LRPPRC and SLIRP Interact in a Ribonucleoprotein Complex That Regulates Posttranscriptional Gene Expression in Mitochondria

Sasarman, Florin; Brunel‐Guitton, Catherine; Antonická, Hana; Wai, Timothy; Shoubridge, Eric A.

doi:10.1091/mbc.e10-01-0047

Cited by 237 publications

(316 citation statements)

References 25 publications

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“…LRPPRC (leucine-rich pentatricopeptide repeat containing) is a RBP that associates with both nuclear and mitochondrial mRNAs (Mili and Piñol-Roma 2003). Some evidence implicates LRPPRC in nuclear mRNA export, while mitochondrial LRPPRC controls RNA processing and translation (Sasarman et al 2010;Chujo et al 2012). Thus, LRPPRC could be involved in rRNP export from the nucleus, akin to what has been described for mRNA export.…”

Section: Identification Of Previously Unrecognized Ribosomal Rbpsmentioning

confidence: 99%

Specific RNP capture with antisense LNA/DNA mixmers

Rogell

Fischer

Rettel

et al. 2017

RNA

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RNA-binding proteins (RBPs) play essential roles in RNA biology, responding to cellular and environmental stimuli to regulate gene expression. Important advances have helped to determine the (near) complete repertoires of cellular RBPs. However, identification of RBPs associated with specific transcripts remains a challenge. Here, we describe "specific ribonucleoprotein (RNP) capture," a versatile method for the determination of the proteins bound to specific transcripts in vitro and in cellular systems. Specific RNP capture uses UV irradiation to covalently stabilize protein-RNA interactions taking place at "zero distance." Proteins bound to the target RNA are captured by hybridization with antisense locked nucleic acid (LNA)/DNA oligonucleotides covalently coupled to a magnetic resin. After stringent washing, interacting proteins are identified by quantitative mass spectrometry. Applied to in vitro extracts, specific RNP capture identifies the RBPs bound to a reporter mRNA containing the Sex-lethal (Sxl) binding motifs, revealing that the Sxl homolog sister of Sex lethal (Ssx) displays similar binding preferences. This method also revealed the repertoire of RBPs binding to 18S or 28S rRNAs in HeLa cells, including previously unknown rRNA-binding proteins.

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Section: Identification Of Previously Unrecognized Ribosomal Rbpsmentioning

confidence: 99%

Specific RNP capture with antisense LNA/DNA mixmers

Rogell

Fischer

Rettel

et al. 2017

RNA

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show abstract

“…44 The mammalian mitochondrial PPR protein, LRPPRC, which is important for polyadenylation and translation, forms an intimate complex with another RNA-binding protein, SLIRP, such that each protein requires the other for their stability. [69][70][71] Importantly, the editing PPR proteins of Arabidopsis must associate with multiple organelle RNA editing factor (MORF) family proteins or, in some cases, an autonomous DYW domain protein, DYW1, to deaminate their target RNA bases. [72][73][74][75] To date, a complete description of the proteins required for RNA editing has not been elucidated.…”

Section: Future Directions: Understanding and Engineering Ppr Proteinsmentioning

confidence: 99%

Pentatricopeptide repeats

Filipovska

Rackham

2013

RNA Biology

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“…24 SLIRP is part of a ribonucleoprotein complex that regulates posttranscriptional gene expression in mitochondria. 29 In this contest, SLIRP interacts with LRPPRC and knockdown of either SLIRP 24 or LRPPRC 25 results in similar decreases in mitochondrial mRNA levels, indicating that the LRPPRC/SLIRP complex has a specific role in mRNA maturation or stabilization after transcription in mitochondria. In particular, it was demonstrated that the LRPPRC/SLIRP complex suppresses the mRNA degradation and promotes polyadenylation in human mitochondria.…”

Section: Discussionmentioning

confidence: 76%