<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Heinkel F</submitter><funding>Gouvernement du Canada | Canadian Institutes of Health Research</funding><funding>CIHR</funding><pagination>16326-16331</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6697873</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>116(33)</volume><pubmed_abstract>Phase separation drives numerous cellular processes, ranging from the formation of membrane-less organelles to the cooperative assembly of signaling proteins. Features such as multivalency and intrinsic disorder that enable condensate formation are found not only in cytosolic and nuclear proteins, but also in membrane-associated proteins. The ABC transporter Rv1747, which is important for &lt;i>Mycobacterium tuberculosis&lt;/i> (&lt;i>Mtb&lt;/i>) growth in infected hosts, has a cytoplasmic regulatory module consisting of 2 phosphothreonine-binding Forkhead-associated domains joined by an intrinsically disordered linker with multiple phospho-acceptor threonines. Here we demonstrate that the regulatory modules of Rv1747 and its homolog in &lt;i>Mycobacterium smegmatis&lt;/i> form liquid-like condensates as a </pubmed_abstract><journal>Proceedings of the National Academy of Sciences of the United States of America</journal><pubmed_title>Phase separation and clustering of an ABC transporter in &lt;i>Mycobacterium tuberculosis&lt;/i>.</pubmed_title><pmcid>PMC6697873</pmcid><funding_grant_id>MOP-136834</funding_grant_id><funding_grant_id>MOP-106622</funding_grant_id><pubmed_authors>Li H</pubmed_authors><pubmed_authors>Gold MR</pubmed_authors><pubmed_authors>Chao J</pubmed_authors><pubmed_authors>Chou KC</pubmed_authors><pubmed_authors>Bach H</pubmed_authors><pubmed_authors>Av-Gay Y</pubmed_authors><pubmed_authors>Bui JM</pubmed_authors><pubmed_authors>McIntosh LP</pubmed_authors><pubmed_authors>Hui LT</pubmed_authors><pubmed_authors>Zhu M</pubmed_authors><pubmed_authors>Ko M</pubmed_authors><pubmed_authors>Abraham L</pubmed_authors><pubmed_authors>Gsponer J</pubmed_authors><pubmed_authors>Heinkel F</pubmed_authors><pubmed_authors>Rogalski JC</pubmed_authors><pubmed_authors>Ling YM</pubmed_authors><pubmed_authors>Scurll J</pubmed_authors><pubmed_authors>Mayor T</pubmed_authors></additional><is_claimable>false</is_claimable><name>Phase separation and clustering of an ABC transporter in &lt;i>Mycobacterium tuberculosis&lt;/i>.</name><description>Phase separation drives numerous cellular processes, ranging from the formation of membrane-less organelles to the cooperative assembly of signaling proteins. Features such as multivalency and intrinsic disorder that enable condensate formation are found not only in cytosolic and nuclear proteins, but also in membrane-associated proteins. The ABC transporter Rv1747, which is important for &lt;i>Mycobacterium tuberculosis&lt;/i> (&lt;i>Mtb&lt;/i>) growth in infected hosts, has a cytoplasmic regulatory module consisting of 2 phosphothreonine-binding Forkhead-associated domains joined by an intrinsically disordered linker with multiple phospho-acceptor threonines. Here we demonstrate that the regulatory modules of Rv1747 and its homolog in &lt;i>Mycobacterium smegmatis&lt;/i> form liquid-like condensates as a </description><dates><release>2019-01-01T00:00:00Z</release><publication>2019 Aug</publication><modification>2025-04-19T19:46:55.013Z</modification><creation>2025-04-19T19:46:55.013Z</creation></dates><accession>S-EPMC6697873</accession><cross_references><pubmed>31366629</pubmed><doi>10.1073/pnas.1820683116</doi></cross_references></HashMap>