The Genome Sequence of Capsaspora owczarzaki ATCC 30864.
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
X-RAY CRYSTALLOGRAPHY (1.34 ANGSTROMS) OF 182-368 IN COMPLEX WITH ADP-D-RIBOSE
Leucine Aminopeptidase, subunit E, domain 1
Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Specifically binds poly-ADP-ribose and plays a key role in NAD(+) metabolism (PubMed:34887560). Able to bind to the ends of poly-ADP-ribose chains created by PARP1 and cap them (PubMed:34887560). This prevents PARP1 from further addition of ADP-ribose and thus limits the consumption of nuclear NAD(+), allowing the cell to maintain proper NAD(+) levels in both the nucleus and the mitochondria to promote proper mitochondrial respiration (PubMed:34887560).
The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers.
Highly expressed during the cystic life stage.
The macro domain specifically binds poly-ADP-ribose (PubMed:34887560). Binds poly-ADP-ribose with much higher affinity compared to vertebrate macroH2A1.1 orthologs (PubMed:34887560).