Cloning, characterization and subcellular localization of a gene encoding a human ubiquitin-conjugating enzyme (E2) homologous to the Arabidopsis thaliana UBC-16 gene product

10.2741/1899 ◽  
2006 ◽  
Vol 11 (1) ◽  
pp. 1500 ◽  
Author(s):  
Gang Yin
Keyword(s):  
Arabidopsis Thaliana ◽  
Subcellular Localization ◽  
Gene Product ◽  
Gene Encoding ◽  
Human Ubiquitin ◽  
Ubiquitin Conjugating Enzyme ◽  
Conjugating Enzyme

Identification, tissue expression, and chromosomal position of a novel gene encoding human ubiquitin-conjugating enzyme E2-230k

Gene ◽  
2001 ◽  
Vol 267 (1) ◽  
pp. 95-100 ◽  
Author(s):  
Takashi Yokota ◽  
Hisaki Nagai ◽  
Haruhito Harada ◽  
Nobuya Mine ◽  
Yoshie Terada ◽  
...  
Keyword(s):  
Tissue Expression ◽  
Gene Encoding ◽  
Chromosomal Position ◽  
Novel Gene ◽  
Human Ubiquitin ◽  
Ubiquitin Conjugating Enzyme ◽  
Conjugating Enzyme

Effect of Arabidopsis COP10 ubiquitin E2 enhancement activity across E2 families and functional conservation among its canonical homologues

2009 ◽  
Vol 418 (3) ◽  
pp. 683-690 ◽  
Author(s):  
On Sun Lau ◽  
Xing Wang Deng
Keyword(s):  
Dna Damage ◽  
Arabidopsis Thaliana ◽  
Plant Development ◽  
Functional Conservation ◽  
Human Ubiquitin ◽  
Ubiquitin Conjugating Enzyme ◽  
Variant Protein ◽  
Conjugating Enzyme

Arabidopsis thaliana COP10 (constitutive photomorphogenic 10) is a UEV [Ub (ubiquitin)-conjugating enzyme (E2) variant protein] that is required for repression of seedling photomorphogenesis in darkness. COP10 forms a complex {the CDD complex [COP10–DET1 (de-etiolated 1)–DDB1 (DNA damage binding protein 1) complex]} with DET1 and DDB1a in vivo and can enhance the activity of Ub-conjugating enzyme (E2) in vitro. To investigate whether COP10 might act as a general regulator of E2s, we tested the specificity of COP10 E2 enhancement activity across E2 families of Arabidopsis. We found that COP10 is capable of enhancing members of four E2 subgroups significantly, while having a milder effect on another. Surprisingly, we found that close canonical E2 homologues of COP10, such as UbcH5a (human ubiquitin-conjugating enzyme 5), are also capable of enhancing E2s. Furthermore, we detected direct interactions between COP10 and three of the enhanced E2s, hinting at a possible mechanism for the enhancements. The present study suggests that some E2s, including the generic Ubc4/5p families involved in many processes, might possess dual activities: the formation of the classic E2–Ub thiol ester and the previously unknown E2 enhancement activity. Therefore COP10, despite being a catalytically inactive E2, might still enhance a variety of E2s and regulate numerous aspects of plant development.

Poly(ADP-ribose) polymerase interacts with a novel human ubiquitin conjugating enzyme: hUbc9

Gene ◽  
1997 ◽  
Vol 190 (2) ◽  
pp. 287-296 ◽  
Author(s):  
Murielle Masson ◽  
Josiane Menissier-de Murcia ◽  
Marie-Geneviève Mattei ◽  
Gilbert de Murcia ◽  
Claude P. Niedergang
Keyword(s):  
Human Ubiquitin ◽  
Ubiquitin Conjugating Enzyme ◽  
Conjugating Enzyme

scholarly journals Mutations in RAD6, a yeast gene encoding a ubiquitin-conjugating enzyme, stimulate retrotransposition.

1990 ◽  
Vol 10 (3) ◽  
pp. 1017-1022 ◽  
Author(s):  
S Picologlou ◽  
N Brown ◽  
S W Liebman
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Fold Increase ◽  
Yeast Gene ◽  
Gene Encoding ◽  
Repair Gene ◽  
Dna Repair Gene ◽  
Ubiquitin Conjugating Enzyme ◽  
First Time ◽  
Conjugating Enzyme

The Saccharomyces cerevisiae DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme which polyubiquitinates histones in vitro. Here we show that mutations in rad6 increase the frequency of transposition of the retrotransposon Ty into the CAN1 and URA3 loci. Using isogenic RAD6 and rad6 strains, we measured a more than 100-fold increase in the spontaneous rate of retrotransposition due to rad6, although there was no increase in the Ty message level. This is the first time that a mutation in a host gene has been shown to result in an increased rate of retrotransposition.

scholarly journals Characterization of functionally independent domains in the human ubiquitin conjugating enzyme UbcH2

FEBS Letters ◽  
1995 ◽  
Vol 377 (2) ◽  
pp. 193-196 ◽  
Author(s):  
Peter Kaiser ◽  
Sonja Mandl ◽  
Manfred Schweiger ◽  
Rainer Schneider
Keyword(s):  
Human Ubiquitin ◽  
Ubiquitin Conjugating Enzyme ◽  
Conjugating Enzyme
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