Guillardia theta CCMP2712
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA53577 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| Other | ||||
| SRR070672.fastq.gz | Fastqsanger.gz | |||
| SRR070673.fastq.gz | Fastqsanger.gz | |||
| SRR070674.fastq.gz | Fastqsanger.gz | |||
| SRR070675.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 5 of 12 |
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Project description:Plants and algae have developed various light harvesting mechanisms for optimal delivery of excitation energy to the photosystems. The cryptophyte algae have evolved a novel soluble light-harvesting antenna utilizing phycobilin pigments to complement the membrane-intrinsic Chl a/c-binding LHC antenna. This new antenna consists of the plastid-encoded beta-subunit, a relict of the ancestral phycobilisome, and a novel nuclear-encoded -subunit unique to cryptophytes. Together, these proteins form the active tetramer, which consists of one alpha 1 and one alpha 2 and two beta susbunits. In all cryptophyte algae investigated so far, the alpha-subunits have duplicated and diversified into a large gene family. Although there is transcriptional evidence for expression of all these genes, the x-ray structures determined to date suggest that only two of the -subunit genes might be significantly expressed at protein level. Using proteomics, we show that phycoerythrin 545 (PE545) of Guillardia theta, the only cryptophyte with a sequenced genome, all 20 alpha-subunits are expressed when the algae grow under white light. Their relative expression levels depend on the intensity of the growth light, but there is no evidence for a specific light-dependent regulation of individual members of the alpha-subunit family under the growth conditions applied. Subunit GtcpeA10 seems to be a special member of the alpha-subunit family, because it consists of two similar N- and C-terminal domains, which likely are the result of a partial gene duplication.
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Project description:DNA polymerase theta (Pol-theta)-mediated end-joining (TMEJ) repairs DNA double-strand breaks and confers resistance to genotoxic agents. How Pol-theta is regulated at the molecular level to exert TMEJ remains unknown. We find that Pol-theta interacts with and is PARylated by PARP1 in vitro and in cells. PARP1 recruits Pol-theta to the vicinity of DNA damage via PARylation dependent liquid demixing, however, PARylated Pol-theta (PAR-Pol-theta) cannot perform TMEJ due to its inability to bind DNA. PARG-mediated de-PARylation of Pol-theta reactivates its DNA binding and end-joining activities in vitro. Consistent with this, PARG is essential for TMEJ in cells and the temporal recruitment of PARG to DNA damage corresponds with TMEJ activation and dissipation of PARP1 and PAR. These studies support a two-step spatiotemporal mechanism of TMEJ regulation. First, PARP1 PARylates Pol-theta and facilitates its recruitment to DNA damage sites in an inactivated state. PARG subsequently activates TMEJ by removing repressive PAR marks on Pol-theta.
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Project description:OT-1 Transgenic CD8 T-cells were isolated from spleens of WT, PKCθ theta KO, and p50 cRel DKO mice. The T-cells were either cultured with non-pulsed DC (WT only and signified as "WT - UN") or with BMDCs pulsed with the OVA peptide SIINFEKL (N4) (WT, PKCθ theta KO, and p50 cRel DKO and signified as 'genotype - N4') at a ratio of 1:10 (DC:T-cell) for 18 hours. DCs then were depleted from the culture and RNA was made from the T-cells to measure gene expression at the early / late stage of T-cell activation
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