185
DOI	10.1021/acs.jpclett.8b02079
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