Covalent labeling of the Arabidopsis plasma membrane H + -ATPase reveals 3D conformational changes involving the C-terminal regulatory domain.

Autor: Blackburn MR; Department of Biochemistry and Center for Genomic Sciences Innovation, University of Wisconsin-Madison, WI, USA., Nguyen TT; Department of Biochemistry and Center for Genomic Sciences Innovation, University of Wisconsin-Madison, WI, USA., Patton SE; Department of Biochemistry and Center for Genomic Sciences Innovation, University of Wisconsin-Madison, WI, USA., Bartosiak JM; Department of Biochemistry and Center for Genomic Sciences Innovation, University of Wisconsin-Madison, WI, USA., Sussman MR; Department of Biochemistry and Center for Genomic Sciences Innovation, University of Wisconsin-Madison, WI, USA.
Jazyk: angličtina
Zdroj: FEBS letters [FEBS Lett] 2024 Dec 03. Date of Electronic Publication: 2024 Dec 03.
DOI: 10.1002/1873-3468.15067
Abstrakt: The plasma membrane proton pump is the primary energy transducing, electrogenic ion pump of the plasma membrane in plants and fungi. Compared to its fungal counterpart, the plant plasma membrane proton pump's regulatory C-terminal domain (CTD) contains an additional regulatory segment that links multiple sensory pathways regulating plant cell length through phosphorylation and recruitment of regulatory 14-3-3 proteins. However, a complete structural model of a plant proton pump is lacking. Here, we performed covalent labeling with mass spectrometric analysis (CL-MS) on the Arabidopsis pump AHA2 to identify potential interactions between the CTD and the catalytic domains. Our results suggest that autoinhibition in the plant enzyme is much more structurally complex than in the fungal enzyme.
(© 2024 Federation of European Biochemical Societies.)
Databáze: MEDLINE
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