Catálogo de publicaciones - revistas

<jats:title>Tethering DNA for packing purposes</jats:title> <jats:p> Condensin protein complexes are critical for chromosome segregation and compaction. They form ring-shaped structures that encircle and topologically constrain DNA strands. Wang <jats:italic>et al.</jats:italic> show that <jats:italic>Bacillus subtilis</jats:italic> condensin complexes hold the two arms of the circular chromosome together (see the Perspective by Sherratt). The complexes seem to do this by encircling individual DNA duplexes and then tethering the two duplexes together by “handcuffing.” The complexes actively travel along the DNA and function to enlarge DNA loops processively, leading to chromosome compaction. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6324" page="524" related-article-type="in-this-issue" vol="355" xlink:href="10.1126/science.aai8982">524</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6324" page="460" related-article-type="in-this-issue" vol="355" xlink:href="10.1126/science.aam7183">460</jats:related-article> </jats:p>

<jats:title>The yeast mitoribosome</jats:title> <jats:p> Mitochondria are eukaryotic organelles that produce ATP, the energy source of the cell. They have dedicated ribosomes (mitoribosomes) that encode some of the membrane proteins that are essential to ATP production. Desai <jats:italic>et al.</jats:italic> present a high-resolution structure of the 75-component yeast mitoribosome, determined by electron cryomicroscopy. Mitoribosomes share an ancestor with modern bacterial ribosomes. Comparing the structure of the yeast mitoribosome with mammalian mitoribosomes suggests how they have evolved differently to perform species-specific functions. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6324" page="528" related-article-type="in-this-issue" vol="355" xlink:href="10.1126/science.aal2415">528</jats:related-article> </jats:p>

<jats:p> A range of cloud-based tools—collectively known as the “Internet of Things” (IoT)—can connect everything in a lab, from research protocols and pipettes to data storage and manuscripts. As these tools get easier to use and data become more secure on them, an increasing number of scientists and companies will likely take advantage of complete connectivity. <jats:list list-type="bullet"> <jats:list-item> <jats:p> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="uri" xlink:href="http://www.sciencemag.org/custom-publishing/technology-features/companies-cloud-digitizing-lab-operations">Read the Feature (Full-Text HTML)</jats:ext-link> </jats:p> </jats:list-item> <jats:list-item> <jats:p> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="uri" xlink:href="http://www.sciencemag.org/sites/default/files/custom-publishing/documents/3FebDigitalLabTechFeature.pdf">Read the Feature (PDF)</jats:ext-link> </jats:p> </jats:list-item> <jats:list-item> <jats:p> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="uri" xlink:href="http://www.sciencemag.org/sites/default/files/custom-publishing/douments/3-Feb-New-Products.pdf">Read New Products (PDF)</jats:ext-link> </jats:p> </jats:list-item> </jats:list> </jats:p>

<jats:p>A weekly roundup of information on newly offered instrumentation, apparatus, and laboratory materials of potential interest to researchers.</jats:p>