![Loading...](https://link.springer.com/static/c4a417b97a76cc2980e3c25e2271af3129e08bbe/images/pdf-preview/spacer.gif)
-
Article
Open AccessStructural basis for the non-self RNA-activated protease activity of the type III-E CRISPR nuclease-protease Craspase
The RNA-targeting type III-E CRISPR-gRAMP effector interacts with a caspase-like protease TPR-CHAT to form the CRISPR-guided caspase complex (Craspase), but their functional mechanism is unknown. Here, we repo...
-
Article
Open AccessThe SWI/SNF chromatin remodeling factor DPF3 regulates metastasis of ccRCC by modulating TGF-β signaling
DPF3, a component of the SWI/SNF chromatin remodeling complex, has been associated with clear cell renal cell carcinoma (ccRCC) in a genome-wide association study. However, the functional role of DPF3 in ccRCC...
-
Article
MARK4 controls ischaemic heart failure through microtubule detyrosination
Myocardial infarction is a major cause of premature death in adults. Compromised cardiac function after myocardial infarction leads to chronic heart failure with systemic health complications and a high mortal...
-
Article
Publisher Correction: Molecular basis of vasohibins-mediated detyrosination and its impact on spindle function and mitosis
An amendment to this paper has been published and can be accessed via a link at the top of the paper.
-
Article
Structural basis of tubulin detyrosination by the vasohibin–SVBP enzyme complex
Vasohibins are tubulin tyrosine carboxypeptidases that are important in neuron physiology. We examined the crystal structures of human vasohibin 1 and 2 in complex with small vasohibin-binding protein (SVBP) i...
-
Article
Molecular basis of vasohibins-mediated detyrosination and its impact on spindle function and mitosis
α-Tubulin detyrosination, largely catalyzed by vasohibins, is involved in many microtubule (MT)-related cellular events. In this study, we identified a core heterodimeric complex of human small vasohibin-bindi...
-
Article
Open AccessStructural and mechanistic insights into ATRX-dependent and -independent functions of the histone chaperone DAXX
The ATRX–DAXX histone chaperone complex incorporates the histone variant H3.3 at heterochromatic regions in a replication-independent manner. Here, we present a high-resolution x-ray crystal structure of an in...
-
Article
Histone chaperone networks sha** chromatin function
Chromatin integrity and functionality is governed by the controlled assembly and disassembly of nucleosomes.
- ...
-
Article
Open AccessStructural basis underlying viral hijacking of a histone chaperone complex
The histone H3.3 chaperone DAXX is implicated in formation of heterochromatin and transcription silencing, especially for newly infecting DNA virus genomes entering the nucleus. Epstein-Barr virus (EBV) can ef...
-
Article
H4K20me0 marks post-replicative chromatin and recruits the TONSL–MMS22L DNA repair complex
We have a limited understanding of how cells mark and identify newly replicated genomic loci that have a sister chromatid; here, unmethylated K20 in the tail of new histone H4 is shown to serve as a signature ...
-
Article
A unique binding mode enables MCM2 to chaperone histones H3–H4 at replication forks
Chromatin reassembly after replication requires recycling of old and deposition of new histones. Structural insights into how MCM2, part of the replicative helicase, interacts with H3–H4 suggest a function in ...
-
Article
DAXX envelops a histone H3.3–H4 dimer for H3.3-specific recognition
Histone chaperones represent a structurally and functionally diverse family of histone-binding proteins that prevent promiscuous interactions of histones before their assembly into chromatin. DAXX is a metazoa...
-
Article
Open AccessSolution structure of the second bromodomain of Brd2 and its specific interaction with acetylated histone tails
Brd2 is a transcriptional regulator and belongs to BET family, a less characterized novel class of bromodomain-containing proteins. Brd2 contains two tandem bromodomains (BD1 and BD2, 46% sequence identity) in...