Engel, Anja J. ; Paech, Steffen ; Langhans, Markus ; Etten, James L. van ; Moroni, Anna ; Thiel, Gerhard ; Rauh, Oliver (2023)
Combination of hydrophobicity and codon usage bias determines sorting of model K+ channel protein to either mitochondria or endoplasmic reticulum.
In: Traffic, 24 (11)
doi: 10.1111/tra.12915
Artikel, Bibliographie
Dies ist die neueste Version dieses Eintrags.
Kurzbeschreibung (Abstract)
When the K channel-like protein Kesv from Ectocarpus siliculosus virus 1 is heterologously expressed in mammalian cells, it is sorted to the mitochondria. This targeting can be redirected to the endoplasmic reticulum (ER) by altering the codon usage in distinct regions of the gene or by inserting a triplet of hydrophobic amino acids (AAs) into the protein's C-terminal transmembrane domain (ct-TMD). Systematic variations in the flavor of the inserted AAs and/or its codon usage show that a positive charge in the inserted AA triplet alone serves as strong signal for mitochondria sorting. In cases of neutral AA triplets, mitochondria sorting are favored by a combination of hydrophilic AAs and rarely used codons; sorting to the ER exhibits the inverse dependency. This propensity for ER sorting is particularly high when a common codon follows a rarer one in the AA triplet; mitochondria sorting in contrast is supported by codon uniformity. Since parameters like positive charge, hydrophobic AAs, and common codons are known to facilitate elongation of nascent proteins in the ribosome the data suggest a mechanism in which local changes in elongation velocity and co-translational folding in the ct-TMD influence intracellular protein sorting.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2023 |
| Autor(en): | Engel, Anja J. ; Paech, Steffen ; Langhans, Markus ; Etten, James L. van ; Moroni, Anna ; Thiel, Gerhard ; Rauh, Oliver |
| Art des Eintrags: | Bibliographie |
| Titel: | Combination of hydrophobicity and codon usage bias determines sorting of model K+ channel protein to either mitochondria or endoplasmic reticulum |
| Sprache: | Englisch |
| Publikationsjahr: | 14 August 2023 |
| Verlag: | Wiley |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Traffic |
| Jahrgang/Volume einer Zeitschrift: | 24 |
| (Heft-)Nummer: | 11 |
| DOI: | 10.1111/tra.12915 |
| Zugehörige Links: | |
| Kurzbeschreibung (Abstract): | When the K channel-like protein Kesv from Ectocarpus siliculosus virus 1 is heterologously expressed in mammalian cells, it is sorted to the mitochondria. This targeting can be redirected to the endoplasmic reticulum (ER) by altering the codon usage in distinct regions of the gene or by inserting a triplet of hydrophobic amino acids (AAs) into the protein's C-terminal transmembrane domain (ct-TMD). Systematic variations in the flavor of the inserted AAs and/or its codon usage show that a positive charge in the inserted AA triplet alone serves as strong signal for mitochondria sorting. In cases of neutral AA triplets, mitochondria sorting are favored by a combination of hydrophilic AAs and rarely used codons; sorting to the ER exhibits the inverse dependency. This propensity for ER sorting is particularly high when a common codon follows a rarer one in the AA triplet; mitochondria sorting in contrast is supported by codon uniformity. Since parameters like positive charge, hydrophobic AAs, and common codons are known to facilitate elongation of nascent proteins in the ribosome the data suggest a mechanism in which local changes in elongation velocity and co-translational folding in the ct-TMD influence intracellular protein sorting. |
| ID-Nummer: | pmid:37578147 |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie 10 Fachbereich Biologie > Plant Membrane Biophyscis (am 20.12.23 umbenannt in Biologie der Algen und Protozoen) 07 Fachbereich Chemie 07 Fachbereich Chemie > Ernst-Berl-Institut 07 Fachbereich Chemie > Ernst-Berl-Institut > Fachgebiet Makromolekulare Chemie 07 Fachbereich Chemie > Ernst-Berl-Institut > Fachgebiet Makromolekulare Chemie > Makromolekulare Chemie und Papierchemie |
| Hinterlegungsdatum: | 29 Aug 2023 08:17 |
| Letzte Änderung: | 05 Jun 2024 09:38 |
| PPN: | 511133758 |
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| Suche nach Titel in: | TUfind oder in Google |
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Combination of hydrophobicity and codon usage bias determines sorting of model K⁺ channel protein to either mitochondria or endoplasmic reticulum. (deposited 04 Jun 2024 12:45)
- Combination of hydrophobicity and codon usage bias determines sorting of model K+ channel protein to either mitochondria or endoplasmic reticulum. (deposited 29 Aug 2023 08:17) [Gegenwärtig angezeigt]
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