Nuclear tau and its potential role in Alzheimer’s disease [PDF]
, 2016 Tau protein, found in both neuronal and non-neuronal cells, forms aggregates in neurons that constitutes one of the hallmarks of Alzheimer’s disease (AD).
Al-Hilaly, Youssra +2 more
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Strategy for the identification of micro-organisms producing food and feed products : bacteria producing food enzymes as study case [PDF]
, 2020 Recent European regulations require safety assessments of food enzymes (FE) before their commercialization. FE are mainly produced by micro-organisms, whose viable strains nor associated DNA can be present in the final products.
De Keersmaecker, Sigrid C. J. +8 more
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NOP3 is an essential yeast protein which is required for pre-rRNA processing. [PDF]
The Journal of cell biology, 1992 The four nucleolar proteins NOP1, SSB1, GAR1, and NSR1 of Saccharomyces cerevisiae share a repetitive domain composed of repeat units rich in glycine and arginine (GAR domain). We have cloned and sequenced a fifth member of this family, NOP3, and shown it to be essential for cell viability.
Russell, I. D., Tollervey, D.
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Saccharomyces cerevisiae ribosomal protein L26 is not essential for ribosome assembly and function [PDF]
, 2012 Ribosomal proteins play important roles in ribosome biogenesis and function. Here, we study the evolutionarily conserved L26 inSaccharomyces cerevisiae, which assembles into pre-60S ribosomal particles in the nucle(ol)us.
Babiano González, Reyes +3 more
core +1 more source
Regulatory Aspects of rRNA Modification and Pre-rRNA Processing
, 2014 The major types of posttranscriptional modification are the isomerization of uracil to pseudouridine, 2′-O-methylation of the ribose moieties and base methylation. In addition to their roles in pre-rRNA modification, both Dim1p and Cbf5p are required for pre-rRNA processing, and Pet56p is required for synthesis of mitochondrial large ribosomal subunits.
Lafontaine, Denis, Tollervey, D
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mTOR signaling regulates the processing of pre-rRNA in human cells
Nucleic Acids Research, 2011 Signaling through the mammalian target of rapamycin, complex 1 (mTORC1), positively regulates the transcription of ribosomal RNA (rRNA) and the synthesis of ribosomal proteins, thereby promoting the complex process of ribosome biogenesis. The major rRNAs are transcribed as a single precursor, which must be processed to create the 5.8S, 18S and 28S ...
Iadevaia, Valentina +3 more
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The structure of the ITS2-proximal stem is required for pre-rRNA processing in yeast [PDF]
RNA, 1998 Accurate and efficient processing of pre-rRNA is critical to the accumulation of mature functional ribosomal subunits for maintenance of cell growth. Processing requires numerous factors which act in trans as well as RNA sequence/ structural elements which function in cis.
B A, Peculis, C L, Greer
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Characterization of nuclear polyadenylated RNA-binding proteins in Saccharomyces cerevisiae. [PDF]
, 1994 To study the functions of heterogeneous nuclear ribonucleoproteins (hnRNPs), we have characterized nuclear polyadenylated RNA-binding (Nab) proteins from Saccharomyces cerevisiae.
Datar, KV +4 more
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The NIP7 protein is required for accurate pre-rRNA processing in human cells [PDF]
Nucleic Acids Research, 2010 Eukaryotic ribosome biogenesis requires the function of a large number of trans-acting factors which interact transiently with the nascent pre-rRNA and dissociate as the ribosomal subunits proceed to maturation and export to the cytoplasm. Loss-of-function mutations in human trans-acting factors or ribosome components may lead to genetic syndromes.
Luis G. Morello +5 more
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Slx9p facilitates efficient ITS1 processing of pre-rRNA in Saccharomyces cerevisiae [PDF]
RNA, 2006 Slx9p (Ygr081cp) is a nonessential yeast protein previously linked genetically with the DNA helicase Sgs1p. Here we report that Slx9p is involved in ribosome biogenesis in the yeast Saccharomyces cerevisiae. Deletion of SLX9 results in a mild growth defect and a reduction in the level of 18S rRNA. Co-immunoprecipitation experiments showed that Slx9p is
Bax, R., Raue, H.A., Vos, J.C.
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