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Covalent attachment of ubiquitin-like proteins to other proteins drives numerous important physiological processes. The recent structure of an ubiquitin-like E1 enzyme provides insight into the curious assembly line–like mechanism that initiates all ubiquitin-related protein processing pathways.
Function analysis of 'insulators' has led to the idea that they comprise two separable and mechanistically distinct insulating activities — one blocking enhancer cross-talk and the other barring heterochromatin spreading. However, results from two recent studies have blurred this mechanistic distinction.
Many different RNA species undergo nucleotide modifications at sites identified by guide small nucleolar ribonucleoprotein (snoRNP) particles. The co-crystal structure of two snoRNP proteins gives valuable clues into the workings of this system.
CREB phosphorylation is required for transcriptional activation, but how dephosphorylation couples with decreased transcription activity was less obvious. New findings indicate that CREB can recruit histone deacetylase HDAC1 and protein phosphatase 1 in a concerted action, thus leading to attenuated transcription.
Recent experiments have shown that the co-translational folding of the multi-domain LDL receptor in the endoplasmic reticulum does not occur in a vectorial manner. Instead, newly translated chains form misfolded states involving incorrect disulfide bonds between residues distant in sequence.
The structure of one of the two catalytic domains of angiotensin converting enzyme in complex with an inhibitor provides molecular insights into the substrate- and inhibitor-binding profiles of this clinically important enzyme.
The high-resolution structure of the N-terminal half of an archaeal MCM protein domain sheds light on the enzyme's helicase activity and its role in DNA replication.
The structure of the extracellular domain of HER2/ErbB2 reveals why the receptor is an orphan and provides valuable insight into the receptor's readiness to partner with other ErbB family members.
Real time measurements of conformational switching in single Holliday junctions reinforce the role of the junction in the site selection and branch migration steps of genetic recombination.
Time-resolved X-ray absorption has been used to investigate the structure of the Zn active site in alcohol dehydrogenase during catalysis. The results support a new mechanistic model for catalysis.
Two recent studies show that some ATP-dependent chromatin remodeling complexes are subject to control by a surprising set of regulators — phosphoinositols. These studies extend earlier observations in mammalian cells and suggest that second messengers are regulators of chromatin remodeling.
Because some translation factors mimic the shape of tRNA, they were thought to bind the ribosome in a similar manner. Recent work suggests that this idea of molecular mimicry needs to be reassessed.
In vivo selection improves the folding efficiency of the GroELS chaperone toward a specific substrate. Optimizing efficiency, however, comes at the price of narrowed substrate specificity.
Protein toxins are known to translocate through intracellular membranes to reach their cytosolic targets. Results from studies with botulinum neurotoxin suggest that the toxin heavy chain functions as both a channel and a chaperone for translocation of the catalytically active light chain.
Dinucleotide CA repeats of variable length in an intron of the human endothelial nitric oxide synthase gene act as regulatory signals for splicing of the gene's pre-mRNA. Repeat length–dependent binding of hnRNP L to the repeats provides an intriguing link between splicing efficiency, nitric oxide synthesis and cardiovascular disease.
The hormone-related protein PTHrP travels from the cytosol to the nucleus by binding to the transport factor importin β. Remarkably, the site of recognition of PTHrP is the N-terminal half of importin β, which also has Ran-binding and nucleoporin-binding capabilities and is, therefore, sufficient by itself to function in PTHrP nuclear import.
