Abstract
The ubiquitin-mediated degradation of cellular proteins requires the sequential activity of E1, E2 and, in some cases, E3 enzymes. Using the yeast two-hybrid system, we have cloned 1.0- and 2.5-kb cDNAs encoding the identical murine E2, or ubiquitin conjugating enzyme by virtue of its interaction with the E2A transcription factor. This cDNA encodes the 158-amino-acid protein, mUBC9, which has considerable sequence homology to UBC9 from Saccharomyces cerevisiae and HUS5 from Schizosaccharomyces pombe and is identical to the human UBC9 protein. HUS5 is essential for DNA damage repair, whereas UBC9 is necessary for G2/M progression. The human protein has been shown to correct the UBC9 defect in yeast. Antisera raised against bacterially expressed mUBC9 fusion protein recognize a murine cellular protein of approximately 18 kDa, corresponding to the predicted mobility. Unlike E2A, the mUBC9 protein level is not regulated by serum growth factors. The activity of the apparent homologues UBC9 and HUS5 suggests that mUBC9 may be involved in the degradation of key nuclear proteins that regulate cell cycle progression.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 169-177 |
| Number of pages | 9 |
| Journal | Gene |
| Volume | 201 |
| Issue number | 1-2 |
| DOIs | |
| State | Published - Nov 12 1997 |
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Keywords
- Cloning
- Fusion protein
- Protein expression
ASJC Scopus subject areas
- Genetics
Cite this
The mUBC9 murine ubiquitin conjugating enzyme interacts with the E2A transcription factors. / Loveys, Deborah A.; Streiff, Michael B; Schaefer, Timothy S.; Kato, Gregory J.
In: Gene, Vol. 201, No. 1-2, 12.11.1997, p. 169-177.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The mUBC9 murine ubiquitin conjugating enzyme interacts with the E2A transcription factors
AU - Loveys, Deborah A.
AU - Streiff, Michael B
AU - Schaefer, Timothy S.
AU - Kato, Gregory J.
PY - 1997/11/12
Y1 - 1997/11/12
N2 - The ubiquitin-mediated degradation of cellular proteins requires the sequential activity of E1, E2 and, in some cases, E3 enzymes. Using the yeast two-hybrid system, we have cloned 1.0- and 2.5-kb cDNAs encoding the identical murine E2, or ubiquitin conjugating enzyme by virtue of its interaction with the E2A transcription factor. This cDNA encodes the 158-amino-acid protein, mUBC9, which has considerable sequence homology to UBC9 from Saccharomyces cerevisiae and HUS5 from Schizosaccharomyces pombe and is identical to the human UBC9 protein. HUS5 is essential for DNA damage repair, whereas UBC9 is necessary for G2/M progression. The human protein has been shown to correct the UBC9 defect in yeast. Antisera raised against bacterially expressed mUBC9 fusion protein recognize a murine cellular protein of approximately 18 kDa, corresponding to the predicted mobility. Unlike E2A, the mUBC9 protein level is not regulated by serum growth factors. The activity of the apparent homologues UBC9 and HUS5 suggests that mUBC9 may be involved in the degradation of key nuclear proteins that regulate cell cycle progression.
AB - The ubiquitin-mediated degradation of cellular proteins requires the sequential activity of E1, E2 and, in some cases, E3 enzymes. Using the yeast two-hybrid system, we have cloned 1.0- and 2.5-kb cDNAs encoding the identical murine E2, or ubiquitin conjugating enzyme by virtue of its interaction with the E2A transcription factor. This cDNA encodes the 158-amino-acid protein, mUBC9, which has considerable sequence homology to UBC9 from Saccharomyces cerevisiae and HUS5 from Schizosaccharomyces pombe and is identical to the human UBC9 protein. HUS5 is essential for DNA damage repair, whereas UBC9 is necessary for G2/M progression. The human protein has been shown to correct the UBC9 defect in yeast. Antisera raised against bacterially expressed mUBC9 fusion protein recognize a murine cellular protein of approximately 18 kDa, corresponding to the predicted mobility. Unlike E2A, the mUBC9 protein level is not regulated by serum growth factors. The activity of the apparent homologues UBC9 and HUS5 suggests that mUBC9 may be involved in the degradation of key nuclear proteins that regulate cell cycle progression.
KW - Cloning
KW - Fusion protein
KW - Protein expression
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UR - http://www.scopus.com/inward/citedby.url?scp=0030782673&partnerID=8YFLogxK
U2 - 10.1016/S0378-1119(97)00444-7
DO - 10.1016/S0378-1119(97)00444-7
M3 - Article
C2 - 9409784
AN - SCOPUS:0030782673
VL - 201
SP - 169
EP - 177
JO - Gene
JF - Gene
SN - 0378-1119
IS - 1-2
ER -