Rad50-Mre11-Xrs2 nuclease activities on 5' flap and nicked DNA structures

CAVDAROVA, Melita. Rad50-Mre11-Xrs2 nuclease activities on 5' flap and nicked DNA structures. 2008.

Basic information

Original name

Rad50-Mre11-Xrs2 nuclease activities on 5' flap and nicked DNA structures

Name in Czech

Nukleázové aktivity Rad50-Mre11-Xrs2 na 5' flap a struktury DNA s jednořetězovým zlomem

Authors

CAVDAROVA, Melita

Edition

2008

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Other information

Language

English

Type of outcome

Audiovizuální tvorba

Field of Study

10600 1.6 Biological sciences

Country of publisher

Germany

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Organization unit

Faculty of Science

Keywords in English

Dna repair; homologous recombination; nuclease

Tags

DNA repair, HOMOLOGOUS RECOMBINATION, nuclease

Tags

International impact

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Abstract

V originále

DNA double-strand breaks (DSBs) are among the most cytotoxic form of DNA damage and can lead to chromosomal aberrations, disruption of genomic integrity and cancer in mammals. This DNA breaks can arise from many sources, including toxic agents, ionizing radiation and enzymatic activities. Predominant cause of DSBs in proliferating cells is errors in DNA replication. Thus cells have evolved various DNA repair pathways that can remove lesions from DNA, but the two major DSB repair pathways are homologous recombination (HR) and non-homologous end joining (NHEJ). Saccharomyces cerevisiae Rad50, Mre11, and Xrs2 proteins are involved in homologous recombination, non-homologous end-joining, DNA damage checkpoint signalling, telomere maintenance and resistance to DNA-damaging agents. These proteins form a stable complex RMX mediated by simultaneous interactions of Mre11 with Rad50 and Xrs2 that has nuclease, DNA binding, and DNA end recognition activities. Mre11 plays a central role in complex assembly by binding Rad50 and Xrs2. Towards defining the biochemical functions of Mre11 and its complexes RMX and RM we have over expressed them in yeast cells and purified to near homogeneity. Furthermore, we tested enzymatic activities (endo and exonuclease) of Mre 11 on different DNA substrates and how those activities were affected by presence of RAD 50 and XRS2. At the moment we are working on expression and purification of Mre11-Xrs2 complex and nuclease deficient mutant Mre11-3.

In Czech

in czech