MCB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Chupreta, S.
Right arrow Articles by Iñiguez-Lluhí, J. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chupreta, S.
Right arrow Articles by Iñiguez-Lluhí, J. A.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, May 2005, p. 4272-4282, Vol. 25, No. 10
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.10.4272-4282.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

A Small Conserved Surface in SUMO Is the Critical Structural Determinant of Its Transcriptional Inhibitory Properties

Sergey Chupreta,{dagger} Sam Holmstrom,{dagger} Lalitha Subramanian, and Jorge A. Iñiguez-Lluhí*

Department of Pharmacology, University of Michigan Medical School, Ann Arbor, Michigan 48109-0632

Received 13 November 2004/ Returned for modification 30 December 2004/ Accepted 16 February 2005

Small ubiquitin-like modifier (SUMO) modification of sequence-specific transcription factors has profound regulatory consequences. By providing an intrinsic inhibitory function, SUMO isoforms can suppress transcriptional activation, particularly at promoters harboring multiple response elements. Through a comprehensive structure-function analysis, we have identified a single critical sector along the second beta sheet and the following alpha helix of SUMO2. This distinct surface is defined by four basic residues (K33, K35, K42, R50) that surround a shallow pocket lined by aliphatic (V30, I34) and polar (T38) residues. Substitutions within this area specifically and dramatically affected the ability of both SUMO2 and SUMO1 to inhibit transcription and revealed that the positively charged nature of the key basic residues is the main feature responsible for their functional role. This highly conserved surface accounts for the inhibitory properties of SUMO on multiple transcription factors and promoter contexts and likely defines the interaction surface for the corepressors that mediate the inhibitory properties of SUMO.


* Corresponding author. Mailing address: Department of Pharmacology, University of Michigan Medical School, 1301 MSRBIII, Ann Arbor, MI 48109-0632. Phone: (734) 625-6565. Fax: (734) 763-4450. E-mail: iniguez{at}umich.edu.

{dagger} S.C. and S.H. contributed equally to this work.


Molecular and Cellular Biology, May 2005, p. 4272-4282, Vol. 25, No. 10
0022-538X/05/$08.00+0     doi:10.1128/MCB.25.10.4272-4282.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 2005 by the American Society for Microbiology. All rights reserved.