izpis_h1_title_alt

Conditional cooperativity in DNA minor-groove recognition by oligopeptides
ID Lah, Jurij (Author), ID Hadži, San (Author)

.pdfPDF - Presentation file, Download (1,68 MB)
MD5: DE7A53F586AFC17B2CC5F54B4F7D6F3F
URLURL - Source URL, Visit https://www.mdpi.com/1420-3049/26/17/5188 This link opens in a new window

Abstract
The recognition of specific DNA sequences in processes such as transcription is associated with a cooperative binding of proteins. Some transcription regulation mechanisms involve additional proteins that can influence the binding cooperativity by acting as corepressors or coactivators. In a conditional cooperativity mechanism, the same protein can induce binding cooperativity at one concentration and inhibit it at another. Here, we use calorimetric (ITC) and spectroscopic (UV, CD) experiments to show that such conditional cooperativity can also be achieved by the small DNA-directed oligopeptides distamycin and netropsin. Using a global thermodynamic analysis of the observed binding and (un)folding processes, we calculate the phase diagrams for this system, which show that distamycin binding cooperativity is more pronounced at lower temperatures and can be first induced and then reduced by increasing the netropsin or/and Na+ ion concentration. A molecular interpretation of this phenomenon is suggested.

Language:English
Keywords:DNA recognition, conditional cooperativity, transcription regulation, protein–DNA interactions, ligand–DNA interactions, distamycin, netropsin, thermodynamics of binding, phase diagrams, DNA folding
Work type:Article
Typology:1.01 - Original Scientific Article
Organization:FKKT - Faculty of Chemistry and Chemical Technology
Publication status:Published
Publication version:Version of Record
Year:2021
Number of pages:10 str.
Numbering:Vol. 26, iss. 17, art. 5188
PID:20.500.12556/RUL-136078 This link opens in a new window
UDC:577.323
ISSN on article:1420-3049
DOI:10.3390/molecules26175188 This link opens in a new window
COBISS.SI-ID:87050755 This link opens in a new window
Publication date in RUL:11.04.2022
Views:749
Downloads:119
Metadata:XML DC-XML DC-RDF
:
Copy citation
Share:Bookmark and Share

Record is a part of a journal

Title:Molecules
Shortened title:Molecules
Publisher:MDPI
ISSN:1420-3049
COBISS.SI-ID:18462981 This link opens in a new window

Licences

License:CC BY 4.0, Creative Commons Attribution 4.0 International
Link:http://creativecommons.org/licenses/by/4.0/
Description:This is the standard Creative Commons license that gives others maximum freedom to do what they want with the work as long as they credit the author.
Licensing start date:01.09.2021

Secondary language

Language:Slovenian
Keywords:prepoznavanje DNA, pogojna kooperativnost, regulacija transkripcije, interakcije protein – DNA, interakcije ligand – DNA, distamicin, netropsin, termodinamika vezave, fazni diagrami, zvitje DNA

Projects

Funder:ARRS - Slovenian Research Agency
Project number:P1-0201
Name:Fizikalna kemija

Funder:ARRS - Slovenian Research Agency
Project number:J1-1706
Name:Stabilnost nove vrste kvadruplesov DNA (AGCGA) in njihovo prepoznavanje z nanotelesi

Similar documents

Similar works from RUL:
Similar works from other Slovenian collections:

Back