Cell-free expression, purification, and membrane reconstitution for NMR studies of the nonstructural protein 4B from hepatitis C virus
We describe the expression of the hepatitis C virus nonstructural protein 4B (NS4B), which is an integral membrane protein, in a wheat germ cell-free system, the subsequent purification and characterization of NS4B and its insertion into proteoliposomes in amounts sufficient for multidimensional sol...
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| Veröffentlicht in: | Journal of biomolecular NMR 2016-06, Vol.65 (2), p.87-98 |
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| creator | Fogeron, Marie-Laure Jirasko, Vlastimil Penzel, Susanne Paul, David Montserret, Roland Danis, Clément Lacabanne, Denis Badillo, Aurélie Gouttenoire, Jérôme Moradpour, Darius Bartenschlager, Ralf Penin, François Meier, Beat H. Böckmann, Anja |
| description | We describe the expression of the hepatitis C virus nonstructural protein 4B (NS4B), which is an integral membrane protein, in a wheat germ cell-free system, the subsequent purification and characterization of NS4B and its insertion into proteoliposomes in amounts sufficient for multidimensional solid-state NMR spectroscopy. First spectra of the isotopically [
2
H,
13
C,
15
N]-labeled protein are shown to yield narrow
13
C resonance lines and a proper, predominantly α-helical fold. Clean residue-selective leucine, isoleucine and threonine-labeling is demonstrated. These results evidence the suitability of the wheat germ-produced integral membrane protein NS4B for solid-state NMR. Still, the proton linewidth under fast magic angle spinning is broader than expected for a perfect sample and possible causes are discussed. |
| doi_str_mv | 10.1007/s10858-016-0040-2 |
| format | Article |
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2
H,
13
C,
15
N]-labeled protein are shown to yield narrow
13
C resonance lines and a proper, predominantly α-helical fold. Clean residue-selective leucine, isoleucine and threonine-labeling is demonstrated. These results evidence the suitability of the wheat germ-produced integral membrane protein NS4B for solid-state NMR. Still, the proton linewidth under fast magic angle spinning is broader than expected for a perfect sample and possible causes are discussed.</description><identifier>ISSN: 0925-2738</identifier><identifier>EISSN: 1573-5001</identifier><identifier>DOI: 10.1007/s10858-016-0040-2</identifier><identifier>PMID: 27233794</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Amino Acid Sequence ; Biochemistry ; Biochemistry, Molecular Biology ; Biological and Medical Physics ; Biophysics ; Carbon-13 Magnetic Resonance Spectroscopy ; Circular Dichroism ; Gene Expression ; Hepatitis ; Hepatitis C virus ; Humans ; Life Sciences ; Magnetic Resonance Spectroscopy - methods ; Membrane Proteins - chemistry ; Microbiology and Parasitology ; Nuclear Magnetic Resonance, Biomolecular - methods ; Physics ; Physics and Astronomy ; Protein Domains ; Proteolipids - chemistry ; Spectroscopy/Spectrometry ; Structural Biology ; Triticum aestivum ; Viral Nonstructural Proteins - chemistry ; Viral Nonstructural Proteins - genetics ; Viral Nonstructural Proteins - isolation & purification ; Virology</subject><ispartof>Journal of biomolecular NMR, 2016-06, Vol.65 (2), p.87-98</ispartof><rights>Springer Science+Business Media Dordrecht 2016</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c482t-d8a940714f810b07e0288ca3f1e5b3e850263e59d888cec9f2967cc6e75e3f7e3</citedby><cites>FETCH-LOGICAL-c482t-d8a940714f810b07e0288ca3f1e5b3e850263e59d888cec9f2967cc6e75e3f7e3</cites><orcidid>0000-0002-9107-4464 ; 0000-0002-2146-8740 ; 0000-0001-5601-9307 ; 0000-0001-8149-7941 ; 0000-0002-2671-5843</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10858-016-0040-2$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10858-016-0040-2$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,780,784,885,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27233794$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-03347523$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Fogeron, Marie-Laure</creatorcontrib><creatorcontrib>Jirasko, Vlastimil</creatorcontrib><creatorcontrib>Penzel, Susanne</creatorcontrib><creatorcontrib>Paul, David</creatorcontrib><creatorcontrib>Montserret, Roland</creatorcontrib><creatorcontrib>Danis, Clément</creatorcontrib><creatorcontrib>Lacabanne, Denis</creatorcontrib><creatorcontrib>Badillo, Aurélie</creatorcontrib><creatorcontrib>Gouttenoire, Jérôme</creatorcontrib><creatorcontrib>Moradpour, Darius</creatorcontrib><creatorcontrib>Bartenschlager, Ralf</creatorcontrib><creatorcontrib>Penin, François</creatorcontrib><creatorcontrib>Meier, Beat H.</creatorcontrib><creatorcontrib>Böckmann, Anja</creatorcontrib><title>Cell-free expression, purification, and membrane reconstitution for NMR studies of the nonstructural protein 4B from hepatitis C virus</title><title>Journal of biomolecular NMR</title><addtitle>J Biomol NMR</addtitle><addtitle>J Biomol NMR</addtitle><description>We describe the expression of the hepatitis C virus nonstructural protein 4B (NS4B), which is an integral membrane protein, in a wheat germ cell-free system, the subsequent purification and characterization of NS4B and its insertion into proteoliposomes in amounts sufficient for multidimensional solid-state NMR spectroscopy. First spectra of the isotopically [
2
H,
13
C,
15
N]-labeled protein are shown to yield narrow
13
C resonance lines and a proper, predominantly α-helical fold. Clean residue-selective leucine, isoleucine and threonine-labeling is demonstrated. These results evidence the suitability of the wheat germ-produced integral membrane protein NS4B for solid-state NMR. Still, the proton linewidth under fast magic angle spinning is broader than expected for a perfect sample and possible causes are discussed.</description><subject>Amino Acid Sequence</subject><subject>Biochemistry</subject><subject>Biochemistry, Molecular Biology</subject><subject>Biological and Medical Physics</subject><subject>Biophysics</subject><subject>Carbon-13 Magnetic Resonance Spectroscopy</subject><subject>Circular Dichroism</subject><subject>Gene Expression</subject><subject>Hepatitis</subject><subject>Hepatitis C virus</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Magnetic Resonance Spectroscopy - methods</subject><subject>Membrane Proteins - chemistry</subject><subject>Microbiology and Parasitology</subject><subject>Nuclear Magnetic Resonance, Biomolecular - methods</subject><subject>Physics</subject><subject>Physics and Astronomy</subject><subject>Protein Domains</subject><subject>Proteolipids - chemistry</subject><subject>Spectroscopy/Spectrometry</subject><subject>Structural Biology</subject><subject>Triticum aestivum</subject><subject>Viral Nonstructural Proteins - 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First spectra of the isotopically [
2
H,
13
C,
15
N]-labeled protein are shown to yield narrow
13
C resonance lines and a proper, predominantly α-helical fold. Clean residue-selective leucine, isoleucine and threonine-labeling is demonstrated. These results evidence the suitability of the wheat germ-produced integral membrane protein NS4B for solid-state NMR. Still, the proton linewidth under fast magic angle spinning is broader than expected for a perfect sample and possible causes are discussed.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>27233794</pmid><doi>10.1007/s10858-016-0040-2</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0002-9107-4464</orcidid><orcidid>https://orcid.org/0000-0002-2146-8740</orcidid><orcidid>https://orcid.org/0000-0001-5601-9307</orcidid><orcidid>https://orcid.org/0000-0001-8149-7941</orcidid><orcidid>https://orcid.org/0000-0002-2671-5843</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Journal of biomolecular NMR, 2016-06, Vol.65 (2), p.87-98 |
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| source | MEDLINE; SpringerLink Journals - AutoHoldings |
| subjects | Amino Acid Sequence Biochemistry Biochemistry, Molecular Biology Biological and Medical Physics Biophysics Carbon-13 Magnetic Resonance Spectroscopy Circular Dichroism Gene Expression Hepatitis Hepatitis C virus Humans Life Sciences Magnetic Resonance Spectroscopy - methods Membrane Proteins - chemistry Microbiology and Parasitology Nuclear Magnetic Resonance, Biomolecular - methods Physics Physics and Astronomy Protein Domains Proteolipids - chemistry Spectroscopy/Spectrometry Structural Biology Triticum aestivum Viral Nonstructural Proteins - chemistry Viral Nonstructural Proteins - genetics Viral Nonstructural Proteins - isolation & purification Virology |
| title | Cell-free expression, purification, and membrane reconstitution for NMR studies of the nonstructural protein 4B from hepatitis C virus |
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