Lisa Baumgartner, Dominik Handler ... Julius Brennecke
Kipferl, a ZAD zinc finger protein from Drosophila, determines the chromatin binding specificity of the heterochromatin protein variant Rhino, defining piRNA clusters and preventing Rhino sequestration by selfish Satellite repeats.
Repression of gene expression by the histone methyltransferase G9a is guided by two zinc finger proteins that can recognize consensus sequences in DNA.
In humans, specific sequence features can predict whether meiotic recombination occurs at sites bound by the protein PRDM9, whose DNA-binding zinc-finger domain can unexpectedly bind to gene promoters and to other copies of PRDM9.
Genetically modified mouse model and comprehensive analysis reveal the molecular mechanisms regulating early T-cell development through intracellular TCRβ expression-mediated β-selection and independent cell survival signaling.
Lentiviral protein transduction offers a new approach for administration of custom-designed nucleases, leading to high-efficacy targeted gene editing and reduced off-target activity after virus-directed delivery of programmable nuclease proteins.
A novel zinc finger transcription factor regulates expression of multiple genes in late stage thymocytes and recent thymic emigrants to promote formation of the naïve T cell compartment.
Unbiased ChIP-seq screens and genetic knockouts of large Kruppel associated box zinc finger protein (KRAB-ZFP) clusters reveal that evolutionarily young KRAB-ZFPs play a redundant role in retrotransposon restriction in mice.
KHNYN, a putative endoribonuclease, interacts with the zinc-finger antiviral protein (ZAP) and is required for the inhibition of HIV replication and RNA abundance by CpG dinucleotides.
Zfp106 functions as an RNA binding protein, binds directly to GGGGCC RNA repeats, is required in motor neurons to prevent ALS-like neurodegeneration in mice, and can suppress neurotoxicity in an established fly model of ALS.
Thomas Pohlmann, Sebastian Baumann ... Michael Feldbrügge
An endosomal component employs a novel PAM2-like motif to recruit a key RNA-binding protein, which explains how mRNAs and associated ribosomes are attached to endosomes during coupled transport.