Characterisation of human RING finger protein TRIM69, a novel testis E3 ubiquitin ligase and its subcellular localisation

Yongqing Han; Rong Li; Jinlan Gao; Shiying Miao; Linfang Wang

doi:10.1016/j.bbrc.2012.10.109

Characterisation of human RING finger protein TRIM69, a novel testis E3 ubiquitin ligase and its subcellular localisation

Biochem Biophys Res Commun. 2012 Dec 7;429(1-2):6-11. doi: 10.1016/j.bbrc.2012.10.109. Epub 2012 Nov 3.

Authors

Yongqing Han¹, Rong Li, Jinlan Gao, Shiying Miao, Linfang Wang

Affiliation

¹ State Key Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences, Peking Union Medical College, Tsinghua University, Beijing 100005, China.

PMID: 23131556
DOI: 10.1016/j.bbrc.2012.10.109

Abstract

The E3 ubiquitin ligase activity and subcellular localisation of human TRIM69 (hTRIM69) gene were studied. It was found that hTRIM69 mediated ubiquitination in an E2 conjugating enzyme selective fashion in vitro and an intact RING finger domain was indispensible for the process. Further evidences showed that hTRIM69 could mediate ubiquitination in vivo, which could be enhanced by a proteasome inhibitor. hTRIM69 was found to localise in both the cytoplasm and the nucleus in a speckled aggregating pattern, which also required an intact RING finger domain. Collectively, hTRIM69 is a novel E3 ubiquitin ligase identified from human testis and may function to ubiquitinate its particular substrates during spermatogenesis.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Catalysis
HEK293 Cells
HeLa Cells
Humans
Intracellular Space / enzymology
Male
RING Finger Domains*
Spermatogenesis*
Testis / enzymology*
Tripartite Motif Proteins
Ubiquitin-Protein Ligases / genetics
Ubiquitin-Protein Ligases / metabolism*
Ubiquitination

Substances

Tripartite Motif Proteins
TRIM69 protein, human
Ubiquitin-Protein Ligases