Results 161 to 170 of about 181,301 (197)

Harnessing S. cerevisiae to advance the engineering of pentatricopeptide repeat proteins

open access: yesThe FEBS Journal, EarlyView.
Heterologous expression systems have been instrumental in furthering our understanding of plant RNA editing proteins. In this commentary, we discuss how the establishment of yeast as a model for studying plant RNA editing by Ramanathan et al. could advance the engineering of pentatricopeptide repeat proteins, and how in return pentatricopeptide repeat ...
Farley M. Kwok van der Giezen, Ian Small
wiley   +1 more source

Proteostasis of organelles in aging and disease

open access: yesThe FEBS Journal, EarlyView.
Cells rely on regulated proteostasis mechanisms to keep their internal compartments functioning properly. When these mechanisms fail, damaged proteins accumulate, disrupting organelles, such as the nucleus, mitochondria, endoplasmic reticulum, Golgi, and lysosomes, as well as membraneless organelles, such as stress granules, processing bodies, the ...
Yara Nabawi   +5 more
wiley   +1 more source

Comparative evaluation of noncanonical amino acids as site‐specific NMR probes for the complex of E. coli SSB with single‐stranded DNA without isotope labelling

open access: yesThe FEBS Journal, EarlyView.
Genetic encoding of noncanonical amino acids (ncAA) enables their site‐specific installation in proteins. This work compares the nuclear magnetic resonance (NMR) performance of different ncAAs in a large protein−DNA complex (~ 100 kDa) without isotope labelling. The ncAAs deliver readily detectable NMR signals in the complex between E.
Sreelakshmi Mekkattu Tharayil   +7 more
wiley   +1 more source

GCN2 in proteostasis: structural logic, signalling networks and disease

open access: yesThe FEBS Journal, EarlyView.
Threats to protein synthesis activate the kinase GCN2, initiating the integrated stress response (ISR). GCN2 is triggered by stalled ribosomes and uncharged tRNAs, which accumulate when amino acids are scarce. The ISR adjusts cellular physiology by promoting redox balance, protein quality control, and mitochondrial optimisation.
JiaYi Zhu, Stefan J. Marciniak
wiley   +1 more source

Genetic dissection reveals distinct contributions of the eS31 N‐terminal domain to translational accuracy in Saccharomyces cerevisiae

open access: yesThe FEBS Journal, EarlyView.
The eukaryote‐specific N‐terminal domain (NTD) of eS31 uses two distinct strategies to maintain translation fidelity. During elongation, a positively charged “hotspot” fine‐tunes the selection of incoming aa‐tRNA. During termination, the entire NTD acts as a structural scaffold to ensure the correct positioning of the release factor eRF1.
Qingxuan Gao   +3 more
wiley   +1 more source

Home - About - Disclaimer - Privacy