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Effect of Mutations in GvpJ and GvpM on Gas Vesicle Formation of Halobacterium salinarum

Jost, Alisa ; Knitsch, Regine ; Völkner, Kerstin ; Pfeifer, Felicitas (2022)
Effect of Mutations in GvpJ and GvpM on Gas Vesicle Formation of Halobacterium salinarum.
In: Frontiers in Microbiology, 2022, 12
doi: 10.26083/tuprints-00020268
Artikel, Zweitveröffentlichung, Verlagsversion

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Kurzbeschreibung (Abstract)

The two haloarchaeal proteins, GvpM and GvpJ, are homologous to GvpA, the major gas vesicle structural protein. All three are hydrophobic and essential for gas vesicle formation. The effect of mutations in GvpJ and GvpM was studied in Haloferax volcanii transformants by complementing the respective mutated gene with the remaining gvp genes and inspecting the cells for the presence of gas vesicles (Vac⁺). In case of GvpJ, 56 of 66 substitutions analyzed yielded Vac⁻ ΔJ + Jmut transformants, indicating that GvpJ is very sensitive to alterations, whereas ten of the 38 GvpM variants resulted in Vac⁻ ΔM + Mmut transformants. The variants were also tested by split-GFP for their ability to interact with their partner protein GvpL. Some of the alterations leading to a Vac⁻ phenotype affected the J/L or M/L interaction. Also, the interactions J/A and J/M were studied using fragments to exclude an unspecific aggregation of these hydrophobic proteins. Both fragments of GvpJ interacted with the M1–25 and M60–84 fragments of GvpM, and fragment J1–56 of GvpJ interacted with the N-terminal fragment A1–22 of GvpA. A comparison of the results on the three homologous proteins indicates that despite their relatedness, GvpA, GvpJ, and GvpM have unique features and cannot substitute each other.

Typ des Eintrags: Artikel
Erschienen: 2022
Autor(en): Jost, Alisa ; Knitsch, Regine ; Völkner, Kerstin ; Pfeifer, Felicitas
Art des Eintrags: Zweitveröffentlichung
Titel: Effect of Mutations in GvpJ and GvpM on Gas Vesicle Formation of Halobacterium salinarum
Sprache: Englisch
Publikationsjahr: 2022
Publikationsdatum der Erstveröffentlichung: 2022
Verlag: Frontiers Media S.A.
Titel der Zeitschrift, Zeitung oder Schriftenreihe: Frontiers in Microbiology
Jahrgang/Volume einer Zeitschrift: 12
Kollation: 17 Seiten
DOI: 10.26083/tuprints-00020268
URL / URN: https://tuprints.ulb.tu-darmstadt.de/20268
Zugehörige Links:
Herkunft: Zweitveröffentlichung DeepGreen
Kurzbeschreibung (Abstract):

The two haloarchaeal proteins, GvpM and GvpJ, are homologous to GvpA, the major gas vesicle structural protein. All three are hydrophobic and essential for gas vesicle formation. The effect of mutations in GvpJ and GvpM was studied in Haloferax volcanii transformants by complementing the respective mutated gene with the remaining gvp genes and inspecting the cells for the presence of gas vesicles (Vac⁺). In case of GvpJ, 56 of 66 substitutions analyzed yielded Vac⁻ ΔJ + Jmut transformants, indicating that GvpJ is very sensitive to alterations, whereas ten of the 38 GvpM variants resulted in Vac⁻ ΔM + Mmut transformants. The variants were also tested by split-GFP for their ability to interact with their partner protein GvpL. Some of the alterations leading to a Vac⁻ phenotype affected the J/L or M/L interaction. Also, the interactions J/A and J/M were studied using fragments to exclude an unspecific aggregation of these hydrophobic proteins. Both fragments of GvpJ interacted with the M1–25 and M60–84 fragments of GvpM, and fragment J1–56 of GvpJ interacted with the N-terminal fragment A1–22 of GvpA. A comparison of the results on the three homologous proteins indicates that despite their relatedness, GvpA, GvpJ, and GvpM have unique features and cannot substitute each other.

Freie Schlagworte: protein–protein interaction, split-GFP, Haloferax volcanii, substitution variants, accessory Gvp proteins
Status: Verlagsversion
URN: urn:nbn:de:tuda-tuprints-202688
Sachgruppe der Dewey Dezimalklassifikatin (DDC): 500 Naturwissenschaften und Mathematik > 570 Biowissenschaften, Biologie
Fachbereich(e)/-gebiet(e): 10 Fachbereich Biologie
10 Fachbereich Biologie > Microbiology and Archaea
Hinterlegungsdatum: 13 Mai 2022 13:26
Letzte Änderung: 16 Mai 2022 05:16
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