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Originally pyblished by Stanford University , on September 21, 2024 Cells before and after TRAMs were introduced. TRAMs link a shuttle protein (red), and a target protein (green). Without the TRAM, the target protein resides in the nucleus (left), and upon TRAM treatment, the target protein is pulled into the cytoplasm by the shuttle protein (right). Credit: Steven Banik and Christine Ng Cells are highly controlled spaces that rely on every protein being in the right place . Many diseases , including cancers and neurodegenerative disorders, are associated with misplaced proteins . In some cancers , for instance, a protein that normally stands watch over DNA replicating in the nucleus is sent far from the DNA it is meant to monitor, allowing cancers to grow. Steven Banik, assistant professor of chemistry in the School of Humanities and Sciences and institute scholar at Sarafan ChEM-H at Stanford University , and his lab have developed a new method to help force misplaced prote

Originally published by by Rose Miyatsu, University of California - Santa Cruz , on May 11, 2024 Shown is the splicing pathway. The pre-messenger RNA (pre-mRNA) has exons (blue) and introns (pink). The spliceosome (not shown) was known to catalyze two chemical reactions (black arrows) in a two-step process (green arrows labeled 1 and 2) that splice the exons together and removes the intron as a lariat. This study demonstrates that after splicing is finished, the spliceosome is still active and can convert the lariat intron into a circle using a third reaction (green arrow 3) marked by an asterix. Credit: Manuel Ares, UC Santa Cruz Although you may not appreciate them, or have even heard of them, throughout your body , countless microscopic machines called spliceosomes are hard at work . As you sit and read, they are faithfully and rapidly putting back together the broken information in your genes by removing sequences called " introns " so that your messenger RNAs can

Originally published by Kyoto University, on February 28,2024   'epidecodeR' is a tool that can streamline the analysis of complex epigenome and epitranscriptome data, allowing for the rapid and accurate prediction of the effects of epimarks on gene expression. Credit: Mindy Takamiya/Kyoto University iCeMS Scientists have extensively researched the structure and sequence of genetic material and its interactions with proteins in the hope of understanding h ow our genetics and environment interact with diseases . This research has partly focused on ' epigenetic marks ,' which are chemical modifications to DNA, RNA , and the associated proteins (known as histones ). Epigenetic marks influence when and how genes get switched on or off . They can also instruct cells about how to interpret and use genetic information , influencing various cellular processes. Changes in epigenetic marks, therefore, significantly impact gene regulation and cellular functions, which mea

Originally published by Olivia Dimmer, Northwestern University, on November 17, 2023   taRNAs built from an array of IRESs increase reporter gene translation. Credit: Nature Communications (2023). DOI: 10.1038/s41467-023-42252-z A new molecular technology capable of binding to mRNA and regulating gene expression may offer a new avenue for treating diseases caused by haploinsufficiency , or the absence of one functional gene copy, according to a study published in Nature Communications . Messenger RNA, or mRNA , contains instructions for DNA to produce proteins. Many diseases , including cancer and many genetic disorders, result from insufficient gene —and therefore protein—expression, but few strategies exist to correct that kind of dysregulation at a molecular level. The new technology, dubbed "translation-activating RNAs" ( taRNAs ), consists of small molecules programmed to attach to specific mRNA molecules to directly control their translation into proteins,

  Originally published by Rohini Subrahmanyam, PhD, on Apr 20, 2023 Researchers repurpose tiny bacterial injection systems to specifically inject a wide variety of proteins into human cells and living mice. S ophisticated, e ffective drugs to treat diseases and other conditions aren’t any good if they can’t reach the part of the body or the specific cells that they’re designed to target. However, scientists have found a new way to deliver tiny proteins into specific cells, using small syringelike structures naturally found on certain bacteria . The study, published in Nature on March 29, could lead to better drug-delivery systems in medicine. “Delivery remains a critical bottleneck in medicine,” said study coauthor and MIT researcher Joseph Kreitz . “Although many powerful new therapies have been developed over the past several decades, we will need a deep bench of options to get these therapies into the right cells in the body.” In the study, Kreitz, Broad Institute r