Self-organization of G-quadruplex structures in the hTERT core promoter stabilized by polyaminic side-chains perylene derivatives

hTERT core promoter regulates telomerase transcription in human cells, thus its structural features are of large interest. We have found that the G-rich hTERT core promoter region, corresponding to the major DNase I hypersensitive site in chromatin organization, contains nine putative G-quadruplex f...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Biophysical chemistry 2010-11, Vol.153 (1)
Hauptverfasser: Micheli, Emanuela, Martufi, Matteo, Cacchione, Stefano, de Santis, Pasquale, Savino, Maria
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page
container_issue 1
container_start_page
container_title Biophysical chemistry
container_volume 153
creator Micheli, Emanuela
Martufi, Matteo
Cacchione, Stefano
de Santis, Pasquale
Savino, Maria
description hTERT core promoter regulates telomerase transcription in human cells, thus its structural features are of large interest. We have found that the G-rich hTERT core promoter region, corresponding to the major DNase I hypersensitive site in chromatin organization, contains nine putative G-quadruplex forming sequences (PQS) and is unfavourable for nucleosome formation. Here we show that four PQS are effectively able to form stable parallel intramolecular G-quadruplexes, using PAGE and CD spectroscopy analysis. The PQS-region, as whole, appears to be organized in three self-interacting G-quadruplexes, probably giving rise to a helicoidal superstructure, as shown by CD and polymerase stop assay.
doi_str_mv 10.1016/j.bpc.2010.10.003
format Article
fullrecord <record><control><sourceid>hal</sourceid><recordid>TN_cdi_hal_primary_oai_HAL_hal_00702310v1</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>oai_HAL_hal_00702310v1</sourcerecordid><originalsourceid>FETCH-hal_primary_oai_HAL_hal_00702310v13</originalsourceid><addsrcrecordid>eNqVjb1Ow0AQhK8AifDzAHTbUtjs2VGgRSiQggrcW2d7HW90vjv2bAun480xiBfINKP59Emj1K3GVKPe3B_SKtRphn87RczP1Apz1Ml6k2UX6jLGAy55RFyp7w-ybeJlbxwfzcDegW_hNfkcTSNjsPQFcZCxHkahCOxg6Ai6YvteQO2FIIjv_UCyWKZiy0dqoJoheDubnh3XELmhpO4MuwiBZLbkCBoSnpa7ieK1Om-NjXTz31fq7mVbPO-SztgyCPdG5tIbLndPb-UvQ3zALNc46fwU9wd01Vr6</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Self-organization of G-quadruplex structures in the hTERT core promoter stabilized by polyaminic side-chains perylene derivatives</title><source>Elsevier ScienceDirect Journals Complete</source><creator>Micheli, Emanuela ; Martufi, Matteo ; Cacchione, Stefano ; de Santis, Pasquale ; Savino, Maria</creator><creatorcontrib>Micheli, Emanuela ; Martufi, Matteo ; Cacchione, Stefano ; de Santis, Pasquale ; Savino, Maria</creatorcontrib><description>hTERT core promoter regulates telomerase transcription in human cells, thus its structural features are of large interest. We have found that the G-rich hTERT core promoter region, corresponding to the major DNase I hypersensitive site in chromatin organization, contains nine putative G-quadruplex forming sequences (PQS) and is unfavourable for nucleosome formation. Here we show that four PQS are effectively able to form stable parallel intramolecular G-quadruplexes, using PAGE and CD spectroscopy analysis. The PQS-region, as whole, appears to be organized in three self-interacting G-quadruplexes, probably giving rise to a helicoidal superstructure, as shown by CD and polymerase stop assay.</description><identifier>ISSN: 0301-4622</identifier><identifier>DOI: 10.1016/j.bpc.2010.10.003</identifier><language>eng</language><publisher>Elsevier</publisher><subject>Chemical Physics ; Physics</subject><ispartof>Biophysical chemistry, 2010-11, Vol.153 (1)</ispartof><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://hal.science/hal-00702310$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Micheli, Emanuela</creatorcontrib><creatorcontrib>Martufi, Matteo</creatorcontrib><creatorcontrib>Cacchione, Stefano</creatorcontrib><creatorcontrib>de Santis, Pasquale</creatorcontrib><creatorcontrib>Savino, Maria</creatorcontrib><title>Self-organization of G-quadruplex structures in the hTERT core promoter stabilized by polyaminic side-chains perylene derivatives</title><title>Biophysical chemistry</title><description>hTERT core promoter regulates telomerase transcription in human cells, thus its structural features are of large interest. We have found that the G-rich hTERT core promoter region, corresponding to the major DNase I hypersensitive site in chromatin organization, contains nine putative G-quadruplex forming sequences (PQS) and is unfavourable for nucleosome formation. Here we show that four PQS are effectively able to form stable parallel intramolecular G-quadruplexes, using PAGE and CD spectroscopy analysis. The PQS-region, as whole, appears to be organized in three self-interacting G-quadruplexes, probably giving rise to a helicoidal superstructure, as shown by CD and polymerase stop assay.</description><subject>Chemical Physics</subject><subject>Physics</subject><issn>0301-4622</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><recordid>eNqVjb1Ow0AQhK8AifDzAHTbUtjs2VGgRSiQggrcW2d7HW90vjv2bAun480xiBfINKP59Emj1K3GVKPe3B_SKtRphn87RczP1Apz1Ml6k2UX6jLGAy55RFyp7w-ybeJlbxwfzcDegW_hNfkcTSNjsPQFcZCxHkahCOxg6Ai6YvteQO2FIIjv_UCyWKZiy0dqoJoheDubnh3XELmhpO4MuwiBZLbkCBoSnpa7ieK1Om-NjXTz31fq7mVbPO-SztgyCPdG5tIbLndPb-UvQ3zALNc46fwU9wd01Vr6</recordid><startdate>20101130</startdate><enddate>20101130</enddate><creator>Micheli, Emanuela</creator><creator>Martufi, Matteo</creator><creator>Cacchione, Stefano</creator><creator>de Santis, Pasquale</creator><creator>Savino, Maria</creator><general>Elsevier</general><scope>1XC</scope><scope>VOOES</scope></search><sort><creationdate>20101130</creationdate><title>Self-organization of G-quadruplex structures in the hTERT core promoter stabilized by polyaminic side-chains perylene derivatives</title><author>Micheli, Emanuela ; Martufi, Matteo ; Cacchione, Stefano ; de Santis, Pasquale ; Savino, Maria</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-hal_primary_oai_HAL_hal_00702310v13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Chemical Physics</topic><topic>Physics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Micheli, Emanuela</creatorcontrib><creatorcontrib>Martufi, Matteo</creatorcontrib><creatorcontrib>Cacchione, Stefano</creatorcontrib><creatorcontrib>de Santis, Pasquale</creatorcontrib><creatorcontrib>Savino, Maria</creatorcontrib><collection>Hyper Article en Ligne (HAL)</collection><collection>Hyper Article en Ligne (HAL) (Open Access)</collection><jtitle>Biophysical chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Micheli, Emanuela</au><au>Martufi, Matteo</au><au>Cacchione, Stefano</au><au>de Santis, Pasquale</au><au>Savino, Maria</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Self-organization of G-quadruplex structures in the hTERT core promoter stabilized by polyaminic side-chains perylene derivatives</atitle><jtitle>Biophysical chemistry</jtitle><date>2010-11-30</date><risdate>2010</risdate><volume>153</volume><issue>1</issue><issn>0301-4622</issn><abstract>hTERT core promoter regulates telomerase transcription in human cells, thus its structural features are of large interest. We have found that the G-rich hTERT core promoter region, corresponding to the major DNase I hypersensitive site in chromatin organization, contains nine putative G-quadruplex forming sequences (PQS) and is unfavourable for nucleosome formation. Here we show that four PQS are effectively able to form stable parallel intramolecular G-quadruplexes, using PAGE and CD spectroscopy analysis. The PQS-region, as whole, appears to be organized in three self-interacting G-quadruplexes, probably giving rise to a helicoidal superstructure, as shown by CD and polymerase stop assay.</abstract><pub>Elsevier</pub><doi>10.1016/j.bpc.2010.10.003</doi><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0301-4622
ispartof Biophysical chemistry, 2010-11, Vol.153 (1)
issn 0301-4622
language eng
recordid cdi_hal_primary_oai_HAL_hal_00702310v1
source Elsevier ScienceDirect Journals Complete
subjects Chemical Physics
Physics
title Self-organization of G-quadruplex structures in the hTERT core promoter stabilized by polyaminic side-chains perylene derivatives
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-07T14%3A42%3A14IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-hal&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Self-organization%20of%20G-quadruplex%20structures%20in%20the%20hTERT%20core%20promoter%20stabilized%20by%20polyaminic%20side-chains%20perylene%20derivatives&rft.jtitle=Biophysical%20chemistry&rft.au=Micheli,%20Emanuela&rft.date=2010-11-30&rft.volume=153&rft.issue=1&rft.issn=0301-4622&rft_id=info:doi/10.1016/j.bpc.2010.10.003&rft_dat=%3Chal%3Eoai_HAL_hal_00702310v1%3C/hal%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true