Human diseases of the SSU processome

Sondalle, Samuel B.; Baserga, Susan J.

doi:10.1016/j.bbadis.2013.11.004

Cited by 39 publications

(44 citation statements)

References 57 publications

(102 reference statements)

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“…Cell Lines and Growth Conditions-HeLa and HEK293 cells were grown in DMEM supplemented with 10% FBS, at 37°C under a humidified atmosphere containing 5% CO 2 .…”

Section: Methodsmentioning

confidence: 99%

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Human NAT10 Is an ATP-dependent RNA Acetyltransferase Responsible for N4-Acetylcytidine Formation in 18 S Ribosomal RNA (rRNA)

Ito

Horikawa

Suzuki

et al. 2014

Journal of Biological Chemistry

187

210

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Background: Post-transcriptional modifications of rRNAs play important roles in biogenesis and function of ribosome. Results: NAT10 is an ATP-dependent RNA acetyltransferase responsible for N 4 -acetylcytidine formation of 18 S rRNA. Conclusion: NAT10 and ac 4 C1842 are required for pre-18 S rRNA processing. Significance: 40 S subunit formation is regulated by a single acetylation of 18 S rRNA, implying a regulatory mechanism for ribosome biogenesis by sensing the cellular energy budget.

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“…Cell Lines and Growth Conditions-HeLa and HEK293 cells were grown in DMEM supplemented with 10% FBS, at 37°C under a humidified atmosphere containing 5% CO 2 .…”

Section: Methodsmentioning

confidence: 99%

“…2E) (1). More than 200 factors and small nucleolar RNAs are involved in ribosome assembly, and mutations in these assembly factors often result in pathological consequence (2,3). During rRNA processing, rRNAs are modified post-transcriptionally; these modifications are involved in fine-tuning translational fidelity and/or modulating ribosome biogenesis (4).…”

mentioning

confidence: 99%

Human NAT10 Is an ATP-dependent RNA Acetyltransferase Responsible for N4-Acetylcytidine Formation in 18 S Ribosomal RNA (rRNA)

Ito

Horikawa

Suzuki

et al. 2014

Journal of Biological Chemistry

187

210

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show abstract

“…While it was long assumed that any defect in this fundamental process would be incompatible with life, mutations affecting ribosome production have now been identified in several human congenital disorders (ribosomopathies) and in animal models [3–15]. Despite all arising from abnormalities in the ubiquitous process of ribosome biogenesis, these diseases exhibit unexpectedly unique phenotypes (Table 1) [1, 16–18]. The reason for this tissue proclivity remains mysterious but its existence hints at a fundamental cell type specificity in ribosome biology during development.…”

Section: Introductionmentioning

confidence: 99%

Expression of ribosomopathy genes during Xenopus tropicalis embryogenesis

et al. 2016

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BackgroundBecause ribosomes are ubiquitously required for protein production, it was long assumed that any inherited defect in ribosome manufacture would be embryonically lethal. However, several human congenital diseases have been found to be associated with mutations in ribosome biogenesis factors. Surprisingly, despite the global requirement for ribosomes, these “ribosomopathies” are characterized by distinct and tissue specific phenotypes. The reasons for such tissue proclivity in ribosomopathies remain mysterious but may include differential expression of ribosome biogenesis factors in distinct tissues.MethodsHere we use in situ hybridization of labeled antisense mRNA probes and ultra high temporal resolution RNA-Seq data to examine and compare expression of 13 disease associated ribosome biogenesis factors at six key stages in Xenopus tropicalis development.ResultsRather than being ubiquitously expressed during development, mRNAs of all examined ribosome biogenesis factors were highly enriched in specific tissues, including the cranial neural crest and ventral blood islands. Interestingly, expression of ribosome biogenesis factors demonstrates clear differences in timing, transcript number and tissue localization.ConclusionRibosome biogenesis factor expression is more spatiotemporally regulated during embryonic development than previously expected and correlates closely with many of the common ribosomopathy phenotypes. Our findings provide information on the dynamic use of ribosome production machinery components during development and advance our understanding of their roles in disease.Electronic supplementary materialThe online version of this article (doi:10.1186/s12861-016-0138-5) contains supplementary material, which is available to authorized users.

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“…The production of ribosomes has been suggested to be a sequential series of quality control steps that block and recycle nonoptimally assembled preribosomes. Defects in the ribosome assembly pathway have been identified in a number of inherited hematopoietic disorders, collectively called ribosomopathies, which have been linked to progression into cancer (Armistead et al 2009;Narla and Ebert 2011;Sondalle and Baserga 2014).…”

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confidence: 99%

Chaperoning 5S RNA assembly

Madru¹,

Lebaron²,

Blaud³

et al. 2015

Genes Dev.

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In eukaryotes, three of the four ribosomal RNAs (rRNAs)-the 5.8S, 18S, and 25S/28S rRNAs-are processed from a single pre-rRNA transcript and assembled into ribosomes. The fourth rRNA, the 5S rRNA, is transcribed by RNA polymerase III and is assembled into the 5S ribonucleoprotein particle (RNP), containing ribosomal proteins Rpl5/ uL18 and Rpl11/uL5, prior to its incorporation into preribosomes. In mammals, the 5S RNP is also a central regulator of the homeostasis of the tumor suppressor p53. The nucleolar localization of the 5S RNP and its assembly into preribosomes are performed by a specialized complex composed of Rpf2 and Rrs1 in yeast or Bxdc1 and hRrs1 in humans. Here we report the structural and functional characterization of the Rpf2-Rrs1 complex alone, in complex with the 5S RNA, and within pre-60S ribosomes. We show that the Rpf2-Rrs1 complex contains a specialized 5S RNA E-loop-binding module, contacts the Rpl5 protein, and also contacts the ribosome assembly factor Rsa4 and the 25S RNA. We propose that the Rpf2-Rrs1 complex establishes a network of interactions that guide the incorporation of the 5S RNP in preribosomes in the initial conformation prior to its rotation to form the central protuberance found in the mature large ribosomal subunit.

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Human diseases of the SSU processome

Cited by 39 publications

References 57 publications

Human NAT10 Is an ATP-dependent RNA Acetyltransferase Responsible for N4-Acetylcytidine Formation in 18 S Ribosomal RNA (rRNA)

Human NAT10 Is an ATP-dependent RNA Acetyltransferase Responsible for N4-Acetylcytidine Formation in 18 S Ribosomal RNA (rRNA)

Expression of ribosomopathy genes during Xenopus tropicalis embryogenesis

Chaperoning 5S RNA assembly

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