The Complex I Subunit B22 Contains a LYR Domain That is Crucial for an Interaction with the Mitochondrial Acyl Carrier Protein SDAP1

Overview

Journal Plant J

Specialties Biology
Cell Biology
Molecular Biology

Date 2025 Feb 21

PMID 39981882

Authors

Saurabh Saha

Simge Parlar

Etienne H Meyer

Monika W Murcha

Affiliations

Soon will be listed here.

Abstract

Mitochondrial complex I (CI), a large multi-subunit respiratory complex contains two LYR (leucine/tyrosine/arginine) domain-containing subunits, B14 (NDUA6/LYRM6) and B22 (NDUB9/LYRM3). Mitochondrial LYR (LYRM) proteins are soluble matrix-located proteins that have been implicated in diverse functions such as iron-sulphur cluster insertion, OXPHOS complex assembly, and mitoribosome biogenesis. B14 and B22 are unique to other LYRM proteins in that they are integral components of CI. To explore the function of B22, we examined T-DNA insertional knockout and knockdown lines, which displayed a mild growth defect linked to reduced CI activity and abundance. Notably, this defect could not be rescued by complementation with a B22 variant that contained a mutated LYR domain, indicating the domain's critical role in B22's function. Protein interaction assays further revealed that the LYR domain is crucial for B22's interaction with the neighbouring CI subunit, mitochondrial acyl carrier protein SDAP1. Similarly, T-DNA insertional knockdown lines of SDAP1 showed a comparable CI defect, suggesting that the interaction between B22 and SDAP1, mediated by the LYR domain, is important for the function and assembly of CI.

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