资源环境科技发展态势分析平台

Massive disk galaxies like the Milky Way are expected to form at late times in traditional models of galaxy formation(1,2), but recent numerical simulations suggest that such galaxies could form as early as a billion years after the Big Bang through the accretion of cold material and mergers(3,4). Observationally, it has been difficult to identify disk galaxies in emission at high redshift(5,6) in order to discern between competing models of galaxy formation. Here we report imaging, with a resolution of about 1.3 kiloparsecs, of the 158-micrometre emission line from singly ionized carbon, the far-infrared dust continuum and the near-ultraviolet continuum emission from a galaxy at a redshift of 4.2603, identified by detecting its absorption of quasar light. These observations show that the emission arises from gas inside a cold, dusty, rotating disk with a rotational velocity of about 272 kilometres per second. The detection of emission from carbon monoxide in the galaxy yields a molecular mass that is consistent with the estimate from the ionized carbon emission of about 72 billion solar masses. The existence of such a massive, rotationally supported, cold disk galaxy when the Universe was only 1.5 billion years old favours formation through either cold-mode accretion or mergers, although its large rotational velocity and large content of cold gas remain challenging to reproduce with most numerical simulations(7,8).

A massive rotating disk galaxy was formed a mere 1.5 billion years after the Big Bang, a surprisingly short time after the origin of the Universe.

A CRISPR-based screening platform was used to identify previously uncharacterized genes that regulate the regulatory T cell-specific master transcription factor Foxp3, indicating that this screening method may be broadly applicable for the discovery of other genes involved in autoimmunity and immune responses to cancer.

The chromatin-remodelling complex SWI/SNF is highly conserved and has critical roles in various cellular processes, including transcription and DNA-damage repair(1,2). It hydrolyses ATP to remodel chromatin structure by sliding and evicting histone octamers(3-8), creating DNA regions that become accessible to other essential factors. However, our mechanistic understanding of the remodelling activity is hindered by the lack of a high-resolution structure of complexes from this family. Here we report the cryo-electron microscopy structure of Saccharomyces cerevisiae SWI/SNF bound to a nucleosome, at near-atomic resolution. In the structure, the actin-related protein (Arp) module is sandwiched between the ATPase and the rest of the complex, with the Snf2 helicase-SANT associated (HSA) domain connecting all modules. The body contains an assembly scaffold composed of conserved subunits Snf12 (also known as SMARCD or BAF60), Snf5 (also known as SMARCB1, BAF47 or INI1) and an asymmetric dimer of Swi3 (also known as SMARCC, BAF155 or BAF170). Another conserved subunit, Swi1 (also known as ARID1 or BAF250), resides in the core of SWI/SNF, acting as a molecular hub. We also observed interactions between Snf5 and the histones at the acidic patch, which could serve as an anchor during active DNA translocation. Our structure enables us to map and rationalize a subset of cancer-related mutations in the human SWI/SNF complex and to propose a model for how SWI/SNF recognizes and remodels the +1 nucleosome to generate nucleosome-depleted regions during gene activation(9).

The cryo-electron microscopy structure of the yeast SWI/SNF complex bound to a nucleosome substrate provides insights into the chromatin-remodelling function of this family of protein complexes and suggests mechanisms by which the mutated proteins may cause cancer.