Tatiana Moiseeva

Tatiana Moiseeva
Tallinn University of Technology | TTU · Department of Chemistry and Biotechnology

PhD

About

36
Publications
2,372
Reads
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423
Citations
Introduction
Independent senior research scientist in the Department of Chemistry and Biotechnology, Tallinn University of Technology. Interested in regulation of replication initiation in human cells.
Additional affiliations
August 2019 - present
Tallinn University of Technology
Position
  • Senior Researcher
February 2013 - July 2019
University of Pittsburgh
Position
  • PostDoc Position
January 2007 - February 2013
Russian Academy of Sciences
Position
  • Institute of Cytology of the Russian Academy of Sciences
Education
November 2007 - October 2010
Institute of Cytology of the Russian Academy of Sciences
Field of study
  • molecular biology
September 2004 - June 2007
September 2001 - September 2004

Publications

Publications (36)
Article
Full-text available
ATR kinase activity slows replication forks and prevents origin firing in damaged cells. Here we describe proteomic analyses that identified mechanisms through which ATR kinase inhibitors induce unscheduled origin firing in undamaged cells. ATR-Chk1 inhibitor-induced origin firing is mediated by Cdc7 kinase through previously undescribed phosphoryl...
Article
Full-text available
DNA damage-induced signaling by ATR and CHK1 inhibits DNA replication, stabilizes stalled and collapsed replication forks, and mediates the repair of multiple classes of DNA lesions. We and others have shown that ATR kinase inhibitors, three of which are currently undergoing clinical trials, induce excessive origin firing during unperturbed DNA rep...
Article
Mechanisms that limit origin firing are essential as the ˜50,000 origins that replicate the human genome in unperturbed cells are chosen from an excess of ˜500,000 licensed origins. Computational models of the spatiotemporal pattern of replication foci assume that origins fire stochastically with a domino-like progression that places later firing o...
Article
Full-text available
ATR kinase is a central regulator of the DNA damage response (DDR) and cell cycle checkpoints. ATR kinase inhibitors (ATRi's) combine with radiation to generate CD8⁺ T cell-dependent responses in mouse models of cancer. We show that ATRi's induce cyclin-dependent kinase 1 (CDK1)-dependent origin firing across active replicons in CD8⁺ T cells activa...
Preprint
DNA polymerase epsilon in an essential enzyme, responsible for the synthesis of the leading strand during DNA replication. Deficiencies and mutations in DNA polymerase epsilon catalytic subunit (POLE1) cause severe developmental abnormalities and cancers. Paradoxically, the non-catalytic C-terminal domain of yeast polymerase epsilon catalytic subun...
Preprint
ATR kinase is a central regulator of the DNA damage response (DDR) and cell cycle checkpoints. However, little is known about the role of ATR in the cell cycle and the impact of DDR inhibitors in immune cells in the absence of DNA damage. We previously showed that the ATR inhibitor AZD6738 (ATRi) combines with radiation to generate delayed, CD8+ T...
Article
Full-text available
WEE1 kinase is a key regulator of the G2/M transition. The WEE1 kinase inhibitor AZD1775 (WEE1i) induces origin firing in replicating cells. We show that WEE1i induces CDK1-dependent RIF1 phosphorylation and CDK2- and CDC7-dependent activation of the replicative helicase. WEE1 suppresses CDK1 and CDK2 kinase activities to regulate the G1/S transiti...
Article
Full-text available
RAD51 plays a central role in homologous recombination during double-strand break repair and in replication fork dynamics. Misregulation of RAD51 is associated with genetic instability and cancer. RAD51 is regulated by many accessory proteins including the highly conserved Shu complex. Here, we report the function of the human Shu complex during re...
Article
Full-text available
ATR kinase is activated by RPA-coated single-stranded DNA (ssDNA) to orchestrate DNA damage responses. Here we show that ATR inhibition differs from ATR loss. Mouse model expressing kinase-dead ATR (Atr+/KD), but not loss of ATR (Atr+/−), displays ssDNA-dependent defects at the non-homologous region of X-Y chromosomes during male meiosis leading to...
Article
The origin of species would not have been possible without high fidelity DNA replication and complex genomes evolved with mechanisms that control the initiation of DNA replication at multiple origins on multiple chromosomes such that the genome is duplicated once and only once. The mechanisms that control the assembly and activation of the replicat...
Article
Full-text available
We describe a dynamic phosphorylation on serine-1940 of the catalytic subunit of human Pol ε, POLE1, following DNA damage. We also describe novel interactions between POLE1 and the iron-sulfur cluster assembly complex CIA proteins CIAO1 and MMS19. We show that serine-1940 is essential for the interaction between POLE1 and MMS19, but not POLE1 and C...
Article
Full-text available
The proteasome is the main intracellular proteolytic machine involved in the regulation of numerous cellular processes, including gene expression. In addition to their proteolytic activity, proteasomes also exhibit ATPase/helicase (the 19S particle) and RNAse (the 20S particle) activities, which are regulated by post-translational modifications. In...
Article
Proteasomes act as the main apparatus of non-lysosomal intracellular proteolysis and participate in the regulation of most important cellular processes. Despite considerable progress in the understanding of proteasome's functioning, some issues, in particular, RNase activity of these ribonucleoprotein complexes and its regulation remain scarcely ex...
Article
Proteasomes function as the main nonlysosomal machinery of intracellular proteolysis and are involved in the regulation of the majority of important cellular processes. Despite the considerable progress that has been made in understanding the functioning of proteasomes, some issues (in particular, the RNase activity of these ribonucleoprotein compl...
Article
Full-text available
Stability of proteins is largely controlled by post-translational covalent modifications. Among those, ubiquitylation plays a central role as it marks the proteins for proteasome-dependent degradation. Proteolytic activities of proteasomes are critical for execution of various cellular processes, including DNA damage signaling and repair. However,...
Article
The 26S proteasome is a large multi-subunit protein complex that exerts specific degradation of proteins in the cell. The 26S proteasome consists of the 20S proteolytic particle and the 19S regulator. In order to be targeted for proteasomal degradation most of the proteins must undergo the post-translational modification of poly-ubiquitination. How...
Article
Full-text available
26S proteasome is a multisubunit protein complex that consists of 19S regulatory and 20S catalytic subcomplexes. The primary proteasome cellular function is protein degradation. It has recently been found that, in addition to its proteolytic activities, the 20S particle also displays endoribonuclease activity mediated by two alpha-type subunits, α1...
Article
Full-text available
26S proteasome is a large multi-subunit protein complex involved in proteolytic degradation of proteins. In addition to its canonical proteolytic activity, the proteasome is also associated with recently characterized endoribonuclease (endo- RNAse) activity. However, neither functional significance, nor the mechanisms of its regulation are currentl...
Article
26S proteasome is a multisubunit protein complex that plays a pivotal role in protein degradation. Proteasome's enzymatic activities - proteolytic, ATPase/helicase and RNase - can be used in regulation of multiple cellular processes. Recent studies confirm the major role of proteasomes in transcriptional regulation. Although various post-translatio...
Article
26S proteasome is a multi-subunit protein complex that consists of the regulatory 19S and the catalytic 20S subcomplexes. The major cellular function of the proteasome is protein degradation. It has been found recently that the 20S particle, besides its proteolytic activity, also possesses endoribonuclease activity. The latter is mediated by two al...
Article
The 26S proteasome is an abundant multi-subunit complex, which, in addition to lysosomes, represents a major cellular "protein degradation factory". The proteasome complex possesses protease, ATPase/helicase, and RNAse enzymatic activities, which are used by the latter to regulate various physiological processes. Recent findings have revealed an im...
Article
Here we have studied changes in the subunit composition, phosphorylation state and enzymatic activities of 26S proteasomes in cells undergoing the programmed cell death. Apoptosis in proerythroleukemic K562 cells was induced by glutathione-depleting agent, diethylmaleate (DEM). We have shown for the first time that proteasomes isolated from the nuc...
Article
The specificity of 26S proteasomes' endoribonuclease activity has been shown to be changed under effect of erythroid differentiation (hemin) and programmed cell death (diethylmaleate) inductors in proerythroleukemic K562 cells. Treatment of K562 cells with apoptosis and differentiation inductors leads to the specific stimulation of RNase activity t...
Article
Full-text available
In the present work, changes in the subunit composition, phosphorylation state, and enzymatic activities of 26S proteasomes undergoing programmed cell death were studied. Apoptosis in proerythroleukemic K562 cells was induced by the glutathione-depleting agent, diethylmaleate (DEM). We have shown for the first time that proteasomes isolated from th...
Article
The specificity of the 26S proteasome endoribonuclease activity in proerythroleukemic K562 cells has been shown to change under the effects of inducers of erythroid differentiation inducers led to specific stimulation of RNase activity for certain mRNAs and to reduction of proteasome RNase activity for other mRNAs. The studied enzymatic activity wa...
Article
The participation of proteasome in the programmed cells death is now extensively investigated. Studies using selective inhibitors of proteasomes have provided a direct evidence of both pro- and anti-apoptotic functions of proteasomes. Such opposite roles of 26S proteasomes in regulation of apoptosis may be defined by the proliferative state of cell...

Questions

Question (1)
Question
I'm looking for a pair of tags that would produce fluorescent signal only whey they are far enough apart. Like anti-BiFC or anti-FRET. Could not find any protein-based fluorescence quenchers in the literature. Any suggestions?
Thank you.

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Projects

Projects (2)
Archived project
proteasome modifications and activity