Expression Regulation, Protein Chemistry and Functional Biology of the Guanine-Rich Sequence Binding Factor 1 (GRSF1)

Dumoulin, Bernhard; Ufer, Christoph; Kühn, Hartmut; Sofi, Sajad

doi:10.1016/j.jmb.2021.166922

Cited by 12 publications

(10 citation statements)

References 122 publications

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“…As a similar difference between mouse and human, it is interesting to note that the ClpP-null MEFs showed a massive induction of the innate immune defense against toxic DNA/RNA, while the patient fibroblasts did not show such immunostimulation. GRSF1 has a physiological presence in the nucleus, as with other members of the hnRNP F/H family [ 72 ], but its function there is not clear. GRSF1 abundance is physiologically controlled by DAZL [ 73 ], the master translational regulator of spermatogenesis [ 74 , 75 ].…”

Section: Discussionmentioning

confidence: 99%

Inactivity of Peptidase ClpP Causes Primary Accumulation of Mitochondrial Disaggregase ClpX with Its Interacting Nucleoid Proteins, and of mtDNA

Key

Torres-Odio

Bach

et al. 2021

Cells

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Biallelic pathogenic variants in CLPP, encoding mitochondrial matrix peptidase ClpP, cause a rare autosomal recessive condition, Perrault syndrome type 3 (PRLTS3). It is characterized by primary ovarian insufficiency and early sensorineural hearing loss, often associated with progressive neurological deficits. Mouse models showed that accumulations of (i) its main protein interactor, the substrate-selecting AAA+ ATPase ClpX, (ii) mitoribosomes, and (iii) mtDNA nucleoids are the main cellular consequences of ClpP absence. However, the sequence of these events and their validity in human remain unclear. Here, we studied global proteome profiles to define ClpP substrates among mitochondrial ClpX interactors, which accumulated consistently in ClpP-null mouse embryonal fibroblasts and brains. Validation work included novel ClpP-mutant patient fibroblast proteomics. ClpX co-accumulated in mitochondria with the nucleoid component POLDIP2, the mitochondrial poly(A) mRNA granule element LRPPRC, and tRNA processing factor GFM1 (in mouse, also GRSF1). Only in mouse did accumulated ClpX, GFM1, and GRSF1 appear in nuclear fractions. Mitoribosomal accumulation was minor. Consistent accumulations in murine and human fibroblasts also affected multimerizing factors not known as ClpX interactors, namely, OAT, ASS1, ACADVL, STOM, PRDX3, PC, MUT, ALDH2, PMPCB, UQCRC2, and ACADSB, but the impact on downstream metabolites was marginal. Our data demonstrate the primary impact of ClpXP on the assembly of proteins with nucleic acids and show nucleoid enlargement in human as a key consequence.

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Section: Discussionmentioning

confidence: 99%

Inactivity of Peptidase ClpP Causes Primary Accumulation of Mitochondrial Disaggregase ClpX with Its Interacting Nucleoid Proteins, and of mtDNA

Key

Torres-Odio

Bach

et al. 2021

Cells

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“…IAV is known to utilize several cellular RNA-binding proteins (RBPs) during its life cycle for various functions such as splicing, replication, and selective translation of viral mRNAs 26 – 28 . Among these RBPs is GRSF1, a member of the heterogeneous nuclear ribonucleoprotein (hnRNP) family 29 . GRSF1 has been shown to directly bind the sequence 10 AGGGU 14 in the 5' UTR of IAV NP and NS mRNAs to enhance their translation efficiency 30 – 32 .…”

Section: Introductionmentioning

confidence: 99%

Host adaptive mutations in the 2009 H1N1 pandemic influenza A virus PA gene regulate translation efficiency of viral mRNAs via GRSF1

2022

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Avian species are the major natural reservoir from which pandemic influenza A viruses can be introduced to humans. Avian influenza A virus genes, including the three viral polymerase genes, PA, PB1 and PB2, require host-adaptive mutations to allow for viral replication and transmission in humans. Previously, PA from the 2009 pH1N1 viral polymerase was found to harbor host-adaptive mutations leading to enhanced viral polymerase activity. By quantifying translation and mRNA transcription, we found that the 2009 pH1N1 PA, and the associated host-adaptive mutations, led to greater translation efficiency. This was due to enhanced cytosolic accumulation of viral mRNA, which was dependent on the host RNA binding protein GRSF1. Mutations to the GRSF1 binding site in viral mRNA, as well as GRSF1 knockdown, reduced cytosolic accumulation and translation efficiency of viral mRNAs. This study identifies a previously unrecognized mechanism by which host-adaptive mutations in PA regulate viral replication and host adaptation. Importantly, these results provide greater insight into the host adaptation process of IAVs and reveal the importance of GRSF1 in the lifecycle of IAV.

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“…[52][53][54] However, all of these studies have been performed through in vitro or ex vivo approaches due to the lack of GRSF1 transgenic mice. 55 In this study, RNA pull-down assay and protein MS were used to find the interaction proteins with lnccytb in mitochondria and cytosol. Western blotting and knockdown assay also indicated that GRSF1 could export lnccytb from mitochondria to cytosol.…”

Section: Discussionmentioning

confidence: 99%

Overexpression of cytosolic long noncoding RNA cytb protects against pressure-overload-induced heart failure via sponging microRNA-103-3p

Zhang

Yuan

Liu

et al. 2022

Molecular Therapy - Nucleic Acids

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Expression Regulation, Protein Chemistry and Functional Biology of the Guanine-Rich Sequence Binding Factor 1 (GRSF1)

Cited by 12 publications

References 122 publications

Inactivity of Peptidase ClpP Causes Primary Accumulation of Mitochondrial Disaggregase ClpX with Its Interacting Nucleoid Proteins, and of mtDNA

Inactivity of Peptidase ClpP Causes Primary Accumulation of Mitochondrial Disaggregase ClpX with Its Interacting Nucleoid Proteins, and of mtDNA

Host adaptive mutations in the 2009 H1N1 pandemic influenza A virus PA gene regulate translation efficiency of viral mRNAs via GRSF1

Overexpression of cytosolic long noncoding RNA cytb protects against pressure-overload-induced heart failure via sponging microRNA-103-3p

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