The mUBC9 murine ubiquitin conjugating enzyme interacts with the E2A transcription factors

Deborah A. Loveys, Michael B Streiff, Timothy S. Schaefer, Gregory J. Kato

Research output: Contribution to journalArticle

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 languageEnglish (US)
Pages (from-to)169-177
Number of pages9
JournalGene
Volume201
Issue number1-2
DOIs
StatePublished - Nov 12 1997

Fingerprint

Ubiquitin-Conjugating Enzymes
Transcription Factors
Proteins
Complementary DNA
Two-Hybrid System Techniques
Schizosaccharomyces
Sequence Homology
Nuclear Proteins
Ubiquitin
DNA Repair
Proteolysis
DNA Damage
Saccharomyces cerevisiae
Immune Sera
Intercellular Signaling Peptides and Proteins
Cell Cycle
Yeasts
Amino Acids
Enzymes
Serum

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 journalArticle

Loveys, Deborah A. ; Streiff, Michael B ; Schaefer, Timothy S. ; Kato, Gregory J. / The mUBC9 murine ubiquitin conjugating enzyme interacts with the E2A transcription factors. In: Gene. 1997 ; Vol. 201, No. 1-2. pp. 169-177.
@article{d7447d27614549ca9b211a419d6572a0,
title = "The mUBC9 murine ubiquitin conjugating enzyme interacts with the E2A transcription factors",
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.",
keywords = "Cloning, Fusion protein, Protein expression",
author = "Loveys, {Deborah A.} and Streiff, {Michael B} and Schaefer, {Timothy S.} and Kato, {Gregory J.}",
year = "1997",
month = "11",
day = "12",
doi = "10.1016/S0378-1119(97)00444-7",
language = "English (US)",
volume = "201",
pages = "169--177",
journal = "Gene",
issn = "0378-1119",
publisher = "Elsevier",
number = "1-2",

}

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

UR - http://www.scopus.com/inward/record.url?scp=0030782673&partnerID=8YFLogxK

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 -