title: The MPN domain of Caenorhabditis elegans UfSP modulates both substrate recognition and deufmylation activity.
abstract: Ubiquitin-fold modifier 1 (Ufm1) specific protease (UfSP) is a novel cysteine protease that activates Ufm1 from its precursor by processing the C-terminus to expose the conserved Gly necessary for substrate conjugation and de-conjugates Ufm1 from the substrate. There are two forms: UfSP1 and UfSP2, the later with an additional domain at the N-terminus. Ufm1 and both the conjugating and deconjugating enzymes are highly conserved. However, in Caenorhabditis elegans there is one UfSP which has extra 136 residues at the N terminus compared to UfSP2. The crystal structure of cUfSP reveals that these additional residues display a MPN fold while the rest of the structure mimics that of UfSP2. The MPN domain does not have the metalloprotease activity found in some MPN-domain containing protein, rather it is required for the recognition and deufmylation of the substrate of cUfSP, UfBP1. In addition, the MPN domain is also required for localization to the endoplasmic reticulum.
authors.affiliation: Biomedical Research Institute, Korea Institute of Science and Technology, Seoul 136-791, Republic of Korea.
authors.forename: Byung Hak
authors.initials: BH
authors.lastname: Ha
authors.affiliation: Biomedical Research Institute, Korea Institute of Science and Technology, Seoul 136-791, Republic of Korea; College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Republic of Korea.
authors.forename: Kyung Hee
authors.initials: KH
authors.lastname: Kim
authors.affiliation: School of Biological Sciences, Seoul National University, Seoul 151-742, Republic of Korea.
authors.forename: Hee Min
authors.initials: HM
authors.lastname: Yoo
authors.affiliation: College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Republic of Korea.
authors.forename: Weontae
authors.initials: W
authors.lastname: Lee
authors.affiliation: Biomedical Research Institute, Korea Institute of Science and Technology, Seoul 136-791, Republic of Korea. Electronic address: eunice@kist.re.kr.
authors.forename: Eunice
authors.initials: E
authors.lastname: EunKyeong Kim
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D017173:Caenorhabditis elegans / Q000201:enzymology* / Q000235:genetics; D029742:Caenorhabditis elegans Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D018360:Crystallography, X-Ray; D057056:Cysteine Proteases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000201:enzymology; D057809:HEK293 Cells; D006801:Humans; D008958:Models, Molecular; D017510:Protein Folding; D054730:Protein Interaction Domains and Motifs; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013379:Substrate Specificity; D014452:Ubiquitins / Q000378:metabolism
chemical_list: D029742:Caenorhabditis elegans Proteins; D011994:Recombinant Proteins; C000617999:UFM-1 protein, C elegans; D014452:Ubiquitins; D057056:Cysteine Proteases
keywords: Crystal structure; Deufmylation; MPN domain; UfSP; Ufm1