scholarly journals A nuclear function for RNase MRP.

1994 ◽  
Vol 91 (11) ◽  
pp. 4615-4617 ◽  
Author(s):  
D. A. Clayton
Keyword(s):  
Nuclear Function ◽  
Rnase Mrp

scholarly journals The enigmatic RNase MRP of kinetoplastids

RNA Biology ◽  
2021 ◽  
pp. 1-9
Author(s):  
Magnus Alm Rosenblad ◽  
Marcela Dávila López ◽  
Tore Samuelsson
Keyword(s):  
Rnase Mrp

scholarly journals Nuclear cGAS: sequestration and beyond

2021 ◽  
Author(s):  
Juli Bai ◽  
Feng Liu
Keyword(s):  
Innate Immune ◽  
Complex Nature ◽  
Type I ◽  
Replication Forks ◽  
The Novel ◽  
Nuclear Function ◽  
Double Stranded Dna ◽  
Open Questions ◽  
Established Role ◽  
Dependent Signaling Pathway

AbstractThe cyclic GMP-AMP (cGAMP) synthase (cGAS) has been identified as a cytosolic double stranded DNA sensor that plays a pivotal role in the type I interferon and inflammation responses via the STING-dependent signaling pathway. In the past several years, a growing body of evidence has revealed that cGAS is also localized in the nucleus where it is associated with distinct nuclear substructures such as nucleosomes, DNA replication forks, the double-stranded breaks, and centromeres, suggesting that cGAS may have other functions in addition to its role in DNA sensing. However, while the innate immune function of cGAS is well established, the non-canonical nuclear function of cGAS remains poorly understood. Here, we review our current understanding of the complex nature of nuclear cGAS and point to open questions on the novel roles and the mechanisms of action of this protein as a key regulator of cell nuclear function, beyond its well-established role in dsDNA sensing and innate immune response.

scholarly journals Insights into a novel nuclear function for Fascin in the regulation of the amino-acid transporter SLC3A2

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Amine Saad ◽  
Krikor Bijian ◽  
Dinghong Qiu ◽  
Sabrina Daniela da Silva ◽  
Maud Marques ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Transporter ◽  
Nuclear Function ◽  
Acid Transporter

scholarly journals Saccharomyces cerevisiae contains an RNase MRP that cleaves at a conserved mitochondrial RNA sequence implicated in replication priming.

1992 ◽  
Vol 12 (6) ◽  
pp. 2561-2569 ◽  
Author(s):  
L L Stohl ◽  
D A Clayton
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Mitochondrial Dna ◽  
Dna Replication ◽  
Rna Processing ◽  
Mitochondrial Rna ◽  
Rna Sequence ◽  
Rnase Mrp ◽  
Processing Activity ◽  
Yeast Mitochondrial Dna ◽  
Human And Mouse

Yeast mitochondrial DNA contains multiple promoters that sponsor different levels of transcription. Several promoters are individually located immediately adjacent to presumed origins of replication and have been suggested to play a role in priming of DNA replication. Although yeast mitochondrial DNA replication origins have not been extensively characterized at the primary sequence level, a common feature of these putative origins is the occurrence of a short guanosine-rich region in the priming strand downstream of the transcriptional start site. This situation is reminiscent of vertebrate mitochondrial DNA origins and raises the possibility of common features of origin function. In the case of human and mouse cells, there exists an RNA processing activity with the capacity to cleave at a guanosine-rich mitochondrial RNA sequence at an origin; we therefore sought the existence of a yeast endoribonuclease that had such a specificity. Whole cell and mitochondrial extracts of Saccharomyces cerevisiae contain an RNase that cleaves yeast mitochondrial RNA in a site-specific manner similar to that of the human and mouse RNA processing activity RNase MRP. The exact location of cleavage within yeast mitochondrial RNA corresponds to a mapped site of transition from RNA to DNA synthesis. The yeast activity also cleaved mammalian mitochondrial RNA in a fashion similar to that of the mammalian RNase MRPs. The yeast endonuclease is a ribonucleoprotein, as judged by its sensitivity to nucleases and proteinase, and it was present in yeast strains lacking mitochondrial DNA, which demonstrated that all components required for in vitro cleavage are encoded by nuclear genes. We conclude that this RNase is the yeast RNase MRP.

Transcription-dependent nucleolar cap localization and possible nuclear function of DExH RNA helicase RHAU

2008 ◽  
Vol 314 (6) ◽  
pp. 1378-1391 ◽  
Author(s):  
Fumiko Iwamoto ◽  
Michael Stadler ◽  
Kateřina Chalupníková ◽  
Edward Oakeley ◽  
Yoshikuni Nagamine
Keyword(s):  
Rna Helicase ◽  
Nuclear Function

scholarly journals Partially Processed pre-rRNA Is Preserved in Association with Processing Components in Nucleolus-derived Foci during Mitosis

1998 ◽  
Vol 9 (9) ◽  
pp. 2407-2422 ◽  
Author(s):  
Miroslav Dundr ◽  
Mark O.J. Olson
Keyword(s):  
Molecular Weight ◽  
Internal Transcribed Spacer ◽  
Rnase P ◽  
Rrna Processing ◽  
Rnase Mrp ◽  
External Transcribed Spacer ◽  
Early Anaphase ◽  
Late Telophase ◽  
Processing Site

Previous studies showed that components implicated in pre-rRNA processing, including U3 small nucleolar (sno)RNA, fibrillarin, nucleolin, and proteins B23 and p52, accumulate in perichromosomal regions and in numerous mitotic cytoplasmic particles, termed nucleolus-derived foci (NDF) between early anaphase and late telophase. The latter structures were analyzed for the presence of pre-rRNA by fluorescence in situ hybridization using probes for segments of pre-rRNA with known half-lives. The NDF did not contain the short-lived 5′-external transcribed spacer (ETS) leader segment upstream from the primary processing site in 47S pre-rRNA. However, the NDF contained sequences from the 5′-ETS core, 18S, internal transcribed spacer 1 (ITS1), and 28S segments and also had detectable, but significantly reduced, levels of the 3′-ETS sequence. Northern analyses showed that in mitotic cells, the latter sequences were present predominantly in 45S-46S pre-rRNAs, indicating that high-molecular weight processing intermediates are preserved during mitosis. Two additional essential processing components were also found in the NDF: U8 snoRNA and hPop1 (a protein component of RNase MRP and RNase P). Thus, the NDF appear to be large complexes containing partially processed pre-rRNA associated with processing components in which processing has been significantly suppressed. The NDF may facilitate coordinated assembly of postmitotic nucleoli.

scholarly journals A Novel Model for the RNase MRP-Induced Switch Between Different Forms of 5.8S rRNA

2021 ◽  
Author(s):  
Xiao Li ◽  
Janice M Zengel ◽  
Lasse Lindahl
Keyword(s):  
Rna Polymerase ◽  
18S Rrna ◽  
Rna Polymerase I ◽  
Published Data ◽  
Primary Transcript ◽  
Rna Molecules ◽  
Rnase Mrp ◽  
5.8S Rrna ◽  
Polymerase I ◽  
Novel Model

Processing of the RNA polymerase I pre-rRNA transcript into the mature 18S, 5.8S, and 25S rRNAs requires removing the “spacer” sequences. The canonical pathway for the removal of the ITS1 spacer, located between 18S and 5.8S rRNAs in the primary transcript, involves cleavages at the 3’ end of 18S rRNA and at two sites inside ITS1. The process generates a long and a short 5.8S rRNA that differ in the number of ITS1 nucleotides retained at the 5.8S 5’ end. Here we document a novel pathway that generates the long 5.8S for ITS1 while bypassing cleavage within ITS1. It entails a single endonuclease cut at the 3’-end of 18S rRNA followed by exonuclease Xrn1 degradation of ITS1. Mutations in RNase MRP increase the accumulation of long relative to short 5.8S rRNA; traditionally this is attributed to a decreased rate of RNase MRP cleavage at its target in ITS1, called A3. In contrast, we report here that the MRP induced switch between long and short 5.8S rRNA formation occurs even when the A3 site is deleted. Based on this and our published data, we propose that the switch may depend on RNase MRP processing RNA molecules other than pre-rRNA.

Sign in / Sign up

Export Citation Format

Share Document