| First Author | Gong L | Year | 1999 |
| Journal | J Biol Chem | Volume | 274 |
| Issue | 17 | Pages | 12036-42 |
| PubMed ID | 10207026 | Mgi Jnum | J:54622 |
| Mgi Id | MGI:1335620 | Doi | 10.1074/jbc.274.17.12036 |
| Citation | Gong L, et al. (1999) Identification of the activating and conjugating enzymes of the NEDD8 conjugation pathway. J Biol Chem 274(17):12036-42 |
| abstractText | NEDD8 is a ubiquitin-like molecule that can be covalently conjugated to a limited number of cellular proteins, such as Cdc53/cullin. We have previously reported that the C terminus of NEDD8 is efficiently processed to expose Gly-76, which is required for conjugation to target proteins. A combination of data base searches and polymerase chain reaction cloning was used to identify a cDNA encoding human UBA3, which is 38% identical to the yeast homologue, 22% identical to human UBA2, and 19% identical to the C-terminal region of human UBE1. The human UBA3 gene is located on chromosome 3p13 and gave rise to a 2.2-kilobase pair transcript that was detected in all tissues. Human UBA3 could be precipitated with glutathione S-transferase (GST)-NEDD8, but not with GST-ubiquitin or GST-sentrin-1. Moreover, human UBA3 could form a beta- mercaptoethanol-sensitive conjugate with NEDD8 in the presence of APP- BP1, a protein with sequence homology to the N-terminal half of ubiquitin-activating enzyme. We have also cloned human UBC12 and demonstrated that it could form a thiol ester linkage with NEDD8 in the presence of the activating enzyme complex. Identification of the activating and conjugating enzymes of the NEDD8 conjugation pathway should allow for a more detailed study of the role of NEDD8 modification in health and disease. |
