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Regulation of TDP2 function by sumo interactions.

Opened Access Regulation of TDP2 function by sumo interactions.
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Autor: Lieberman, Jenna
Director: Cortes Ledesma, Felipe
Departamento: Universidad de Sevilla. Departamento de Genética
Fecha: 2017-09-29
Tipo de documento: Tesis Doctoral
Resumen: Topoisomerase 2 (TOP2) performs a vital enzymatic activity, solving DNA topological problems in fundamental metabolic processes. The enzyme is able to untangle DNA by passing an intact helix through a transient double-strand break (DSB). The intermediate of its catalytic cycle, TOP2 covalently bound to DNA, is usually short lived, and is known as the TOP2 cleavage complex (TOP2cc). Tyrosyl DNA phosphodiesterase 2 (TDP2) is a protein involved in the removal of proteasome degraded TOP2cc, thus im-portant for the efficient repair of TOP2-induced DNA DSBs. Consequently, TDP2-deficient cells are sensitive to the TOP2 poison etoposide. Sumoylation is an important modification involved in the DNA damage response (DDR). While TOP2 sumoylation is important in several cellular processes, it is not known whether TOP2 is sumoylated in the context of the cleavage complex and the possible physiological relevance. In this work, Here, we describe for the first time SUMO1 and SUMO2/3 modification of T...
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Cita: Lieberman , J. (2017). Regulation of TDP2 function by sumo interactions.. (Tesis Doctoral Inédita). Universidad de Sevilla, Sevilla.
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