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Tytuł:
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Expression, purification and oligomerization of the S-adenosylmethionine transporter.
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Autorzy:
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Wang D; State Key Laboratory of Medicinal Chemical Biology, Tianjin, 300350, China; College of Pharmacy, Nankai University, Tianjin, 300350, China.
Liu M; State Key Laboratory of Medicinal Chemical Biology, Tianjin, 300350, China; College of Pharmacy, Nankai University, Tianjin, 300350, China.
Li X; State Key Laboratory of Medicinal Chemical Biology, Tianjin, 300350, China; College of Pharmacy, Nankai University, Tianjin, 300350, China.
Wang X; State Key Laboratory of Medicinal Chemical Biology, Tianjin, 300350, China; College of Pharmacy, Nankai University, Tianjin, 300350, China. Electronic address: xq_.
Shen Y; State Key Laboratory of Medicinal Chemical Biology, Tianjin, 300350, China; College of Life Sciences, Nankai University, Tianjin, 300071, China. Electronic address: .
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Źródło:
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Protein expression and purification [Protein Expr Purif] 2020 Sep; Vol. 173, pp. 105648. Date of Electronic Publication: 2020 Apr 23.
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Typ publikacji:
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Journal Article; Research Support, Non-U.S. Gov't
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Język:
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English
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Imprint Name(s):
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Publication: Orlando, FL : Academic Press
Original Publication: San Diego : Academic Press, c1990-
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MeSH Terms:
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Amino Acid Transport Systems*/biosynthesis
Amino Acid Transport Systems*/chemistry
Amino Acid Transport Systems*/genetics
Amino Acid Transport Systems*/isolation & purification
Gene Expression*
Protein Multimerization*
Zebrafish Proteins*/biosynthesis
Zebrafish Proteins*/chemistry
Zebrafish Proteins*/genetics
Zebrafish Proteins*/isolation & purification
Zebrafish/*genetics
Animals ; Humans ; Male ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification ; Zebrafish/metabolism
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Contributed Indexing:
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Keywords: Expression; Membrane protein; Purification; S-Adenosylmethionine; SAMC
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Substance Nomenclature:
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0 (Amino Acid Transport Systems)
0 (Recombinant Proteins)
0 (Zebrafish Proteins)
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Entry Date(s):
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Date Created: 20200427 Date Completed: 20210121 Latest Revision: 20210121
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Update Code:
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20240105
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DOI:
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10.1016/j.pep.2020.105648
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PMID:
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32335303
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The S-adenosylmethionine carrier (SAMC) is a membrane transport protein located on the inner membrane of mitochondria that catalyzes the import of S-adenosylmethionine (SAM) into the mitochondrial matrix. SAMC mutations can cause a series of mitochondrial defects, including those affecting RNA stability, protein modification, mitochondrial translation and biosynthesis. Here, we describe the expression, purification and oligomerization of SAMC. The SAMC genes from three species were cloned into a eukaryotic expression vector with a GFP tag, and confocal microscopy analysis showed that these SAMCs were localized to mitochondria. A BacMam expression system was used for the expression of D. rerio SAMC with a FLAG tag. A size-exclusion chromatography analysis showed that SAMC may form a hexamer. A negative-staining electron microscopy analysis showed that SAMC formed tiny uniform particles and also confirmed the oligomerization of SAMC.
(Copyright © 2020 Elsevier Inc. All rights reserved.)
