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Interaction partners of HypA and HypB metallochaperones from Methanococcus maripaludis

ABSTRACT: This project is focused on identifying proteins interacting with the HypA and HypB metallochaperones in the methanogen, Methanococcus maripaludis. Strep-tagged proteins were over expressed and purified from M. maripaludis, followed by LC-MS/MS analysis of co-purified proteins.

INSTRUMENT(S):

ORGANISM(S): Methanococcus Maripaludis

TISSUE(S): Cell Culture

SUBMITTER: Keith Ray

LAB HEAD: Kylie Allen

PROVIDER: PXD074172 | Pride | 2026-06-11

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	230628_GelBands_M1_01.mgf	Mgf
	230628_GelBands_M1_01.raw	Raw
	230628_GelBands_M2_01.mgf	Mgf
	230628_GelBands_M2_01.raw	Raw
	230628_QC_M3_01.mgf	Mgf

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1 - 5 of 17

Publications

The HypA and HypB metallochaperones from Methanococcus maripaludis have unique metal-binding properties and a distinct nickel transfer mechanism.

Dinh Thuc-Anh TA Jiang Nanqi N Lyons Kimberly B KB Thomas Anna A Boulware Perry P Ray W Keith WK Duin Evert C EC Allen Kylie D KD

The Journal of biological chemistry 20260417 6

[NiFe] hydrogenases are widespread microbial metalloenzymes that catalyze the reversible conversion of hydrogen (H<sub>2</sub>) to protons and electrons, playing key roles in energy metabolism. The biosynthesis of the NiFe(CN)<sub>2</sub>CO cofactor involves a suite of maturation proteins, including the HypA and HypB nickel metallochaperones. Here, we define the metal-binding properties, nucleotide-dependent behavior, and functional interplay of HypA and HypB from the hydrogenotrophic methanogen ...[more]

PMID: 42001940

Similar Datasets

Interaction partners of HypA and HypB metallochaperones from Methanococcus maripaludis

Project description:This project is focused on identifying proteins interacting with the HypA and HypB metallochaperones in the methanogen, Methanococcus maripaludis. Strep-tagged proteins were over expressed and purified from M. maripaludis, followed by LC-MS/MS analysis of co-purified proteins.

2026-03-31 | PXD074259 | Pride

Human RBM33_HNSC_LC-MS/MS in project "RBM33 Acts as an m6A Reader Required for ALKBH5-mediated m6A Demethylation"

Project description:To identify the potential RBM33 interaction proteins, we established UM-SCC-1 cells stably expressing pCDH-Strep-Vec, or Strep-RBM33. After strep-tactin beads enrichment of RBM33 and its ascociated proteins, all the pull-downed proteins are subjected to LC-MS/MS analysis.

2023-05-30 | PXD033861 | Pride

ChIP-seq of H2A.Z and its histone chaperones during the cell cycle

Project description:The aim of this study was to uncover cell cycle dependent chromatin binding of H2A.Z and its histone chaperones. U2OS cells were stably transfected with Twin-Strep-tagged H2A.Z, ANP32e, or YL1 constructs, and WT cells were used as a negative/background control. U2OS cells were synchronised in G1 or G2-M phase using hydroxyurea or nocodazole, respectively, and protein-DNA complexes were isolated by affinity purification.

2023-06-29 | E-MTAB-11617 | biostudies-arrayexpress

Strep MIWI Elution Mass Spectrometry

Project description:In this project, we aimed to unravel the structure of endogenous mouse MIWI via affinity purification of the Strep-II tagged protein. In order to confirm that the protein retains its canonical interactors despite the internal Strep II tag, we affinity purified the protein and inspected its interactors via DIA.

2026-01-13 | PXD071431 | Pride

Purification of AtNAA10 and AtHYPK from leaves of transgenic Arabidopsis plants expressing Strep II –tagged NAA10 or HYPK

Project description:In humans and plants, 40 % of the proteome is co-translationally acetylated at the N-terminus by a single Nα-acetyltransferase (Nat) termed NatA. The core NatA complex consists of the catalytic subunit NAA10 and the ribosome-anchoring subunit NAA15. In humans, the regulatory subunit HYPK and the acetyltransferase NAA50 join this complex. Even though both are conserved in Arabidopsis thaliana, only AtHYPK is known to interact with AtNatA. Here we fused AtNAA10 and AtHYPK with the Strep II®-tag and expressed them separately in stably transformed Arabidopsis thaliana ecotype Col-0 (for AtNAA10) or the hypk-3 (for AtHYPK) mutant (Miklánková et al., 2022). Stably transformed plants of the T2 generation were grown on soil under short-day conditions. Six weeks after germination, the Strep-tagged proteins were purified from leaf material and subjected to mass-spectrometry to identify potential interaction partners.

2024-03-05 | PXD043208 | Pride

MMP103

Project description:Methanococcus maripaludis is a methanogenic Archaea that conserves energy from molecular hydrogen to reduce carbon dioxide to methane. Chemostat grown cultures limited for phosphate or leucine were compared to determine the regulatory response to leucine limitation. Keywords: archaea, hydrogen, leucine, phosphate, nutrient limitation, growth rate, methanogen

2007-08-30 | GSE8728 | GEO

Proteins identified by LC-MS/MS analysis to associate with RecJ4-StrepII (vs. empty vector).

Project description:RecJ4 association with RecJ3, RNase J and Cdc48A investigated by pullingown strep tagged-RecJ4 with its partner proteins

2023-06-22 | PXD019933 | Pride

Phosphorylation of Asc1p and Asc1p-dependent phospho-proteome

Project description:Phosphorylation of Asc1p and Asc1p-dependent phospho-proteome We determined 1) the phosphorylation sites within the Asc1 protein purified from Saccharomyces cerevisiae via its Strep-tag and 2) the Asc1p-dependent phospho-proteome. 1) Phospho-sites within tryptic peptides of Asc1p were identified using the Proteome Discoverer 1.4 software with the SequestHT and Mascot search engines and phosphorylation site localization was evaluated with the phosphoRS tool. 2) Quantitative triple SILAC-based phospho-proteome comparison of an ASC1 wild-type strain with asc1 mutant strains. MS data were analyzed with MaxQuant and Perseus.

2016-12-13 | PXD003031 | Pride

Mtr complex and MtrI quantification from Methanosarcina mazei

Project description:This dataset contains LC-MS/MS data from multiple experiments investigating the N⁵-methyltetrahydromethanopterin:CoM-S-methyltransferase (Mtr) complex of Methanosarcina mazei, with quantitative analysis performed using MaxQuant. Experiment 1: Strep-Tactin-based purification of the native Mtr complex from M. mazei grown on methanol. Samples were divided into two conditions: Group 1: Purification performed under aerobic conditions Group 2: Purification performed under anaerobic conditions Each condition was analyzed in biological triplicates. The aim was to quantify the relative abundance of MtrI (Uniprot ID: Q8PUD4) compared to other Mtr subunits, particularly MtrA. Experiment 2: Similar to Experiment 1, but cells were grown on H₂/CO₂ instead of methanol. Group 1: Aerobic purification Group 2: Anaerobic purification Again, biological triplicates were performed for each condition. The objective remained the same: to quantify MtrI in both groups relative to other Mtr subunits. Experiment 3: Reciprocal pulldown of Mtr subunits using His-tagged MtrI expressed in M. mazei, purified via Ni-NTA affinity chromatography. Empty vector control purifications were included to assess specificity of interactions. Full experimental details are available in the associated manuscript (Reif-Trauttmansdorff et al., 2025, in preparation).

2026-01-19 | PXD064689 | Pride

Analysis of the interactomes of ZAP70, CD247 and SLP76 upon stimulation of murine CD8+ T cells with ligands of different affinity to the TCR

Project description:T cells have the remarkable ability to sense and discriminate between a wide range of antigenic peptides bound to major histocompatibility complex molecules (pMHC). Here, we use interactomics to monitor in a time dependent manner the early molecular events taking place upon stimulation of murine CD8+ T cells with ligands of different affinity to the TCR. We used the mouse OT-I model in which T cells specifically recognize the ovalbumin OVA 257-264 peptide (SIINFEKL, also named N4) bound to the MHC-I molecule H-2Kb (pMHC). The OT-I TCR also recognizes altered peptide ligands amongst which SIITFEKL (T4) and SIIGFEKL (G4) with sub-optimal binding capacities (ligand affinity N4>T4>G4). For affinity purification (AP) of signalling complexes, we crossed OT-I TCR transgenic mice onto mice expressing an endogenous tagged (One-Strep-Tag: OST) version of the CD3z (also called CD247), ZAP70 or SLP76 molecules. CD8+ T cells were purified from pooled lymph nodes and spleens, shortly expanded, and were left unstimulated or stimulated with N4, T4 and G4 soluble pMHC tetramers for 30, 120 or 300 s. Complexes formed around either CD247, ZAP70 or SLP76 were then purified and analysed by mass spectrometry. Each AP-MS purification is associated with a corresponding control (purification from OT-I CD8+ T cells expressing only the endogenous version of each bait, cultured and stimulated in the same conditions). The number of replicate biological experiments was n=3 for all time-points, and each sample was analyzed twice by single-run nano LC-MS. In addition, the whole proteome of OT-I cell was analyzed by label-free shotgun proteomics in order to calculate cellular protein abundances for each interactor.

2022-07-05 | PXD029974 | Pride

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