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KMID : 0624620080410120852
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BMB Reports
2008 Volume.41 No. 12 p.852 ~ p.857
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Direct characterization of E2-dependent target specificity and processivity using an artificial p27-linker-E2 ubiquitination system
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Ryu Kyoung-Seok
Choi Yun-Seok
Ko Jun-Sang
Kim Seong-Ock
Kim Hyun-Jung
Cheong Hae-Kap
Jeon Young-Ho
Choi Byong-Seok
Cheong Chae-Joon
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Abstract
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Little attention has been paid to the specificity between E2 and the target protein during ubiquitination, although RING-E3 induces a potential intra-molecular reaction by mediating the direct transfer of ubiquitin from E2 to the target protein. We have constructed artificial E2 fusion proteins in which a target protein (p27) is tethered to one of six E2s via a flexible linker. Interestingly, only three E2s (UbcH5b, hHR6b, and Cdc34) are able to ubiquitinate p27 via an intra-molecular reaction in this system. Although the first ubiquitination of p27 (p27-Ub) by Cdc34 is less efficient than that of UbcH5b and hHR6b, the additional ubiquitin attachment to p27-Ub by Cdc34 is highly efficient. The E2 core of Cdc34 provides specificity to p27, and the residues 184-196 are required for possessive ubiquitination by Cdc34. We demonstrate direct E2 specificity for p27 and also show that differential ubiquitin linkages can be dependent on E2 alone.
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KEYWORD
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Direct target specificity of E2, p27-E2 fusion protein, Processive ubiquitination, Ubiquitin, Ubiquitin-linkage
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