The Missing Electrostatic Interactions between DNA Substrate and Sulfolobus solfataricus DNA Photolyase

What is the Role of Charged Amino Acids in Thermophilic DNA Binding Proteins?

Yvonne Gindt, Ban H. Edani, Antonia Olejnikova, Ariana N. Roberts, Sudipto Munshi, Robert J. Stanley

Research output: Contribution to journalArticleResearchpeer-review

5 Citations (Scopus)

Abstract

DNA photolyase can be used to study how a protein with its required cofactor has adapted over a large temperature range. The enzymatic activity and thermodynamics of substrate binding for protein from Sulfolobus solfataricus were directly compared to protein from Escherichia coli. Turnover numbers and catalytic activity were virtually identical, but organic cosolvents may be necessary to maintain activity of the thermophilic protein at higher temperatures. UV-damaged DNA binding to the thermophilic protein is less favorable by ∼2 kJ/mol. The enthalpy of binding is ∼10 kJ/mol less exothermic for the thermophile, but the amount and type of surface area buried upon DNA binding appears to be somewhat similar. The most important finding was observed when ionic strength studies were used to separate binding interactions into electrostatic and nonelectrostatic contributions; DNA binding to the thermophilic protein appears to lack the electrostatic contributions observed with the mesophilic protein.

Original languageEnglish
Pages (from-to)10234-10242
Number of pages9
JournalJournal of Physical Chemistry B
Volume120
Issue number39
DOIs
StatePublished - 6 Oct 2016

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Deoxyribodipyrimidine Photo-Lyase
DNA-Binding Proteins
Coulomb interactions
amino acids
Amino acids
DNA
deoxyribonucleic acid
electrostatics
proteins
Proteins
Amino Acids
Substrates
interactions
thermophiles
Escherichia coli Proteins
Ionic strength
Electrostatics
Enthalpy
Catalyst activity
Carrier Proteins

Cite this

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title = "The Missing Electrostatic Interactions between DNA Substrate and Sulfolobus solfataricus DNA Photolyase: What is the Role of Charged Amino Acids in Thermophilic DNA Binding Proteins?",
abstract = "DNA photolyase can be used to study how a protein with its required cofactor has adapted over a large temperature range. The enzymatic activity and thermodynamics of substrate binding for protein from Sulfolobus solfataricus were directly compared to protein from Escherichia coli. Turnover numbers and catalytic activity were virtually identical, but organic cosolvents may be necessary to maintain activity of the thermophilic protein at higher temperatures. UV-damaged DNA binding to the thermophilic protein is less favorable by ∼2 kJ/mol. The enthalpy of binding is ∼10 kJ/mol less exothermic for the thermophile, but the amount and type of surface area buried upon DNA binding appears to be somewhat similar. The most important finding was observed when ionic strength studies were used to separate binding interactions into electrostatic and nonelectrostatic contributions; DNA binding to the thermophilic protein appears to lack the electrostatic contributions observed with the mesophilic protein.",
author = "Yvonne Gindt and Edani, {Ban H.} and Antonia Olejnikova and Roberts, {Ariana N.} and Sudipto Munshi and Stanley, {Robert J.}",
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publisher = "American Chemical Society",
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The Missing Electrostatic Interactions between DNA Substrate and Sulfolobus solfataricus DNA Photolyase : What is the Role of Charged Amino Acids in Thermophilic DNA Binding Proteins? / Gindt, Yvonne; Edani, Ban H.; Olejnikova, Antonia; Roberts, Ariana N.; Munshi, Sudipto; Stanley, Robert J.

In: Journal of Physical Chemistry B, Vol. 120, No. 39, 06.10.2016, p. 10234-10242.

Research output: Contribution to journalArticleResearchpeer-review

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