scholarly journals Multiple protein/protein and protein/RNA interactions suggest roles for yeast DNA/RNA helicase Sen1p in transcription, transcription-coupled DNA repair and RNA processing

2004 ◽  
Vol 32 (8) ◽  
pp. 2441-2452 ◽  
Author(s):  
D. Ursic
Keyword(s):  
Dna Repair ◽  
Rna Processing ◽  
Rna Helicase ◽  
Multiple Protein

scholarly journals Exosome substrate targeting: the long and short of it

2014 ◽  
Vol 42 (4) ◽  
pp. 1129-1134 ◽  
Author(s):  
Phil Mitchell
Keyword(s):  
Rna Processing ◽  
Rna Helicase ◽  
Rrna Processing ◽  
Catalytic Subunits ◽  
The Core ◽  
Complete Destruction ◽  
Pathway Data ◽  
Complex Functions ◽  
Tramp Complex ◽  
Cytoplasmic Rnas

The exosome ribonuclease complex functions in both the limited trimming of the 3′-ends of nuclear substrates during RNA processing events and the complete destruction of nuclear and cytoplasmic RNAs. The two RNases of the eukaryotic exosome, Rrp44 (rRNA-processing protein 44) and Rrp6, are bound at either end of a catalytically inert cylindrical core. RNA substrates are threaded through the internal channel of the core to Rrp44 by RNA helicase components of the nuclear TRAMP complex (Trf4–Air2–Mtr4 polyadenylation complex) or the cytoplasmic Ski (superkiller) complex. Recent studies reveal that Rrp44 can also associate directly with substrates via channel-independent routes. Although the substrates of the exosome are known, it is not clear whether specific substrates are restricted to one or other pathway. Data currently available support the model that processed substrates are targeted directly to the catalytic subunits, whereas at least some substrates that are directed towards discard pathways must be threaded through the exosome core.

scholarly journals Systems based mapping demonstrates that recovery from alkylation damage requires DNA repair, RNA processing, and translation associated networks

Genomics ◽  
2009 ◽  
Vol 93 (1) ◽  
pp. 42-51 ◽  
Author(s):  
John P. Rooney ◽  
Ajish D. George ◽  
Ashish Patil ◽  
Ulrike Begley ◽  
Erin Bessette ◽  
...  
Keyword(s):  
Dna Repair ◽  
Rna Processing ◽  
Alkylation Damage

scholarly journals HrpA, an RNA Helicase Involved in RNA Processing, Is Required for Mouse Infectivity and Tick Transmission of the Lyme Disease Spirochete

2013 ◽  
Vol 9 (12) ◽  
pp. e1003841 ◽  
Author(s):  
Aydan Salman-Dilgimen ◽  
Pierre-Olivier Hardy ◽  
Justin D. Radolf ◽  
Melissa J. Caimano ◽  
George Chaconas
Keyword(s):  
Lyme Disease ◽  
Rna Processing ◽  
Rna Helicase ◽  
Tick Transmission

scholarly journals c-Jun Supports Ribosomal RNA Processing and Nucleolar Localization of RNA Helicase DDX21

2008 ◽  
Vol 283 (11) ◽  
pp. 7046-7053 ◽  
Author(s):  
Tim H. Holmström ◽  
Antoine Mialon ◽  
Marko Kallio ◽  
Yvonne Nymalm ◽  
Leni Mannermaa ◽  
...  
Keyword(s):  
Ribosomal Rna ◽  
Rna Processing ◽  
Rna Helicase ◽  
Nucleolar Localization ◽  
Ribosomal Rna Processing

scholarly journals Over‐Expression of RNA Processing, Heat Shock, and DNA Repair Proteins in Breast Tumor Compared to Normal Tissue

PROTEOMICS ◽  
2020 ◽  
Vol 20 (15-16) ◽  
pp. 2000044
Author(s):  
Ten‐Yang Yen ◽  
Richard Wong ◽  
Donald Pizzo ◽  
Moe Thein ◽  
Bruce A. Macher ◽  
...  
Keyword(s):  
Dna Repair ◽  
Heat Shock ◽  
Rna Processing ◽  
Breast Tumor ◽  
Normal Tissue ◽  
Over Expression ◽  
Dna Repair Proteins

scholarly journals Rrp47 and the function of the Sas10/C1D domain

2010 ◽  
Vol 38 (4) ◽  
pp. 1088-1092 ◽  
Author(s):  
Phil Mitchell
Keyword(s):  
Dna Repair ◽  
Nucleic Acid ◽  
Rna Processing ◽  
Translational Control ◽  
Specific Interactions ◽  
Amino Acid Residues ◽  
Dna Repair Mechanisms ◽  
Binding Surface ◽  
Eukaryotic Proteins ◽  
Repair Mechanisms

The Sas10/C1D domain is found in a small group of eukaryotic proteins that have functions in RNA processing events, translational control and DNA repair mechanisms. The domain is predicted to be α-helical in nature and comprises approx. 80 amino acid residues. Whereas the Sas10/C1D domain has yet to be functionally characterized, available results suggest that this domain forms a binding surface for specific interactions with other proteins and can concomitantly interact with RNA or DNA. This property of the Sas10/C1D domain may facilitate this family of proteins to dock other proteins on to nucleic acid substrates.

scholarly journals Structure and reconstitution of yeast Mpp6-nuclear exosome complexes reveals that Mpp6 stimulates RNA decay and recruits the Mtr4 helicase

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
Elizabeth V Wasmuth ◽  
John C Zinder ◽  
Dimitrios Zattas ◽  
Mom Das ◽  
Christopher D Lima
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Genetic Analysis ◽  
Central Region ◽  
Rna Processing ◽  
Rna Helicase ◽  
Rna Decay ◽  
Central Channel ◽  
Nuclear Rna ◽  
Nuclear Exosome

Nuclear RNA exosomes catalyze a range of RNA processing and decay activities that are coordinated in part by cofactors, including Mpp6, Rrp47, and the Mtr4 RNA helicase. Mpp6 interacts with the nine-subunit exosome core, while Rrp47 stabilizes the exoribonuclease Rrp6 and recruits Mtr4, but it is less clear if these cofactors work together. Using biochemistry with Saccharomyces cerevisiae proteins, we show that Rrp47 and Mpp6 stimulate exosome-mediated RNA decay, albeit with unique dependencies on elements within the nuclear exosome. Mpp6-exosomes can recruit Mtr4, while Mpp6 and Rrp47 each contribute to Mtr4-dependent RNA decay, with maximal Mtr4-dependent decay observed with both cofactors. The 3.3 Å structure of a twelve-subunit nuclear Mpp6 exosome bound to RNA shows the central region of Mpp6 bound to the exosome core, positioning its Mtr4 recruitment domain next to Rrp6 and the exosome central channel. Genetic analysis reveals interactions that are largely consistent with our model.

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