Subunit redundancy within the NuRD complex ensures fidelity of ES cell lineage commitment

Multiprotein chromatin remodelling complexes show remarkable conservation of function amongst metazoans, even though components present in invertebrates are often present as multiple paralogous proteins in vertebrate complexes. In some cases these paralogues specify distinct biochemical and/or funct...

Full description

Saved in:
Bibliographic Details
Published inbioRxiv
Main Authors Burgold, Thomas, Barber, Michael, Kloet, Susan, Cramard, Julie, Gharbi, Sarah, Floyd, Robin, Kinoshita, Masaki, Ralser, Meryem, Vermeulen, Michiel, Reynolds, Nicola, Dietmann, Sabine, Hendrich, Brian
Format Paper
LanguageEnglish
Published Cold Spring Harbor Cold Spring Harbor Laboratory Press 10.07.2018
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary:Multiprotein chromatin remodelling complexes show remarkable conservation of function amongst metazoans, even though components present in invertebrates are often present as multiple paralogous proteins in vertebrate complexes. In some cases these paralogues specify distinct biochemical and/or functional activities in vertebrate cells. Here we set out to define the biochemical and functional diversity encoded by one such group of proteins within the mammalian Nucleosome Remodelling and Deacetylation (NuRD) complex: Mta1, Mta2 and Mta3. We find that, in contrast to what has been described in somatic cells, MTA proteins are not mutually exclusive within ES cell NuRD and, despite subtle differences in chromatin binding and biochemical interactions, serve largely redundant functions. Nevertheless, ES cells lacking all three MTA proteins represent a complete NuRD null and are viable, allowing us to identify a previously undetected function for NuRD in maintaining differentiation trajectory during early stages of lineage commitment. Footnotes * Change of title, fixed typos
DOI:10.1101/362988