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 Ross, E. D.
Right arrow Articles by Maher, L. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ross, E. D.
Right arrow Articles by Maher, L. J., III

 Previous Article  |  Next Article 

Molecular and Cellular Biology, October 2001, p. 6598-6605, Vol. 21, No. 19
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.19.6598-6605.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

HMG Proteins and DNA Flexibility in Transcription Activation

Eric D. Ross, Philip R. Hardwidge, and L. James Maher III*

Department of Biochemistry and Molecular Biology, Mayo Foundation, Rochester Minnesota 55905

Received 18 April 2001/Returned for modification 31 May 2001/Accepted 27 June 2001

The relative stiffness of naked DNA is evident from measured values of longitudinal persistence length (~150 bp) and torsional persistence length (~180 bp). These parameters predict that certain arrangements of eukaryotic transcription activator proteins in gene promoters should be much more effective than others in fostering protein-protein interactions with the basal RNA polymerase II transcription apparatus. Thus, if such interactions require some kind of DNA looping, DNA loop energies should depend sensitively on helical phasing of protein binding sites, loop size, and intrinsic DNA curvature within the loop. Using families of artificial transcription templates where these parameters were varied, we were surprised to find that the degree of transcription activation by arrays of Gal4-VP1 transcription activators in HeLa cell nuclear extract was sensitive only to the linear distance separating a basal promoter from an array of bound activators on DNA templates. We now examine the hypothesis that this unexpected result is due to factors in the extract that act to enhance apparent DNA flexibility. We demonstrate that HeLa cell nuclear extract is rich in a heat-resistant activity that dramatically enhances apparent DNA longitudinal and torsional flexibility. Recombinant mammalian high-mobility group 2 (HMG-2) protein can substitute for this activity. We propose that the abundance of HMG proteins in eukaryotic nuclei provides an environment in which DNA is made sufficiently flexible to remove many constraints on protein binding site arrangements that would otherwise limit efficient transcription activation to certain promoter geometries.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, Mayo Foundation, 200 First St., SW, Rochester, MN 55905. Phone: (507) 284-9041. Fax: (507) 284-2053. E-mail: maher{at}mayo.edu.

Molecular and Cellular Biology, October 2001, p. 6598-6605, Vol. 21, No. 19
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.19.6598-6605.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Zhang, J., McCauley, M. J., Maher, L. J. III, Williams, M. C., Israeloff, N. E. (2009). Mechanism of DNA flexibility enhancement by HMGB proteins. Nucleic Acids Res 37: 1107-1114 [Abstract] [Full Text]  
  • Becker, N. A., Kahn, J. D., Maher, L. J. III (2008). Eukaryotic HMGB proteins as replacements for HU in E. coli repression loop formation. Nucleic Acids Res 36: 4009-4021 [Abstract] [Full Text]  
  • Becker, N. A., Kahn, J. D., Maher, L. J. III (2007). Effects of nucleoid proteins on DNA repression loop formation in Escherichia coli. Nucleic Acids Res 0: gkm419v2-13 [Abstract] [Full Text]  
  • Petrascheck, M., Escher, D., Mahmoudi, T., Verrijzer, C. P., Schaffner, W., Barberis, A. (2005). DNA looping induced by a transcriptional enhancer in vivo. Nucleic Acids Res 33: 3743-3750 [Abstract] [Full Text]  
  • Das, D., Peterson, R. C., Scovell, W. M. (2004). High Mobility Group B Proteins Facilitate Strong Estrogen Receptor Binding to Classical and Half-Site Estrogen Response Elements and Relax Binding Selectivity. Mol. Endocrinol. 18: 2616-2632 [Abstract] [Full Text]  
  • Biswas, D., Imbalzano, A. N., Eriksson, P., Yu, Y., Stillman, D. J. (2004). Role for Nhp6, Gcn5, and the Swi/Snf Complex in Stimulating Formation of the TATA-Binding Protein-TFIIA-DNA Complex. Mol. Cell. Biol. 24: 8312-8321 [Abstract] [Full Text]  
  • Ruone, S., Rhoades, A. R., Formosa, T. (2003). Multiple Nhp6 Molecules Are Required to Recruit Spt16-Pob3 to Form yFACT Complexes and to Reorganize Nucleosomes. J. Biol. Chem. 278: 45288-45295 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»