Basic N-terminus of yeast Nhp6A regulates the mechanism of its DNA flexibility enhancement

Jingyun Zhang, Micah J. McCauley, L James Maher III, Mark C. Williams, Nathan E. Israeloff

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

HMGB (high-mobility group box) proteins are members of a class of small proteins that are ubiquitous in eukaryotic cells and nonspecifically bind to DNA, inducing large-angle DNA bends, enhancing the flexibility of DNA, and likely facilitating numerous important biological interactions. To determine the nature of this behavior for different HMGB proteins, we used atomic force microscopy to quantitatively characterize the bend angle distributions of DNA complexes with human HMGB2(Box A), yeast Nhp6A, and two chimeric mutants of these proteins. While all of the HMGB proteins bend DNA to preferred angles, Nhp6A promoted the formation of higher-order oligomer structures and induced a significantly broader distribution of angles, suggesting that the mechanism of Nhp6A is like a flexible hinge more than that of HMGB2(Box A). To determine the structural origins of this behavior, we used portions of the cationic N-terminus of Nhp6A to replace corresponding HMGB2(Box A) sequences. We found that the oligomerization and broader angle distribution correlated directly with the length of the N-terminus incorporated into the HMGB2(Box A) construct. Therefore, the basic N-terminus of Nhp6A is responsible for its ability to act as a flexible hinge and to form high-order structures.

Original languageEnglish (US)
Pages (from-to)10-20
Number of pages11
JournalJournal of Molecular Biology
Volume416
Issue number1
DOIs
StatePublished - Feb 10 2012

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HMGB2 Protein
HMGB Proteins
Yeasts
DNA
Mutant Chimeric Proteins
Aptitude
Atomic Force Microscopy
Eukaryotic Cells
Proteins

Keywords

  • atomic force microscopy
  • DNA binding
  • DNA melting
  • HMGB2
  • single molecule

ASJC Scopus subject areas

  • Molecular Biology

Cite this

Basic N-terminus of yeast Nhp6A regulates the mechanism of its DNA flexibility enhancement. / Zhang, Jingyun; McCauley, Micah J.; Maher III, L James; Williams, Mark C.; Israeloff, Nathan E.

In: Journal of Molecular Biology, Vol. 416, No. 1, 10.02.2012, p. 10-20.

Research output: Contribution to journalArticle

Zhang, Jingyun ; McCauley, Micah J. ; Maher III, L James ; Williams, Mark C. ; Israeloff, Nathan E. / Basic N-terminus of yeast Nhp6A regulates the mechanism of its DNA flexibility enhancement. In: Journal of Molecular Biology. 2012 ; Vol. 416, No. 1. pp. 10-20.
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