{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,3]],"date-time":"2026-03-03T05:20:20Z","timestamp":1772515220418,"version":"3.50.1"},"reference-count":65,"publisher":"Wiley","issue":"17","license":[{"start":{"date-parts":[[2025,2,22]],"date-time":"2025-02-22T00:00:00Z","timestamp":1740182400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2025,9]]},"abstract":"<jats:p>\n                    The assembly of the 26S proteasome, a multi\u2010subunit complex for regulated protein turnover, proceeds via the formation of intermediates.\n                    <jats:italic>Giardia lamblia<\/jats:italic>\n                    does not encode proteasome regulatory subunit Rpn12 or proteasome complex subunit Sem1, two proteins crucial for assembling the proteasome lid. To understand how the interactions between the giardial proteasome lid subunits may have changed to compensate for their absence, we used yeast two\u2010hybrid to generate a binary interactome map of\n                    <jats:italic>Giardia<\/jats:italic>\n                    's lid subunits. Most interactions within the\n                    <jats:italic>Giardia<\/jats:italic>\n                    lid are stronger than\n                    <jats:italic>Saccharomyces cerevisiae<\/jats:italic>\n                    lid, which may compensate for Rpn12 and Sem1 absence. A notable exception was the weaker interaction between the two non\u2010ATPase lid subunits, GlRpn11 and GlRpn8, compared to the strong interaction between yeast orthologs Rpn11 and Rpn8. The Rpn11\u2013Rpn8 dimer provides a platform for lid assembly. Their interaction involves the insertion of a methionine residue of Rpn11 into a hydrophobic pocket of Rpn8. Molecular modeling indicates that GlRpn8's pocket is wider, reconciling the experimental observation of its weak interaction with GlRpn11. This weaker interaction may have evolved to support proteasome\u2010independent functions of GlRpn11, which localizes to multiple subcellular regions, including the mitosomes, where other proteasome subunits cannot be detected. Functional complementation in yeast shows that GlRpn11 can influence mitochondrial function and distribution. Together these observations show that GlRpn11 functions at the mitosome. Thus, this parasite's proteasome lid has a simpler subunit architecture than that of yeast with structural attributes to support dual functionalities for GlRpn11. Such parasite\u2010specific proteasome features provide opportunities for controlling parasite transmission.\n                  <\/jats:p>","DOI":"10.1111\/febs.70027","type":"journal-article","created":{"date-parts":[[2025,2,22]],"date-time":"2025-02-22T03:11:03Z","timestamp":1740193863000},"page":"4591-4610","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Binary protein interactome mapping of the\n                    <i>Giardia lamblia<\/i>\n                    proteasome lid reveals extra proteasomal functions of\n                    <scp>GlRpn11<\/scp>"],"prefix":"10.1111","volume":"292","author":[{"given":"Ankita","family":"Das","sequence":"first","affiliation":[{"name":"Department of Biological Sciences Bose Institute  Kolkata India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Atrayee","family":"Ray","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences Bose 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