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The zinc finger motif in bL36m supports mitoribosome assembly and function

ABSTRACT: We have performed structure-function studies to determine the role of zinc coordinating cysteines in the mitochondrial ribosome protein bL36m.

INSTRUMENT(S): Orbitrap Exploris 480

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Antonio Barrientos

LAB HEAD: Antoni Barrientos

PROVIDER: PXD046465 | Pride | 2025-05-06

REPOSITORIES: Pride

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			Action	DRS
	20191003_HFX_YX_ZhongH_C66AC69A_5.raw	Raw
	20191003_HFX_YX_ZhongH_C82AH88A_5.raw	Raw
	20191003_HFX_YX_ZhongH_LFQ_Results-2.mzML	Mzml
	20191003_HFX_YX_ZhongH_LFQ_Results-2.mzid.gz	Mzid
	20191003_HFX_YX_ZhongH_LFQ_Results.mgf	Mgf

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1 - 5 of 26

Publications

The zinc finger motif in the mitochondrial large ribosomal subunit protein bL36m is essential for optimal yeast mitoribosome assembly and function.

Zhong Hui H Barrientos Antoni A

Biochimica et biophysica acta. Molecular cell research 20240316 4

Ribosomes across species contain subsets of zinc finger proteins that play structural roles by binding to rRNA. While the majority of these zinc fingers belong to the C2-C2 type, the large subunit protein L36 in bacteria and mitochondria exhibits an atypical C2-CH motif. To comprehend the contribution of each coordinating residue in S. cerevisiae bL36m to mitoribosome assembly and function, we engineered and characterized strains carrying single and double mutations in the zinc coordinating resi ...[more]

PMID: 38493895

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Fe-S clusters-binding proteins in mitoribosome

Project description:The human mitochondrial ribosome contains three [2Fe-2S] clusters whose assembly pathway, role, and implications for mitochondrial and metabolic diseases are unknown. Here, structure-function correlation studies show that the clusters play structural roles during mitoribosome assembly. To uncover the assembly pathway, we have examined the effect of silencing the expression of Fe-S cluster biosynthetic and delivery factors on mitoribosome stability. We have found that the mitoribosome receives its [2Fe-2S] clusters from the GLRX5-BOLA3. Additionally, the assembly of the small subunit depends on METTL17, recently reported to contain a [4Fe-4S] cluster, which we found to be inserted via ISCA1-NFU1. Consistently, fibroblasts from patients suffering from “multiple mitochondrial dysfunction” syndrome due to mutations in BOLA3 or NFU1 display previously unrecognized attenuation of mitochondrial protein synthesis that contributes to their cellular and pathophysiological phenotypes. Finally, we report that, in addition to their structural role, the mitoribosomal [2Fe-2S] clusters sense changes in the redox environment. In this way, the mitoribosome checks the availability and stability of mitochondrial Fe-S clusters to regulate organellar protein synthesis accordingly.

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