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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 (2021)
Effect of Mutations in GvpJ and GvpM on Gas Vesicle Formation of Halobacterium salinarum.
In: Frontiers in microbiology, 12
doi: 10.3389/fmicb.2021.794240
Artikel, Bibliographie

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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 transformants by complementing the respective mutated gene with the remaining genes and inspecting the cells for the presence of gas vesicles (Vac). In case of GvpJ, 56 of 66 substitutions analyzed yielded Vac ΔJ + J transformants, indicating that GvpJ is very sensitive to alterations, whereas ten of the 38 GvpM variants resulted in Vac ΔM + M 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: 2021
Autor(en): Jost, Alisa ; Knitsch, Regine ; Völkner, Kerstin ; Pfeifer, Felicitas
Art des Eintrags: Bibliographie
Titel: Effect of Mutations in GvpJ and GvpM on Gas Vesicle Formation of Halobacterium salinarum
Sprache: Englisch
Publikationsjahr: Dezember 2021
Titel der Zeitschrift, Zeitung oder Schriftenreihe: Frontiers in microbiology
Jahrgang/Volume einer Zeitschrift: 12
DOI: 10.3389/fmicb.2021.794240
Zugehörige Links:
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 transformants by complementing the respective mutated gene with the remaining genes and inspecting the cells for the presence of gas vesicles (Vac). In case of GvpJ, 56 of 66 substitutions analyzed yielded Vac ΔJ + J transformants, indicating that GvpJ is very sensitive to alterations, whereas ten of the 38 GvpM variants resulted in Vac ΔM + M 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.

ID-Nummer: pmid:34975818
Zusätzliche Informationen:

Artikel-ID 794240

Fachbereich(e)/-gebiet(e): 10 Fachbereich Biologie
10 Fachbereich Biologie > Microbiology and Archaea
Hinterlegungsdatum: 10 Jan 2022 12:37
Letzte Änderung: 03 Jul 2024 02:55
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