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Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family

Baker, Rohan T. and Tobias, John W. and Varshavsky, Alexander (1992) Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family. Journal of Biological Chemistry, 267 (32). pp. 23364-23375. ISSN 0021-9258. doi:10.1016/s0021-9258(18)50100-9.

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In eukaryotes, both natural and engineered ubiquitin (Ub) fusions to itself or other proteins are cleaved by processing proteases after the last (Gly76) residue of ubiquitin. YUH1 and UBP1, the genes for two ubiquitin-specific proteases of the yeast Saccharomyces cerevisiae, have been cloned previously and shown to encode nonhomologous proteins. Using an Escherichia coli-based genetic screen, we have isolated two other yeast genes for ubiquitin-specific proteases, named UBP2 and UBP3. Ubp2 (1,264 residues), Ubp3 (912 residues), and the previously cloned Ubp1 (809 residues) are largely dissimilar except for two short regions containing Cys and His which encompass their putative active sites. Neither of these proteases has sequence similarities to Yuh1. Both Ubp2 and the previously identified Ubp1 cleave in vitro at the C terminus of the ubiquitin moiety in natural and engineered fusions irrespective of their size, poly-Ub being the exception. However, both Ubp1 and Ubp2 are also capable of cleaving poly-Ub when coexpressed with it in E. coli, suggesting that such cleavage is largely cotranslational. Although inactive in E. coli extracts, Ubp3 was active with all of the tested ubiquitin fusions except poly-Ub when coexpressed with them in E. coli. Null yuh1 ubp1 ubp2 ubp3 quadruple mutants are viable and retain the ability to deubiquitinate ubiquitin fusions, indicating the presence of at least one more ubiquitin-specific processing protease in S. cerevisiae.

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Varshavsky, Alexander0000-0002-4011-258X
Additional Information:© 1992 American Society for Biochemistry and Molecular Biology. Under an Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0). (Received for publication, May 29, 1992). This work was supported by National Institutes of Health Grants AG08991 and GM31530 (to A. V.). 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. The nucleotide sequence(s) reported in this paper has been submitted to the GenBank TM/EMBL Data Bank with accession number(s) M94916 and M94917. Supported by fellowships from the Life Sciences Research Foundation and the Fulbright Foundation. We are indebted to Tom Shrader and Jürgen Dohmen for assistance with the development of the screen protocol. We thank Barbara Doran for secretarial assistance.
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Life Sciences Research FoundationUNSPECIFIED
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Issue or Number:32
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Official Citation:Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family Baker, R.T. et al. Journal of Biological Chemistry, Volume 267, Issue 32, 23364 - 23375
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:107994
Deposited By: George Porter
Deposited On:10 Feb 2021 23:59
Last Modified:16 Nov 2021 19:08

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