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Ppr10 and Mpa1 copurify with a subset of mitoribosomal proteins

ABSTRACT: This study aims to investigate the additional proteins assocatied with Ppr10 which function to mediate mitochondrial translation initiationin.The study performed tandem affinity purification (TAP) using extracts from strains expressing untagged Ppr10 or TAP-tagged Ppr10 under the control of its own promoter and analysis of Ppr10-copurified proteins by Mass spectrometry (MS).

INSTRUMENT(S): TOF/TOF 5800

ORGANISM(S): Schizosaccharomyces Pombe 972h-

SUBMITTER: Yirong Wang

LAB HEAD: Ying Huang

PROVIDER: PXD025862 | Pride | 2022-02-17

REPOSITORIES: Pride

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	R20171200024-F.xlt	Other
	R20171200024-S.xlt	Other
	R20171200024_spectrum_raw.zip	Other
	R20171200155_U_S.xlt	Other
	R20171200155_spectrum_raw.zip	Other

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Publications

Schizosaccharomyces pombe Ppr10 and Mpa1 together mediate mitochondrial translational initiation.

Luo Ying Y Wang Yirong Y Huang Ying Y

The Journal of biological chemistry 20210610 1

Pentatricopeptide repeat (PPR) proteins are a large family of proteins that act primarily at different posttranscriptional steps of organellar gene expression. We have previously found that the Schizosaccharomyces pombe PPR protein mpal10 interacts with mitochondrial translational activator Mpa1, and both are essential for mitochondrial protein synthesis. However, it is unclear how these two proteins function in mitochondrial protein synthesis in S. pombe. In this study, we further investigated ...[more]

PMID: 34119521

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