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ProteomicsPreparation of the RecJ3/4-RNase J complex from Haloferax volcanii
Purification of RecJ3/4-RNase J complex from Haloferax.volcanii
ORGANISM(S): Haloferax volcanii DS2 
2023-06-22 | PXD019898 | Pride
Recj4 Recj3 Rnasej 
ProteomicsRNase J, RecJ3, RNase J, RecJ3, Cdc48a and Cas7 co-purify with RecJ4-StrepII in the presence of γATP. and Cas7 co-purify with RecJ4-StrepII in the presence of γATP.
detecting core complex formation for RecJ3/4 and RNase J form a core complex.
ORGANISM(S): Haloferax volcanii DS2 
2023-06-22 | PXD019932 | Pride
Recj4 and cdc48a Recj3 
ProteomicsRNAseJ pull down to identify associated proteins
RNAse J, HVO_2724 from halophilic archaeon to identify the proteins it associates with
ORGANISM(S): Haloferax volcanii DS2 
2023-06-22 | PXD019896 | Pride
Rnase j Haloferax volcanii Hvo_2724 
ProteomicsProteins identified by LC-MS/MS analysis to associate with RecJ4-StrepII (vs. empty vector).
RecJ4 association with RecJ3, RNase J and Cdc48A investigated by pullingown strep tagged-RecJ4 with its partner proteins
ORGANISM(S): Haloferax volcanii DS2 
2023-06-22 | PXD019933 | Pride
Recj4 
ProteomicsCdc48A pulldown from an amino lonk column baited with SAMP1
H. volcanii Cdc48a, RecJ3/4 and RNase J associate with Ubl-coated beads. A) Strategy to isolate H. volcanii proteins that bind agarose beads charged with monomeric Ubl (vs. BSA) as bait. Cell lysate was from triplicate cultures of H. volcanii NH02-pJAM957. B) Left, Non-reducing SDS-PAGE of H. volcan...
ORGANISM(S): Haloferax volcanii DS2 
2023-06-22 | PXD019897 | Pride
Cdc48a Samp1 Hvo_2380 
ProteomicsProteins associated with Cdc48A identified by LC-MS\MS data
His6-Cdc48a and associated proteins purified from H. volcanii. A) SDS- PAGE of proteins purified by Ni2+ -chromatography. H. volcanii carrying empty vector control (H1209-pJAM202c, lane 1) and ectopically expressing His6-Cdc48a (H1209- pJAM1409, lane 2). Red bars indicate regions of gel excised. B)...
ORGANISM(S): Haloferax volcanii DS2 
2023-06-22 | PXD019906 | Pride
Cdc48a Hvo_2380 
ProteomicsHaloferax volcanii lysine acetylation
Oxidative stress adaptation strategies are important to cell function and are linked to cardiac, neurodegenerative disease and cancer. Representatives of the domain Archaea are used as model organisms based on their extreme tolerance to oxidants and close evolutionary relationship with eukaryotes. S...
ORGANISM(S): Haloferax volcanii DS2 
2023-07-20 | PXD041799 | Pride
Ptms Halophiles Acetylation Haloferax volcanii Oxidative stress 
ProteomicsUb-like SAMP1 and its associated proteins
Identifying proteins that associate with Ub like SAMP1 using an amino link column.
ORGANISM(S): Haloferax volcanii DS2 
2023-06-22 | PXD019931 | Pride
Samp1 Cdc48a Recj3/recj4 and rnasej 
ProteomicsHaloferax volcanii SILAC study of Oxidative stress
SILAC was used to monitor proteome changes to Haloferax volcanii after treatment with oxidizing agent NaOCl. SILAC amino acids used were Lysine(+8) and Arginine(+6). For treatment and control groups 4 replicates were used. In replicates 1 and 3, the control group had supplementation of both light l...
ORGANISM(S): Haloferax volcanii DS2 
2018-01-09 | PXD006877 | Pride
Archaea Silac Haloferax volcanii Quantitative proteomics Sodium hypochlorite Oxidative stress 
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