%0 Journal Article
%A Bin HU
%A Hua CHEN
%A Ma YU
%A Mingyue YUAN
%A Tianzhong ZHOU
%A Xiangyu LONG
%T Cloning and Functional Analysis of Deubiquitinating Enzyme Gene UCHs from <i>Hevea brasiliensis</i>
%D 2023
%R 10.7525/j.issn.1673-5102.2023.04.015
%J Bulletin of Botanical Research
%P 622-630
%V 43
%N 4
%X <p>To investigate the potential function of ubiquitin carboxyl terminal hydrolases（UCHs） in the ubiquitination process of laticiferous of <i>Hevea brasiliensis</i>， the full-length sequences of two UCHs family members（<i>HbUCH</i>-<i>L3</i> and <i>HbUCH</i>-<i>L5</i>） were isolated from <i>Hevea brasiliensis</i>， and both had typical UCHs domains. The open reading frame of <i>HbUCH</i>-<i>L3</i> and <i>HbUCH</i>-<i>L5</i> were 993 bp and 558 bp， and encoded 330 and 185 amino acids， respectively. The results of qRT-PCR showed that <i>HbUCH</i>-<i>L3</i> and <i>HbUCH</i>-<i>L5</i> were constitutively expressed in all tissues， but was low in latex. <i>In vitro</i> ubiquitination substrates cleavage of recombinant HbUCHs showed that both HbUCH-L3 and HbUCH-L5 had the function of hydrolyzing ubiquitin. HbUCHs significantly reduced the overall ubiquitination level of C-serum proteins； while， the deubiquitinating activity of HbUCH-L3 was higher than that of HbUCH-L5. Therefore， it was speculated that UCHs played a role in maintaining the dynamic balance of laticiferous ubiquitination and thus played a specific biological function， but the exact mechanism was still unclear.</p>
%U https://bbr.nefu.edu.cn/EN/10.7525/j.issn.1673-5102.2023.04.015