Person: Mintseris, Julian
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Mintseris
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Julian
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Mintseris, Julian
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Publication Drosophila Protein interaction Map (DPiM): A paradigm for metazoan protein complex interactions(Landes Bioscience, 2012) Guruharsha, K.G.; Obar, Robert; Mintseris, Julian; Aishwarya, K.; Krishnan, R.T.; VijayRaghavan, K.; Artavanis-Tsakonas, SpyrosProteins perform essential cellular functions as part of protein complexes, often in conjunction with RNA, DNA, metabolites and other small molecules. The genome encodes thousands of proteins but not all of them are expressed in every cell type; and expressed proteins are not active at all times. Such diversity of protein expression and function accounts for the level of biological intricacy seen in nature. Defining protein-protein interactions in protein complexes, and establishing the when, what and where of potential interactions, is therefore crucial to understanding the cellular function of any protein—especially those that have not been well studied by traditional molecular genetic approaches. We generated a large-scale resource of affinity-tagged expression-ready clones and used co-affinity purification combined with tandem mass-spectrometry to identify protein partners of nearly 5,000 Drosophila melanogaster proteins. The resulting protein complex “map” provided a blueprint of metazoan protein complex organization. Here we describe how the map has provided valuable insights into protein function in addition to generating hundreds of testable hypotheses. We also discuss recent technological advancements that will be critical in addressing the next generation of questions arising from the map.Publication Prokayrotic Ubiquitin-Like Protein (Pup) Proteome of Mycobacterium tuberculosis(Public Library of Science, 2010) Festa, Richard A.; McAllister, Fiona Elizabeth; Pearce, Michael J.; Mintseris, Julian; Burns, Kristin E.; Gygi, Steven; Darwin, K. HeranProkaryotic ubiquitin-like protein (Pup) in Mycobacterium tuberculosis (Mtb) is the first known post-translational small protein modifier in prokaryotes, and targets several proteins for degradation by a bacterial proteasome in a manner akin to ubiquitin (Ub) mediated proteolysis in eukaryotes. To determine the extent of pupylation in Mtb, we used tandem affinity purification to identify its “pupylome”. Mass spectrometry identified 55 out of 604 purified proteins with confirmed pupylation sites. Forty-four proteins, including those with and without identified pupylation sites, were tested as substrates of proteolysis in Mtb. Under steady state conditions, the majority of the test proteins did not accumulate in degradation mutants, suggesting not all targets of pupylation are necessarily substrates of the proteasome under steady state conditions. Four proteins implicated in Mtb pathogenesis, Icl (isocitrate lyase), Ino1 (inositol-1-phosphate synthase), MtrA (Mtb response regulator A) and PhoP (phosphate response regulator P), showed altered levels in degradation defective Mtb. Icl, Ino1 and MtrA accumulated in Mtb degradation mutants, suggesting these proteins are targeted to the proteasome. Unexpectedly, PhoP was present in wild type Mtb but undetectable in the degradation mutants. Taken together, these data demonstrate that pupylation regulates numerous proteins in Mtb and may not always lead to degradation.Publication DPP9 sequesters the C terminus of NLRP1 to repress inflammasome activation(Springer Science and Business Media LLC, 2021-03-17) Hollingsworth, L. Robert; Sharif, Humayun; Griswold, Andrew; Fontana, Pietro; Mintseris, Julian; Dagbay, Kevin B.; Paulo, Joao A.; Gygi, Steven; Bachovchin, Daniel A.; Wu, Hao