Engel, Anja J. ; Paech, Steffen ; Langhans, Markus ; Etten, James L. van ; Moroni, Anna ; Thiel, Gerhard ; Rauh, Oliver (2024)
Combination of hydrophobicity and codon usage bias determines sorting of model K⁺ channel protein to either mitochondria or endoplasmic reticulum.
In: Traffic : The moving front of cell biology, 2023, 24 (11)
doi: 10.26083/tuprints-00027170
Artikel, Zweitveröffentlichung, Verlagsversion
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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: | 2024 |
| Autor(en): | Engel, Anja J. ; Paech, Steffen ; Langhans, Markus ; Etten, James L. van ; Moroni, Anna ; Thiel, Gerhard ; Rauh, Oliver |
| Art des Eintrags: | Zweitveröffentlichung |
| Titel: | Combination of hydrophobicity and codon usage bias determines sorting of model K⁺ channel protein to either mitochondria or endoplasmic reticulum |
| Sprache: | Englisch |
| Publikationsjahr: | 4 Juni 2024 |
| Ort: | Darmstadt |
| Publikationsdatum der Erstveröffentlichung: | November 2023 |
| Ort der Erstveröffentlichung: | Oxford |
| Verlag: | Wiley-Blackwell |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Traffic : The moving front of cell biology |
| Jahrgang/Volume einer Zeitschrift: | 24 |
| (Heft-)Nummer: | 11 |
| DOI: | 10.26083/tuprints-00027170 |
| URL / URN: | https://tuprints.ulb.tu-darmstadt.de/27170 |
| Zugehörige Links: | |
| Herkunft: | Zweitveröffentlichung DeepGreen |
| 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. |
| Freie Schlagworte: | codon usage, effect of synonymous codon exchange, membrane protein sorting, transmembrane domain hydrophobicity |
| Status: | Verlagsversion |
| URN: | urn:nbn:de:tuda-tuprints-271701 |
| Sachgruppe der Dewey Dezimalklassifikatin (DDC): | 500 Naturwissenschaften und Mathematik > 540 Chemie 500 Naturwissenschaften und Mathematik > 570 Biowissenschaften, Biologie |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie 10 Fachbereich Biologie > 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: | 04 Jun 2024 12:45 |
| Letzte Änderung: | 05 Jun 2024 09:37 |
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| Suche nach Titel in: | TUfind oder in Google |
Verfügbare Versionen dieses Eintrags
- 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) [Gegenwärtig angezeigt]
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