scholarly journals Sirtuin 7 promotes 45S pre-rRNA cleavage at site 2 and determines the processing pathway

2019 ◽  
Vol 132 (17) ◽  
pp. jcs228601 ◽  
Author(s):  
Valentina Sirri ◽  
Alice Grob ◽  
Jérémy Berthelet ◽  
Nathalie Jourdan ◽  
Pascal Roussel
Keyword(s):  
Rrna Cleavage

Multiple apoptotic death types triggered through activation of separate pathways by cAMP and inhibitors of protein phosphatases in one (IPC leukemia) cell line

1994 ◽  
Vol 107 (12) ◽  
pp. 3363-3377 ◽  
Author(s):  
B.T. Gjertsen ◽  
L.I. Cressey ◽  
S. Ruchaud ◽  
G. Houge ◽  
M. Lanotte ◽  
...  
Keyword(s):  
Okadaic Acid ◽  
Leukemia Cell ◽  
S Phase ◽  
Leukemia Cell Line ◽  
Calyculin A ◽  
The Novel ◽  
Phosphatase Inhibitors ◽  
Apoptotic Death ◽  
Protein Phosphatase Inhibitors ◽  
Rrna Cleavage

The protein phosphatase inhibitors okadaic acid and calyculin A at moderate concentrations induced three types of apoptotic promyelocytic leukemia cell death, distinct with respect to ultrastructure and polynucleotide fragmentation. Calyculin A at higher concentrations (> 50 nM) induced a non-apoptotic death type with high ATP and pronounced micromitochondriosis. This suggests that protein phosphorylation pathways are involved in the triggering of several death pathways. Activation of the cAMP kinase induced yet another apoptotic death type, preferentially affecting cells in S-phase. In fact, cAMP acted in two ways to stop IPC promyelocyte proliferation: (1) block in late G1 (preventing new cells from entering DNA replication); and (2) induction of apoptosis in S-phase. cAMP and phosphatase inhibitors acted via distinct pathways. The inhibitors suppressed cAMP-induced death, but only at concentrations high enough to commit the cells to alternative, less conspicuous death types. The tumor-promoting activity of okadaic acid and calyculin A may therefore not be by protection against apoptosis. DNA fragmentation correlated with the novel feature of limited 28 S rRNA cleavage, suggesting co-ordinated polynucleotide cleavage, possibly directed against illegitimate polynucleotides, in some apoptotic death types.

3.2-Å-resolution structure of the 90S preribosome before A1 pre-rRNA cleavage

2017 ◽  
Vol 24 (11) ◽  
pp. 954-964 ◽  
Author(s):  
Jingdong Cheng ◽  
Nikola Kellner ◽  
Otto Berninghausen ◽  
Ed Hurt ◽  
Roland Beckmann
Keyword(s):  
Rrna Cleavage ◽  
Resolution Structure

scholarly journals Quantitative detection of culturable methanogenic archaea abundance in anaerobic treatment systems using the sequence-specific rRNA cleavage method

2009 ◽  
Vol 3 (5) ◽  
pp. 522-535 ◽  
Author(s):  
Takashi Narihiro ◽  
Takeshi Terada ◽  
Akiko Ohashi ◽  
Jer-Horng Wu ◽  
Wen-Tso Liu ◽  
...  
Keyword(s):  
Methanogenic Archaea ◽  
Anaerobic Treatment ◽  
Quantitative Detection ◽  
Rrna Cleavage ◽  
Cleavage Method

scholarly journals Dhr1p, a Putative DEAH-Box RNA Helicase, Is Associated with the Box C+D snoRNP U3

2000 ◽  
Vol 20 (19) ◽  
pp. 7238-7246 ◽  
Author(s):  
Alan Colley ◽  
Jean D. Beggs ◽  
David Tollervey ◽  
Denis L. J. Lafontaine
Keyword(s):  
18S Rrna ◽  
Mrna Splicing ◽  
Rrna Synthesis ◽  
Detectable Effect ◽  
Rna Helicases ◽  
Structural Reorganization ◽  
Rrna Cleavage ◽  
Processing Steps

ABSTRACT Putative RNA helicases are involved in most aspects of gene expression. All previously characterized members of the DEAH-box family of putative RNA helicases are involved in pre-mRNA splicing. Here we report the analysis of two novel DEAH-box RNA helicases, Dhr1p and Dhr2p, that were found to be predominantly nucleolar. Both genes are essential for viability, and MET-regulated alleles were therefore created. Depletion of Dhr1p or Dhr2p had no detectable effect on pre-mRNA splicing in vivo or in vitro. Both Dhr1p and Dhr2p were, however, required for 18S rRNA synthesis. Depletion of Dhr2p inhibited pre-rRNA cleavage at sites A0, A1, and A2, while Dhr1p depletion inhibited cleavage at sites A1 and A2. No coprecipitation of snoRNAs was detected with ProtA-Dhr2p, but Dhr1p-ProtA was stably associated with the U3 snoRNA. Depletion of Dhr1p inhibited processing steps that require base pairing of U3 to the 5′ end of the 18S rRNA. We speculate that Dhr1p is targeted to the preribosomal particles by the U3-18S rRNA interaction and is required for the structural reorganization of the rRNA during formation of the central pseudoknot.

scholarly journals The complete structure of the small subunit processome

2017 ◽  
Author(s):  
Jonas Barandun ◽  
Malik Chaker-Margot ◽  
Mirjam Hunziker ◽  
Kelly R. Molloy ◽  
Brian T. Chait ◽  
...  
Keyword(s):  
Ribosomal Proteins ◽  
18S Rrna ◽  
Molecular Mimicry ◽  
Ribosomal Subunit ◽  
Small Subunit ◽  
Ribosome Assembly ◽  
Complete Structure ◽  
Small Ribosomal Subunit ◽  
Rna Remodeling ◽  
Rrna Cleavage

The small subunit processome represents the earliest stable precursor of the eukaryotic small ribosomal subunit. Here we present the cryo-EM structure of the Saccharomyces cerevisiae small subunit processome at an overall resolution of 3.8 Å, which provides an essentially complete atomic model of this assembly. In this nucleolar superstructure, 51 ribosome assembly factors and two RNAs encapsulate the 18S rRNA precursor and 15 ribosomal proteins in a state that precedes pre-rRNA cleavage at site A1. Extended flexible proteins are employed to connect distant sites in this particle. Molecular mimicry, steric hindrance as well as protein-and RNA-mediated RNA remodeling are used in a concerted fashion to prevent the premature formation of the central pseudoknot and its surrounding elements within the small ribosomal subunit.

scholarly journals Cloning of a gene involved in rRNA precursor processing and 23S rRNA cleavage in Rhodobacter capsulatus.

1994 ◽  
Vol 176 (4) ◽  
pp. 1121-1127 ◽  
Author(s):  
E Kordes ◽  
S Jock ◽  
J Fritsch ◽  
F Bosch ◽  
G Klug
Keyword(s):  
Rhodobacter Capsulatus ◽  
23S Rrna ◽  
Precursor Processing ◽  
Rrna Cleavage

Sequence-specific cleavage of 16S rRNA for rapid and quantitative detection of particular groups of anaerobes in bioreactors

2005 ◽  
Vol 52 (1-2) ◽  
pp. 107-113 ◽  
Author(s):  
Y. Sekiguchi ◽  
Y. Uyeno ◽  
A. Sunaga ◽  
H. Yoshida ◽  
Y. Kamagata
Keyword(s):  
16S Rrna ◽  
Rnase H ◽  
Quantitative Detection ◽  
Specific Group ◽  
Simple Method ◽  
Experimental Procedure ◽  
Anaerobic Microorganisms ◽  
Complex Microbial Community ◽  
Rrna Cleavage ◽  
Digested Sewage Sludge

We developed a rapid and simple method for rRNA-based quantitative detection of a specific group of microorganisms in complex ecosystems. The method relies on the sequence-specific scission of 16S rRNA with ribonuclease H (RNase H) and oligonucleotides that specifically hybridize with targeted rRNA molecules. RNAs from a complex community were first mixed with an oligonucleotide and were subsequently digested with RNase H to achieve sequence-dependent rRNA cleavage at the hybridization site. For the quantitative detection of targeted rRNAs, the resulting RNA fragment patterns were analyzed by gel-electrophoresis, which separated and quantified cleaved and intact rRNA fragments. This method enabled the quantitative detection of microbes in a complex microbial community by a relatively simple and fast experimental procedure. We then applied the cleavage method to actual anaerobic microbial communities such as digested sewage sludge and UASB sludges. The results demonstrated that the present method was fully applicable to anaerobic digestor ecosystems containing complex anaerobic microorganisms.

scholarly journals Crosslinking-MS analysis reveals RNA polymerase I domain architecture and basis of rRNA cleavage

2012 ◽  
Vol 40 (12) ◽  
pp. 5591-5601 ◽  
Author(s):  
Stefan Jennebach ◽  
Franz Herzog ◽  
Ruedi Aebersold ◽  
Patrick Cramer
Keyword(s):  
Rna Polymerase ◽  
Domain Architecture ◽  
Rna Polymerase I ◽  
Ms Analysis ◽  
Rrna Cleavage ◽  
Polymerase I

scholarly journals An RNA Conformational Switch Regulates Pre-18S rRNA Cleavage

2011 ◽  
Vol 405 (1) ◽  
pp. 3-17 ◽  
Author(s):  
Allison C. Lamanna ◽  
Katrin Karbstein
Keyword(s):  
18S Rrna ◽  
Conformational Switch ◽  
Rrna Cleavage
Sign in / Sign up

Export Citation Format

Share Document