Large-scale organization of ribosomal DNA chromatin is regulated by Tip5

Zillner, Karina; Filarsky, Michael; Rachow, Katrin; Weinberger, Michael; Längst, Gernot; Németh, Attila

doi:10.1093/nar/gkt218

Cited by 29 publications

(37 citation statements)

References 47 publications

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“…5). Similarly, Zillner et al [72] investigated the binding event for specific peptides known as (AT-hook) of Tip5 protein (major regulatory subunit in nucleolar remodeling complex) with ribozyme DNA (rDNA) in order to identify the regulatory function of Tip5 protein in regulation of higher-order rDNA chromatin structure. MST results revealed weak affinity in comparison to control (HMGA1).…”

Section: Mst Of Nucleic Acids Interactionsmentioning

confidence: 99%

Thermophoresis for characterizing biomolecular interaction

Asmari

Ratih

Alhazmi

et al. 2018

Methods

101

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The study of biomolecular interactions is crucial to get more insight into the biological system. The interactions of protein-protein, protein-nucleic acids, protein-sugars, nucleic acid-nucleic acids and protein-small molecules are supporting therapeutics and technological developments. Recently, the development in a large number of analytical techniques for characterizing biomolecular interactions reflect the promising research investments in this field. In this review, microscale thermophoresis technology (MST) is presented as an analytical technique for characterizing biomolecular interactions. Recent years have seen much progress and several applications established. MST is a powerful technique in quantitation of binding events based on the movement of molecules in microscopic temperature gradient. Simplicity, free solutions analysis, low sample volume, short analysis time, and immobilization free are the MST advantages over other competitive techniques. A wide range of studies in biomolecular interactions have been successfully carried out using MST, which tend to the versatility of the technique to use in screening binding events in order to save time, cost and obtained high data quality.

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Section: Mst Of Nucleic Acids Interactionsmentioning

confidence: 99%

Thermophoresis for characterizing biomolecular interaction

Asmari

Ratih

Alhazmi

et al. 2018

Methods

101

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“…This need not, however, be a direct effect. Given that a similar effect is mimicked by serum starvation, it is possible that there the eNoSC complex may also influence this process, although the direct physical association of Tip5 with the nuclear matrix reported here (Zillner et al, 2013) could be an additional way of amplifying local chromatin remodelling into an rDNA-wide effect. As an interesting aside, TTF-I may also have more general functions in maintaining heterochromatin stability throughout eukaryotic nuclei.…”

Section: Silencing Of Aberrant Rna Pol II Transcription In Nucleolimentioning

confidence: 82%

“…In mammals, too, recent work has suggested that NoRC, or at least one of its component proteins, is important for the overall chromatin organisation of the rDNA repeats. The authors indicate that over-expression of Tip5 causes general changes to DNaseI accessibility (Zillner et al, 2013), a standard measure of chromatin compaction. This need not, however, be a direct effect.…”

Section: Silencing Of Aberrant Rna Pol II Transcription In Nucleolimentioning

confidence: 99%

Mechanisms of rDNA silencing and the Nucleolar Remodelling Complex (NoRC)

McKeown¹

2014

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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Protein synthesis in living cells requires functional ribosomes which are composed of ribosomal proteins and ribosomal RNA (rRNA) molecules. rRNA is transcribed from tandemly repeated ribosomal DNA (rDNA) which is organised into a nuclear compartment termed the nucleolus in S-phase cells. It is essential that rDNA transcription is properly regulated in order to meet the cell's requirements for ribosomes and hence protein synthesis without wasting metabolic energy. In the last twenty years many proteins involved in regulating this process have been identified, suggesting that most organisms contain multiple protein complexes that regulate rDNA packaging and transcription. Importantly, it has become clear that errors in the function of these proteins can permit aberrant cellular growth, including in several classes of cancer. In this review, I discuss the history of how protein complexes such as the Nucleolar Remodelling Complex (NoRC) were discovered, using examples from humans and from model research organisms from different biological groups. I will discuss recent discoveries of the critical roles of rDNA-binding complexes in nucleolar assembly, the widespread occurrence of regulatory non-coding RNAs which interact with these complexes, and the pathways which regulate rDNA transcription in response to cellular energy status. Finally, I will review the growing evidence that misregulation of rDNA transcription not only allows the growth of cancerous cells, but can trigger oncogenesis itself.

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“…[139] BAZ2A (also called TIP5 and TTF5) is a component of the nucleolar remodeling complex NoRC. [142] In addition, the NoRC complex is implicated in the upkeep of high-order chromatin structure at telomere and centromere regions of chromosomes. Interaction of NoRC with the DNA regions coding for rRNA modifies the local histone marks and increases DNA methylation, thus leading to transcriptional shutdown.…”

Section: Baz Familymentioning

confidence: 99%

“…[141] Different BAZ2A regions play a role in nuclear matrix association, nu-cleolar targeting, and DNA binding. [142] In addition, the NoRC complex is implicated in the upkeep of high-order chromatin structure at telomere and centromere regions of chromosomes. [140a] In line with this, silencing of BAZ2A expression is followed by increased recombination between telomere repeats and chromosomal translocations.…”

Section: Baz Familymentioning

confidence: 99%

Bromodomains and Their Pharmacological Inhibitors

et al. 2014

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Over 60 bromodomains belonging to proteins with very different functions have been identified in humans. Several of them interact with acetylated lysine residues, leading to the recruitment and stabilization of protein complexes. The bromodomain and extra-terminal domain (BET) proteins contain tandem bromodomains which bind to acetylated histones and are thereby implicated in a number of DNA-centered processes, including the regulation of gene expression. The recent identification of inhibitors of BET and non-BET bromodomains is one of the few examples in which effective blockade of a protein-protein interaction can be achieved with a small molecule. This has led to major strides in the understanding of the function of bromodomain-containing proteins and their involvement in diseases such as cancer and inflammation. Indeed, BET bromodomain inhibitors are now being clinically evaluated for the treatment of hematological tumors and have also been tested in clinical trials for the relatively rare BRD-NUT midline carcinoma. This review gives an overview of the newest developments in the field, with a focus on the biology of selected bromodomain proteins on the one hand, and on reported pharmacological inhibitors on the other, including recent examples from the patent literature.

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Large-scale organization of ribosomal DNA chromatin is regulated by Tip5

Cited by 29 publications

References 47 publications

Thermophoresis for characterizing biomolecular interaction

Thermophoresis for characterizing biomolecular interaction

Mechanisms of rDNA silencing and the Nucleolar Remodelling Complex (NoRC)

Bromodomains and Their Pharmacological Inhibitors

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