Identification of Proteassemblin,a Mammalian Homologue of the Yeast Protein,Ump1p,That Is Required for Normal Proteasome Assembly |
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Institution: | 1. William S. Rowe Division of Rheumatology, Children''s Hospital Medical Center, 3333 Burnet Avenue, Cincinnati, Ohio, 45229-3039;2. Department of Molecular Genetics, Howard Hughes Medical Institute, University of Cincinnati School of Medicine, Cincinnati, Ohio, 45267-0524;1. Department of Molecular Science and Nanosystems, Ca’ Foscari University Venice, Scientific Campus, via Torino 155, 30172 Venezia, Italy;2. Department of Chemistry and Chemical Technology, Al-Farabi Kazakh National University, al-Farabi 71, 050038 Almaty, Kazakhstan;1. Program of Natural Product Medicinal Chemistry, Key Laboratory of Plant Resources Conservation and Sustainable Utilization, Guangdong Provincial Key Laboratory of Applied Botany, South China Botanical Garden, Chinese Academy of Sciences, Guangzhou 510650, People’s Republic of China;2. University of Chinese Academy of Sciences, Beijing 100049, People’s Republic of China;3. State Key Laboratory of Chemical Oncogenomics, Peking University Shenzhen Graduate School, Shenzhen 518055, People’s Republic of China;4. School of Materials Science and Engineering, Central South University of Forestry and Technology, Changsha 410004, People’s Republic of China;5. Guangzhou Green Health Biotechnology Co., Ltd., Guangzhou 510070, People’s Republic of China |
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Abstract: | We have identified a mammalian homologue of yeast Ump1p by searching for similar proteins in human and mouse expressed sequence tag (EST) databases. Ump1p is an accessory protein that is required for normal proteasome assembly in yeast (1). A mammalian homologue, which we refer to as “proteassemblin,” is a constituent of proteasome assembly intermediates (preproteasomes), but not fully assembled 20S proteasomes, as is Ump1p in yeast. We also provide evidence that proteassemblin is a constituent of pre-immunoproteasomes that contain the precursor of the interferon-γ-inducible subunit LMP2. By analogy with Ump1p, we hypothesize that proteassemblin is required for normal mammalian proteasome assembly. |
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