Results 261 to 270 of about 476,829 (342)

Structural insights for enhanced ROS detoxification of eKatE, a recently identified catalase in atypical E. coli

open access: yesThe FEBS Journal, EarlyView.
We revealed the crystal structure of eKatE from atypical E. coli. eKatE exhibits a hydrogen‐peroxide‐sensitive major channel, a stabilized dimeric interface, an unusual covalent bond between C392 and Y415, and other distinctive features. These structural features contribute to its enhanced catalase activity compared to KatE in typical E.
Eunhee Koh   +7 more
wiley   +1 more source

Homeostatic Influence of Fig4 Outside of the Fab1-Vac14-Fig4 Complex in Saccharomyces cerevisiae. [PDF]

open access: yesMol Microbiol
Reeves HE   +13 more
europepmc   +1 more source

Biostimulants in plant brassinosteroid hormone receptor BRI1 activation—a new system to evaluate activation capacity

open access: yesThe FEBS Journal, EarlyView.
A novel assay evaluates plant biostimulants targeting the brassinosteroid receptor BRI1, a central component in plant growth and development. By expressing BRI1 in fission yeast, functional activation by brassinolide (BL) was enabled. Transcriptomic profiling identified BL‐responsive genes, leading to a GFP‐based reporter system. This platform offers a
Maribel Marquina   +9 more
wiley   +1 more source

Evolutionary divergence and functional insights into the heteromeric cis‐prenyltransferase of Paramecium tetraurelia

open access: yesThe FEBS Journal, EarlyView.
Heteromeric cis‐prenyltransferases (CPT) are indispensable for dolichol synthesis and protein N‐glycosylation in most eukaryotes. The catalytic subunits are strongly conserved throughout evolution, in contrast to the evolutionarily variable accessory subunits. The POC1 protein from Paramecium tetraurelia is the smallest identified CPT‐accessory subunit
Agnieszka Onysk   +8 more
wiley   +1 more source

Synthetic trap‐peptides identify a TOM complex phosphatase – PP2A dephosphorylates Tom6

open access: yesThe FEBS Journal, EarlyView.
Synthetic trap‐peptides facilitate the identification of complete holoenzymes that bind to the target sequence remarkably close to the phosphorylation site. PP4 bound to, but did not dephosphorylate, the peptide substrate taken from yeast Tom6 pSer16, showing that proximity alone does not induce phosphatase activity.
Laura Scheinost   +7 more
wiley   +1 more source

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