TrmBL2 from Pyrococcus furiosus Interacts Both with Double-Stranded and Single-Stranded DNA

In many hyperthermophilic archaea the DNA binding protein TrmBL2 or one of its homologues is abundantly expressed. TrmBL2 is thought to play a significant role in modulating the chromatin architecture in combination with the archaeal histone proteins and Alba. However, its precise physiological role...

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Main Authors:	Wierer, Sebastian, Daldrop, Peter, Ud Din Ahmad, Misbha, Boos, Winfried, Drescher, Malte, Welte, Wolfram, Seidel, Ralf
Format:	Online
Language:	English
Published:	Public Library of Science 2016
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4877046/

id	pubmed-4877046
recordtype	oai_dc
spelling	pubmed-48770462016-06-09 TrmBL2 from Pyrococcus furiosus Interacts Both with Double-Stranded and Single-Stranded DNA Wierer, Sebastian Daldrop, Peter Ud Din Ahmad, Misbha Boos, Winfried Drescher, Malte Welte, Wolfram Seidel, Ralf Research Article In many hyperthermophilic archaea the DNA binding protein TrmBL2 or one of its homologues is abundantly expressed. TrmBL2 is thought to play a significant role in modulating the chromatin architecture in combination with the archaeal histone proteins and Alba. However, its precise physiological role is poorly understood. It has been previously shown that upon binding TrmBL2 covers double-stranded DNA, which leads to the formation of a thick and fibrous filament. Here we investigated the filament formation process as well as the stabilization of DNA by TrmBL2 from Pyroccocus furiosus in detail. We used magnetic tweezers that allow to monitor changes of the DNA mechanical properties upon TrmBL2 binding on the single-molecule level. Extended filaments formed in a cooperative manner and were considerably stiffer than bare double-stranded DNA. Unlike Alba, TrmBL2 did not form DNA cross-bridges. The protein was found to bind double- and single-stranded DNA with similar affinities. In mechanical disruption experiments of DNA hairpins this led to stabilization of both, the double- (before disruption) and the single-stranded (after disruption) DNA forms. Combined, these findings suggest that the biological function of TrmBL2 is not limited to modulating genome architecture and acting as a global repressor but that the protein acts additionally as a stabilizer of DNA secondary structure. Public Library of Science 2016-05-23 /pmc/articles/PMC4877046/ /pubmed/27214207 http://dx.doi.org/10.1371/journal.pone.0156098 Text en © 2016 Wierer et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Wierer, Sebastian Daldrop, Peter Ud Din Ahmad, Misbha Boos, Winfried Drescher, Malte Welte, Wolfram Seidel, Ralf
spellingShingle	Wierer, Sebastian Daldrop, Peter Ud Din Ahmad, Misbha Boos, Winfried Drescher, Malte Welte, Wolfram Seidel, Ralf TrmBL2 from Pyrococcus furiosus Interacts Both with Double-Stranded and Single-Stranded DNA
author_facet	Wierer, Sebastian Daldrop, Peter Ud Din Ahmad, Misbha Boos, Winfried Drescher, Malte Welte, Wolfram Seidel, Ralf
author_sort	Wierer, Sebastian
title	TrmBL2 from Pyrococcus furiosus Interacts Both with Double-Stranded and Single-Stranded DNA
title_short	TrmBL2 from Pyrococcus furiosus Interacts Both with Double-Stranded and Single-Stranded DNA
title_full	TrmBL2 from Pyrococcus furiosus Interacts Both with Double-Stranded and Single-Stranded DNA
title_fullStr	TrmBL2 from Pyrococcus furiosus Interacts Both with Double-Stranded and Single-Stranded DNA
title_full_unstemmed	TrmBL2 from Pyrococcus furiosus Interacts Both with Double-Stranded and Single-Stranded DNA
title_sort	trmbl2 from pyrococcus furiosus interacts both with double-stranded and single-stranded dna
description	In many hyperthermophilic archaea the DNA binding protein TrmBL2 or one of its homologues is abundantly expressed. TrmBL2 is thought to play a significant role in modulating the chromatin architecture in combination with the archaeal histone proteins and Alba. However, its precise physiological role is poorly understood. It has been previously shown that upon binding TrmBL2 covers double-stranded DNA, which leads to the formation of a thick and fibrous filament. Here we investigated the filament formation process as well as the stabilization of DNA by TrmBL2 from Pyroccocus furiosus in detail. We used magnetic tweezers that allow to monitor changes of the DNA mechanical properties upon TrmBL2 binding on the single-molecule level. Extended filaments formed in a cooperative manner and were considerably stiffer than bare double-stranded DNA. Unlike Alba, TrmBL2 did not form DNA cross-bridges. The protein was found to bind double- and single-stranded DNA with similar affinities. In mechanical disruption experiments of DNA hairpins this led to stabilization of both, the double- (before disruption) and the single-stranded (after disruption) DNA forms. Combined, these findings suggest that the biological function of TrmBL2 is not limited to modulating genome architecture and acting as a global repressor but that the protein acts additionally as a stabilizer of DNA secondary structure.
publisher	Public Library of Science
publishDate	2016
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4877046/
_version_	1613582909877256192

TrmBL2 from Pyrococcus furiosus Interacts Both with Double-Stranded and Single-Stranded DNA

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