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Science 17 May 2002:
Vol. 296. no. 5571, pp. 1254 - 1258
DOI: 10.1126/science.1067466
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Review

Emerging Roles of Ubiquitin in Transcription Regulation

Ronald C. Conaway,12 Christopher S. Brower,3 Joan Weliky Conaway124*

Ubiquitin is a small protein that was initially found to function as a tag that can be covalently attached to proteins to mark them for destruction by a multisubunit, adenosine 5'-triphosphate-dependent protease called the proteasome. Ubiquitin is now emerging as a key regulator of eukaryotic messenger RNA synthesis, a process that depends on the RNA synthetic enzyme RNA polymerase II and the transcription factors that control its activity. Ubiquitin controls messenger RNA synthesis not only by mechanisms involving ubiquitin-dependent destruction of transcription factors by the proteasome, but also by an intriguing collection of previously unknown and unanticipated mechanisms that appear to be independent of the proteasome.

1 Stowers Institute for Medical Research, Kansas City, MO 64110, USA.
2 Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS 66160, USA.
3 Division of Biology, California Institute of Technology, Pasadena, CA 91125, USA.
4 Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73190, USA.
*   To whom correspondence should be addressed. E-mail: jlc{at}stowers-institute.org

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Polyubiquitination of p53 by a Ubiquitin Ligase Activity of p300.
S. R. Grossman, M. E. Deato, C. Brignone, H. M. Chan, A. L. Kung, H. Tagami, Y. Nakatani, and D. M. Livingston (2003)
Science 300, 342-344
   Abstract »    Full Text »    PDF »
Bone Morphogenetic Proteins, Their Antagonists, and the Skeleton.
E. Canalis, A. N. Economides, and E. Gazzerro (2003)
Endocr. Rev. 24, 218-235
   Abstract »    Full Text »    PDF »
Posttranscriptional and Posttranslational Regulation of C/EBPdelta in G0 Growth-arrested Mammary Epithelial Cells.
L. R. Dearth and J. DeWille (2003)
J. Biol. Chem. 278, 11246-11255
   Abstract »    Full Text »    PDF »
A binding motif for Siah ubiquitin ligase.
C. M. House, I. J. Frew, H.-L. Huang, G. Wiche, N. Traficante, E. Nice, B. Catimel, and D. D. L. Bowtell (2003)
PNAS 100, 3101-3106
   Abstract »    Full Text »    PDF »
The Drosophila trithorax group gene tonalli(tna) interacts genetically with the Brahma remodeling complex and encodes an SP-RING finger protein.
L. Gutierrez, M. Zurita, J. A. Kennison, and M. Vazquez (2003)
Development 130, 343-354
   Abstract »    Full Text »    PDF »
Functional Analysis of Murine Aryl Hydrocarbon (AH) Receptors Defective in Nuclear Import: Impact on AH Receptor Degradation and Gene Regulation.
Z. Song and R. S. Pollenz (2003)
Mol. Pharmacol. 63, 597-606
   Abstract »    Full Text »    PDF »
Protein-Protein Interactions within an E2-RING Finger Complex. IMPLICATIONS FOR UBIQUITIN-DEPENDENT DNA DAMAGE REPAIR.
H. D. Ulrich (2003)
J. Biol. Chem. 278, 7051-7058
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Loss of HR6B Ubiquitin-Conjugating Activity Results in Damaged Synaptonemal Complex Structure and Increased Crossing-Over Frequency during the Male Meiotic Prophase.
W. M. Baarends, E. Wassenaar, J. W. Hoogerbrugge, G. van Cappellen, H. P. Roest, J. Vreeburg, M. Ooms, J. H. J. Hoeijmakers, and J. A. Grootegoed (2003)
Mol. Cell. Biol. 23, 1151-1162
   Abstract »    Full Text »    PDF »
Just how complex is the BrassicaS-receptor complex?.
B. P. Kemp and J. Doughty (2003)
J. Exp. Bot. 54, 157-168
   Abstract »    Full Text »    PDF »
CUL7: A DOC domain-containing cullin selectively binds Skp1{middle dot}Fbx29 to form an SCF-like complex.
D. C. Dias, G. Dolios, R. Wang, and Z.-Q. Pan (2002)
PNAS 99, 16601-16606
   Abstract »    Full Text »    PDF »
Secondary and tertiary structures of gaseous protein ions characterized by electron capture dissociation mass spectrometry and photofragment spectroscopy.
H. Oh, K. Breuker, S. K. Sze, Y. Ge, B. K. Carpenter, and F. W. McLafferty (2002)
PNAS 99, 15863-15868
   Abstract »    Full Text »    PDF »
Involvement of Proteasome in the Dynamic Assembly of the Androgen Receptor Transcription Complex.
Z. Kang, A. Pirskanen, O. A. Janne, and J. J. Palvimo (2002)
J. Biol. Chem. 277, 48366-48371
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Pairs of dipeptides synergistically activate the binding of substrate by ubiquitin ligase through dissociation of its autoinhibitory domain.
F. Du, F. Navarro-Garcia, Z. Xia, T. Tasaki, and A. Varshavsky (2002)
PNAS 99, 14110-14115
   Abstract »    Full Text »    PDF »


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