SulfurTransferaseV1, Main, Exploration, bibRecord, 000196

Substrate Binding Regulates Redox Signaling in Human DNA Primase.

Identifieur interne : 000196 ( Main/Exploration ); précédent : 000195; suivant : 000197

Substrate Binding Regulates Redox Signaling in Human DNA Primase.

Auteurs : Elizabeth O'Brien [États-Unis] ; Marilyn E. Holt [États-Unis] ; Lauren E. Salay [États-Unis] ; Walter J. Chazin [États-Unis] ; Jacqueline K. Barton [États-Unis]

Source :

Journal of the American Chemical Society [ 1520-5126 ] ; 2018.

RBID : pubmed:30433774

Descripteurs français

KwdFr :
- ADN (composition chimique), ADN (métabolisme), DNA primase (composition chimique), DNA primase (génétique), DNA primase (métabolisme), Domaines protéiques (MeSH), Ferrosulfoprotéines (composition chimique), Ferrosulfoprotéines (métabolisme), Humains (MeSH), Initiation de la transcription (MeSH), Liaison aux protéines (MeSH), Nucléotides (composition chimique), Nucléotides (métabolisme), Oxydoréduction (MeSH), Techniques électrochimiques (méthodes), Élongation de la transcription (MeSH).
MESH :
- composition chimique : ADN, DNA primase, Ferrosulfoprotéines, Nucléotides.
- génétique : DNA primase.
- métabolisme : ADN, DNA primase, Ferrosulfoprotéines, Nucléotides.
- méthodes : Techniques électrochimiques.
- Domaines protéiques, Humains, Initiation de la transcription, Liaison aux protéines, Oxydoréduction, Élongation de la transcription.

English descriptors

KwdEn :
- DNA (chemistry), DNA (metabolism), DNA Primase (chemistry), DNA Primase (genetics), DNA Primase (metabolism), Electrochemical Techniques (methods), Humans (MeSH), Iron-Sulfur Proteins (chemistry), Iron-Sulfur Proteins (metabolism), Nucleotides (chemistry), Nucleotides (metabolism), Oxidation-Reduction (MeSH), Protein Binding (MeSH), Protein Domains (MeSH), Transcription Elongation, Genetic (MeSH), Transcription Initiation, Genetic (MeSH).
MESH :
- chemical , chemistry : DNA, DNA Primase, Iron-Sulfur Proteins, Nucleotides.
- chemical , genetics : DNA Primase.
- chemical , metabolism : DNA, DNA Primase, Iron-Sulfur Proteins, Nucleotides.
- methods : Electrochemical Techniques.
- Humans, Oxidation-Reduction, Protein Binding, Protein Domains, Transcription Elongation, Genetic, Transcription Initiation, Genetic.

Abstract

Generation of daughter strands during DNA replication requires the action of DNA primase to synthesize an initial short RNA primer on the single-stranded DNA template. Primase is a heterodimeric enzyme containing two domains whose activity must be coordinated during primer synthesis: an RNA polymerase domain in the small subunit (p48) and a [4Fe4S] cluster-containing C-terminal domain of the large subunit (p58C). Here we examine the redox switching properties of the [4Fe4S] cluster in the full p48/p58 heterodimer using DNA electrochemistry. Unlike with isolated p58C, robust redox signaling in the primase heterodimer requires binding of both DNA and NTPs; NTP binding shifts the p48/p58 cluster redox potential into the physiological range, generating a signal near 160 mV vs NHE. Preloading of primase with NTPs enhances catalytic activity on primed DNA, suggesting that primase configurations promoting activity are more highly populated in the NTP-bound protein. We propose that p48/p58 binding of anionic DNA and NTPs affects the redox properties of the [4Fe4S] cluster; this electrostatic change is likely influenced by the alignment of primase subunits during activity because the configuration affects the [4Fe4S] cluster environment and coupling to DNA bases for redox signaling. Thus, both binding of polyanionic substrates and configurational dynamics appear to influence [4Fe4S] redox signaling properties. These results suggest that these factors should be considered generally in characterizing signaling networks of large, multisubunit DNA-processing [4Fe4S] enzymes.

DOI: 10.1021/jacs.8b09914
PubMed: 30433774
PubMed Central: PMC6470046

Affiliations:

États-Unis

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000182
to stream Main, to step Curation: 000182

Le document en format XML

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<term>DNA Primase (metabolism)</term>
<term>Electrochemical Techniques (methods)</term>
<term>Humans (MeSH)</term>
<term>Iron-Sulfur Proteins (chemistry)</term>
<term>Iron-Sulfur Proteins (metabolism)</term>
<term>Nucleotides (chemistry)</term>
<term>Nucleotides (metabolism)</term>
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<term>DNA primase (métabolisme)</term>
<term>Domaines protéiques (MeSH)</term>
<term>Ferrosulfoprotéines (composition chimique)</term>
<term>Ferrosulfoprotéines (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Initiation de la transcription (MeSH)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Nucléotides (composition chimique)</term>
<term>Nucléotides (métabolisme)</term>
<term>Oxydoréduction (MeSH)</term>
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<term>DNA Primase</term>
<term>Iron-Sulfur Proteins</term>
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<term>DNA Primase</term>
<term>Iron-Sulfur Proteins</term>
<term>Nucleotides</term>
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<term>Oxidation-Reduction</term>
<term>Protein Binding</term>
<term>Protein Domains</term>
<term>Transcription Elongation, Genetic</term>
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<term>Humains</term>
<term>Initiation de la transcription</term>
<term>Liaison aux protéines</term>
<term>Oxydoréduction</term>
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<front><div type="abstract" xml:lang="en">Generation of daughter strands during DNA replication requires the action of DNA primase to synthesize an initial short RNA primer on the single-stranded DNA template. Primase is a heterodimeric enzyme containing two domains whose activity must be coordinated during primer synthesis: an RNA polymerase domain in the small subunit (p48) and a [4Fe4S] cluster-containing C-terminal domain of the large subunit (p58C). Here we examine the redox switching properties of the [4Fe4S] cluster in the full p48/p58 heterodimer using DNA electrochemistry. Unlike with isolated p58C, robust redox signaling in the primase heterodimer requires binding of both DNA and NTPs; NTP binding shifts the p48/p58 cluster redox potential into the physiological range, generating a signal near 160 mV vs NHE. Preloading of primase with NTPs enhances catalytic activity on primed DNA, suggesting that primase configurations promoting activity are more highly populated in the NTP-bound protein. We propose that p48/p58 binding of anionic DNA and NTPs affects the redox properties of the [4Fe4S] cluster; this electrostatic change is likely influenced by the alignment of primase subunits during activity because the configuration affects the [4Fe4S] cluster environment and coupling to DNA bases for redox signaling. Thus, both binding of polyanionic substrates and configurational dynamics appear to influence [4Fe4S] redox signaling properties. These results suggest that these factors should be considered generally in characterizing signaling networks of large, multisubunit DNA-processing [4Fe4S] enzymes.</div>
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<Abstract><AbstractText>Generation of daughter strands during DNA replication requires the action of DNA primase to synthesize an initial short RNA primer on the single-stranded DNA template. Primase is a heterodimeric enzyme containing two domains whose activity must be coordinated during primer synthesis: an RNA polymerase domain in the small subunit (p48) and a [4Fe4S] cluster-containing C-terminal domain of the large subunit (p58C). Here we examine the redox switching properties of the [4Fe4S] cluster in the full p48/p58 heterodimer using DNA electrochemistry. Unlike with isolated p58C, robust redox signaling in the primase heterodimer requires binding of both DNA and NTPs; NTP binding shifts the p48/p58 cluster redox potential into the physiological range, generating a signal near 160 mV vs NHE. Preloading of primase with NTPs enhances catalytic activity on primed DNA, suggesting that primase configurations promoting activity are more highly populated in the NTP-bound protein. We propose that p48/p58 binding of anionic DNA and NTPs affects the redox properties of the [4Fe4S] cluster; this electrostatic change is likely influenced by the alignment of primase subunits during activity because the configuration affects the [4Fe4S] cluster environment and coupling to DNA bases for redox signaling. Thus, both binding of polyanionic substrates and configurational dynamics appear to influence [4Fe4S] redox signaling properties. These results suggest that these factors should be considered generally in characterizing signaling networks of large, multisubunit DNA-processing [4Fe4S] enzymes.</AbstractText>
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Substrate Binding Regulates Redox Signaling in Human DNA Primase.

Substrate Binding Regulates Redox Signaling in Human DNA Primase.

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