WeightNameValue
1000 Titel
  • Mistic's membrane association and its assistance in overexpression of a human GPCR are independent processes
1000 Autor/in
  1. Marino, Jacopo |
  2. Keller, Sandro |
  3. Zerbe, Oliver |
  4. Bordag, Natalie |
1000 Erscheinungsjahr 2014
1000 LeibnizOpen
1000 Publikationstyp
  1. Artikel |
1000 Online veröffentlicht
  • 2014-10-25
1000 Erschienen in
1000 Quellenangabe
  • 24(1): 38–48
1000 FRL-Sammlung
1000 Verlagsversion
  • https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4282410/ |
  • https://doi.org/10.1002/pro.2582 |
1000 Ergänzendes Material
  • http://onlinelibrary.wiley.com/doi/10.1002/pro.2582/full#footer-support-info |
1000 Publikationsstatus
1000 Begutachtungsstatus
1000 Sprache der Publikation
1000 Abstract/Summary
  • The interaction of the Bacillus subtilis protein Mistic with the bacterial membrane and its role in promoting the overexpression of other membrane proteins are still matters of debate. In this study, we aimed to determine whether individual helical fragments of Mistic are sufficient for its interaction with membranes in vivo and in vitro. To this end, fragments encompassing each of Mistic's helical segments and combinations of them were produced as GFP-fusions, and their cellular localization was studied in Escherichia coli. Furthermore, peptides corresponding to the four helical fragments were synthesized by solid-phase peptide synthesis, and their ability to acquire secondary structure in a variety of lipids and detergents was studied by circular dichroism spectroscopy. Both types of experiments demonstrate that the third helical fragment of Mistic interacts only with LDAO micelles but does not partition into lipid bilayers. Interestingly, the other three helices interact with membranes in vivo and in vitro. Nevertheless, all of these short sequences can replace full-length Mistic as N-terminal fusions to achieve overexpression of a human G-protein-coupled receptor in E. coli, although with different effects on quantity and quality of the protein produced. A bioinformatic analysis of the Mistic family expanded the number of homologs from 4 to 20, including proteins outside the genus Bacillus. This information allowed us to discover a highly conserved Shine-Dalgarno sequence in the operon mstX-yugO that is important for downstream translation of the potassium ion channel yugO.
1000 Sacherschließung
lokal GFP-fusion
lokal lipids
lokal Mistic
lokal peptide–membrane interaction
lokal yugO
lokal GPCR expression
1000 Fachgruppe
  1. Biologie |
1000 Fächerklassifikation (DDC)
1000 Liste der Beteiligten
  1. https://frl.publisso.de/adhoc/creator/TWFyaW5vLCBKYWNvcG8=|https://frl.publisso.de/adhoc/creator/S2VsbGVyLCBTYW5kcm8=|https://frl.publisso.de/adhoc/creator/WmVyYmUsIE9saXZlcg==|http://orcid.org/0000-0002-9505-6271
1000 Objektart article
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1000 @id frl:6406495.rdf
1000 Erstellt am 2018-01-25T16:17:13.678+0100
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1000 Vgl. frl:6406495
1000 Oai Id
  1. oai:frl.publisso.de:frl:6406495 |
1000 Sichtbarkeit Metadaten public
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