Non-homologous end joining

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Related publications (28)

Increased drug permeability of a stiffened mycobacterial outer membrane in cells lacking MFS transporter Rv1410 and lipoprotein LprG

Georg Fantner, Haig Alexander Eskandarian

The major facilitator superfamily transporter Rv1410 and the lipoprotein LprG (Rv1411) are encoded by a conserved two-gene operon and contribute to virulence in Mycobacterium tuberculosis. Rv1410 was originally postulated to function as a drug efflux pump, ...

2019

The telomeric DNA damage response: Insights into telomere compaction and identification of novel damage signaling factors

Aleksandra Vancevska

Telomeres are dynamic nucleo-protein structures capping the ends of all eukaryotic chromosomes. Together with telomerase, they counteract replication-dependent telomere attrition. Additionally, they disguise the linear ends of the chromosome from the DNA d ...

EPFL2018

Trypanosoma brucei UMSBP2 is a single-stranded telomeric DNA binding protein essential for chromosome end protection

Galina Glousker

Universal minicircle sequence binding proteins (UMSBPs) are CCHC-type zinc-finger proteins that bind a single-stranded G-rich sequence, UMS, conserved at the replication origins of the mitochondrial (kinetoplast) DNA of trypanosomatids. Here, we report tha ...

OXFORD UNIV PRESS2018

MAR-Mediated transgene integration into permissive chromatin and increased expression by recombination pathway engineering

Christian Iseli, Nicolas Mermod, Thomas Junier, Samuel Neuenschwander, Ioannis Xenarios

Untargeted plasmid integration into mammalian cell genomes remains a poorly understood and inefficient process. The formation of plasmid concatemers and their genomic integration has been ascribed either to non-homologous end-joining (NHEJ) or homologous r ...

2017

The telomeric DNA damage response occurs in the absence of chromatin decompaction

Joachim Lingner, Suliana Manley, Verena Pfeiffer, Aleksandra Vancevska, Kyle Michael Douglass

Telomeres are specialized nucleoprotein structures that protect chromosome ends from DNA damage response (DDR) and DNA rearrangements. The telomeric shelterin protein TRF2 suppresses the DDR, and this function has been attributed to its abilities to trigge ...

Cold Spring Harbor Laboratory2017

TRF2-Mediated Control of Telomere DNA Topology as a Mechanism for Chromosome-End Protection

Eric Aeby, Jing Ye, Bei Pei

The shelterin proteins protect telomeres against activation of the DNA damage checkpoints and recombinational repair. We show here that a dimer of the shelterin subunit TRF2 wraps similar to 90 bp of DNA through several lysine and arginine residues localiz ...

Cell Press2016

Recombinant protein production from stable mammalian cell lines and pools

David Hacker, Sowmya Balasubramanian

We highlight recent developments for the production of recombinant proteins from suspension-adapted mammalian cell lines. We discuss the generation of stable cell lines using transposons and lentivirus vectors (non-targeted transgene integration) and site- ...

Elsevier2016

ALT Telomeres Get Together with Nuclear Receptors

Joachim Lingner, Eric Aeby

Nuclear receptors bind chromosome ends in "alternative lengthening of telomeres" (ALT) cancer cells that maintain their ends by homologous recombination instead of telomerase. Marzec et al. now demonstrate that, in ALT cells, nuclear receptors not only tri ...

Cell Press2015

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