Archaeal Chromatin Proteins Cren7 and Sul7d Compact DNA by Bending and Bridging.

MBio
ZhenFeng ZhangLi Huang

Abstract

Archaeal chromatin proteins Cren7 and Sul7d from Sulfolobus are DNA benders. To better understand their architectural roles in chromosomal DNA organization, we analyzed DNA compaction by Cren7 and Sis7d, a Sul7d family member, from Sulfolobus islandicus at the single-molecule (SM) level by total single-molecule internal reflection fluorescence microscopy (SM-TIRFM) and atomic force microscopy (AFM). We show that both Cren7 and Sis7d were able to compact singly tethered λ DNA into a highly condensed structure in a three-step process and that Cren7 was over an order of magnitude more efficient than Sis7d in DNA compaction. The two proteins were similar in DNA bending kinetics but different in DNA condensation patterns. At saturating concentrations, Sis7d formed randomly distributed clusters whereas Cren7 generated a single and highly condensed core on plasmid DNA. This observation is consistent with the greater ability of Cren7 than of Sis7d to bridge DNA. Our results offer significant insights into the mechanism and kinetics of chromosomal DNA organization in Crenarchaea.IMPORTANCE A long-standing question is how chromosomal DNA is packaged in Crenarchaeota, a major group of archaea, which synthesize large amounts of unique smal...Continue Reading

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Citations

Oct 29, 2020·Transcription·Breanna R Wenck, Thomas J Santangelo
Jan 1, 2021·Journal of Molecular Biology·Shawn P LaursenKarolin Luger
Jan 22, 2021·FEMS Microbiology Reviews·April M LewisRobert M Kelly

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Methods Mentioned

BETA
fluorescence
atomic force microscopy
fluorescence microscopy
pulldown
electrophoresis
AFM
surface plasmon resonance
chip
PCR

Software Mentioned

pLink
ImageJ
BIA evaluation
Matlab
NanoScope
ScanAsyst

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