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J. Biol. Chem., Vol. 282, Issue 8, 5256-5262, February 23, 2007

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Two Novel Ubiquitin-fold Modifier 1 (Ufm1)-specific Proteases, UfSP1 and UfSP2^*

Sung Hwan Kang, Gi Ryang Kim¹, Minu Seong¹, Sung Hee Baek, Jae Hong Seol, Ok Sun Bang, Huib Ovaa, Kanako Tatsumi^¶, Masaaki Komatsu^¶, Keiji Tanaka^¶, and Chin Ha Chung²

From the School of Biological Sciences, Seoul National University, Seoul 151-742, Korea, the Division of Cellular Biochemistry, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, the Netherlands, and the ^¶Laboratory of Frontier Science, Tokyo Metropolitan Institute of Medical Science, Bunkyo-ku, Tokyo 113-8613, Japan

Ubiquitin-fold modifier 1 (Ufm1) is a recently identified new ubiquitin-like protein, whose tertiary structure displays a striking resemblance to ubiquitin. Similar to ubiquitin, it has a Gly residue conserved across species at the C-terminal region with extensions of various amino acid sequences that need to be processed in vivo prior to conjugation to target proteins. Here we report the isolation, cloning, and characterization of two novel mouse Ufm1-specific proteases, named UfSP1 and UfSP2. UfSP1 and UfSP2 are composed of 217 and 461 amino acids, respectively, and they have no sequence homology with previously known proteases. UfSP2 is present in most, if not all, of multicellular organisms including plant, nematode, fly, and mammal, whereas UfSP1 could not be found in plant and nematode upon data base search. UfSP1 and UfSP2 cleaved the C-terminal extension of Ufm1 but not that of ubiquitin or other ubiquitin-like proteins, such as SUMO-1 and ISG15. Both were also capable of releasing Ufm1 from Ufm1-conjugated cellular proteins. They were sensitive to inhibition by sulfhydryl-blocking agents, such as N-ethylmaleimide, and their active site Cys could be labeled with Ufm1-vinylmethylester. Moreover, replacement of the conserved Cys residue by Ser resulted in a complete loss of the UfSP1 and UfSP2 activities. These results indicate that UfSP1 and UfSP2 are novel thiol proteases that specifically process the C terminus of Ufm1.

Received for publication, November 15, 2006 , and in revised form, December 20, 2006.

^* This work was supported by grants from the Korea Research Foundation (Grant KRF-2005-084-C00025) and the Korea Science and Engineering Foundation (Grant M10533010001-05N3301-00100) (to C. H. C.) and by a VIDI grant from the Netherlands Foundation for Scientific Research (to H. O.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Recipients of a fellowship from the BK21 Program.

² To whom correspondence should be addressed. Tel.: 82-2-880-6693; Fax: 82-2-871-9193; E-mail: chchung{at}snu.ac.kr.

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				B. H. Ha, H.-C. Ahn, S. H. Kang, K. Tanaka, C. H. Chung, and E. E. Kim Structural Basis for Ufm1 Processing by UfSP1 J. Biol. Chem., May 23, 2008; 283(21): 14893 - 14900. [Abstract] [Full Text] [PDF]