PMID- 19234544
OWN - NLM
STAT- MEDLINE
DCOM- 20090608
LR  - 20090223
IS  - 0829-8211 (Print)
IS  - 0829-8211 (Linking)
VI  - 87
IP  - 1
DP  - 2009 Feb
TI  - DNA sequence-dependent variation in nucleosome structure, stability, and dynamics 
      detected by a FRET-based analysis.
PG  - 323-35
LID - 10.1139/O08-126 [doi]
AB  - Forster resonance energy transfer (FRET) techniques provide powerful and 
      sensitive methods for the study of conformational features in biomolecules. Here, 
      we review FRET-based studies of nucleosomes, focusing particularly on our work 
      comparing the widely used nucleosome standard, 5S rDNA, and 2 promoter-derived 
      regulatory element-containing nucleosomes, mouse mammary tumor virus (MMTV)-B and 
      GAL10. Using several FRET approaches, we detected significant DNA 
      sequence-dependent structure, stability, and dynamics differences among the 
      three. In particular, 5S nucleosomes and 5S H2A/H2B-depleted nucleosomal 
      particles have enhanced stability and diminished DNA dynamics, compared with 
      MMTV-B and GAL10 nucleosomes and particles. H2A/H2B-depleted nucleosomes are of 
      interest because they are produced by the activities of many 
      transcription-associated complexes. Significant location-dependent 
      (intranucleosomal) stability and dynamics variations were also observed. These 
      also vary among nucleosome types. Nucleosomes restrict regulatory factor access 
      to DNA, thereby impeding genetic processes. Eukaryotic cells possess mechanisms 
      to alter nucleosome structure, to generate DNA access, but alterations often must 
      be targeted to specific nucleosomes on critical regulatory DNA elements. By 
      endowing specific nucleosomes with intrinsically higher DNA accessibility and 
      (or) enhanced facility for conformational transitions, DNA sequence-dependent 
      nucleosome dynamics and stability variations have the potential to facilitate 
      nucleosome recognition and, thus, aid in the crucial targeting process. This and 
      other nucleosome structure and function conclusions from FRET analyses are 
      discussed.
FAU - Kelbauskas, L
AU  - Kelbauskas L
AD  - Biodesign Institute, Arizona State University, Tempe, AZ 85287, USA. 
      laimonas.kelbauskas@asu.edu
FAU - Woodbury, N
AU  - Woodbury N
FAU - Lohr, D
AU  - Lohr D
LA  - eng
GR  - CA 85990/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Review
PL  - Canada
TA  - Biochem Cell Biol
JT  - Biochemistry and cell biology = Biochimie et biologie cellulaire
JID - 8606068
RN  - 0 (Nucleosomes)
SB  - IM
MH  - Animals
MH  - Base Sequence
MH  - *Fluorescence Resonance Energy Transfer
MH  - Humans
MH  - Nucleosomes/*chemistry/*metabolism
RF  - 75
EDAT- 2009/02/24 09:00
MHDA- 2009/06/09 09:00
CRDT- 2009/02/24 09:00
PHST- 2009/02/24 09:00 [entrez]
PHST- 2009/02/24 09:00 [pubmed]
PHST- 2009/06/09 09:00 [medline]
AID - o08-126 [pii]
AID - 10.1139/O08-126 [doi]
PST - ppublish
SO  - Biochem Cell Biol. 2009 Feb;87(1):323-35. doi: 10.1139/O08-126.