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ProteomicsMechanism of cooperative strigolactone perception by the MAX2 ubiquitin ligase–receptor–substrate complex
Strigolactones are plant hormones that regulate development and mediate interactions with soil organisms, including the germination of parasitic plants such as Striga hermonthica. Strigolactone perception by receptors initiates the degradation of transcriptional repressors via E3 ubiquitin ligases, ...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) Striga hermonthica 
2025-09-19 | PXD068313 | Pride
E3 ligase Cryo-em Plant hormone Hdx-ms 
Proteomicsβ-Carotene alleviates substrate inhibition caused by asymmetric cooperativity
Enzymes play a crucial role in biological systems and biotechnological processes as vital and sustainable catalysts that facilitate and regulate biochemical reactions. Inhibition of product formation of an enzyme by its own substrate was originally dismissed as an artifact of biochemical analysis, b...
ORGANISM(S): Nicotiana benthamiana 
2025-03-06 | PXD056344 | Pride
Hdxms X-ray crystallography Substrate inhibition Ugt Nicotiana benthamiana 
ProteomicsSelective ubiquitination of drug-like small molecules by the ubiquitin ligase HUWE1
The ubiquitin system regulates eukaryotic physiology by modifying specific substrate proteins. Substrate recruitment and the assembly of ubiquitin signals are determined by ubiquitin ligases, some of which also modify non-protein biomolecules. Here we expand this substrate realm, revealing that the ...
ORGANISM(S): Homo sapiens (Human) 
2025-09-02 | PXD066563 | Pride
Small-molecule inhibitor Hect e3 Mass spectrometry Enzymology Click chemistry Non-protein ubiquitination 
Unknown(p)ppGpp: Magic Modulators of Bacterial Physiology and Metabolism.
Not available
S-EPMC7504894 | biostudies-literature
ProteomicsStructure of the minimal type I-F2 CRISPR-Cas DNA-interference complex
CRISPR–Cas systems provide adaptive immunity in prokaryotes by targeting and degrading invasive genetic elements. Among them, the type I-F2 system represents the most compact type I CRISPR–Cas system, distinguished by the absence of small and large subunits. These subunits are otherwise essential fo...
ORGANISM(S): Shewanella putrefaciens CN-32 
2026-03-09 | PXD068253 | Pride
Cryo-em Shewanella putrefaciens Hdx-ms Dna interference Interference complex 
Proteomicsc-di-GMP-induced conformational dynamics of the c-di-GMP-binding protein A (CdbA) from Myxococcus xanthus
The second messenger c-di-GMP has important functions in response to changing environmental and cellular cues in bacteria. Here, we report the identification of CdbA, a DNA binding protein of the ribbon-helix-helix family in Myxococcus xanthus, and show that it binds c-di-GMP in vitro. CdbA is essen...
ORGANISM(S): Myxococcus xanthus DK 1622 
2020-04-16 | PXD018028 | Pride
C-di-gmp Plgs Hdx-ms Dynamx 
ProteomicsInteraction of human eIF5A and DHS K329A variant studied by HDX-MS
Hypusination is a unique post-translational modification of the eukaryotic translation factor 5A (eIF5A) that is essential for overcoming ribosome stalling at polyproline sequence stretches. The initial step of hypusination, the formation of deoxyhypusine, is catalyzed by deoxyhypusine synthase (DHS...
ORGANISM(S): Homo sapiens (Human) Escherichia coli 
2023-05-10 | PXD040460 | Pride
Eif5a Hdx-ms Synapt-g2 si Dhs k329a variant 
UnknownFRET Monitoring of a Nonribosomal Peptide Synthetase Elongation Module Reveals Carrier Protein Shuttling between Catalytic Domains.
Not available
S-EPMC9828546 | biostudies-literature
UnknownLayered entrenchment maintains essentiality in the evolution of Form I Rubisco complexes.
Not available
S-EPMC11696622 | biostudies-literature
ProteomicsPausing protein acetylation by an Ac-CoA synthetase/acetyltransferase complex.
Acetyl-CoA synthetase (Acs) generates acetyl-Coenzyme A (Ac-CoA) but its excessive activity can deplete ATP and lead to growth arrest. To prevent this, Acs is tightly regulated through Ac-CoA-dependent feedback inhibition executed by Ac-CoA-dependent acetyltransferases such as AcuA in Bacillus subti...
ORGANISM(S): Bacillus subtilis subsp. subtilis str. 168 
2025-02-28 | PXD058390 | Pride
Acsa Cryo-em Protein acetylation Hdx-ms Acua 
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