An Iron-Sulfur Cluster in the C-terminal Domain of the p58 Subunit of Human DNA Primase

DNA primase synthesizes short RNA primers that are required to initiate DNA synthesis on the parental template strands during DNA replication. Eukaryotic primase contains two subunits, p48 and p58, and is normally tightly associated with DNA polymerase α. Despite the fundamental importance of primas...

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Published inThe Journal of biological chemistry Vol. 282; no. 46; pp. 33444 - 33451
Main Authors Weiner, Brian E., Huang, Hao, Dattilo, Brian M., Nilges, Mark J., Fanning, Ellen, Chazin, Walter J.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 16.11.2007
American Society for Biochemistry and Molecular Biology
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Abstract DNA primase synthesizes short RNA primers that are required to initiate DNA synthesis on the parental template strands during DNA replication. Eukaryotic primase contains two subunits, p48 and p58, and is normally tightly associated with DNA polymerase α. Despite the fundamental importance of primase in DNA replication, structural data on eukaryotic DNA primase are lacking. The p48/p58 dimer was subjected to limited proteolysis, which produced two stable structural domains: one containing the bulk of p48 and the other corresponding to the C-terminal fragment of p58. These domains were identified by mass spectrometry and N-terminal sequencing. The C-terminal p58 domain (p58C) was expressed, purified, and characterized. CD and NMR spectroscopy experiments demonstrated that p58C forms a well folded structure. The protein has a distinctive brownish color, and evidence from inductively coupled plasma mass spectrometry, UV-visible spectrophotometry, and EPR spectroscopy revealed characteristics consistent with the presence of a [4Fe-4S] high potential iron protein cluster. Four putative cysteine ligands were identified using a multiple sequence alignment, and substitution of just one was sufficient to cause loss of the iron-sulfur cluster and a reduction in primase enzymatic activity relative to the wild-type protein. The discovery of an iron-sulfur cluster in DNA primase that contributes to enzymatic activity provides the first suggestion that the DNA replication machinery may have redox-sensitive activities. Our results offer new horizons in which to investigate the function of high potential [4Fe-4S] clusters in DNA-processing machinery.
AbstractList DNA primase synthesizes short RNA primers that are required to initiate DNA synthesis on the parental template strands during DNA replication. Eukaryotic primase contains two subunits, p48 and p58, and is normally tightly associated with DNA polymerase α. Despite the fundamental importance of primase in DNA replication, structural data on eukaryotic DNA primase are lacking. The p48/p58 dimer was subjected to limited proteolysis, which produced two stable structural domains: one containing the bulk of p48 and the other corresponding to the C-terminal fragment of p58. These domains were identified by mass spectrometry and N-terminal sequencing. The C-terminal p58 domain (p58C) was expressed, purified, and characterized. CD and NMR spectroscopy experiments demonstrated that p58C forms a well folded structure. The protein has a distinctive brownish color, and evidence from inductively coupled plasma mass spectrometry, UV-visible spectrophotometry, and EPR spectroscopy revealed characteristics consistent with the presence of a [4Fe-4S] high potential iron protein cluster. Four putative cysteine ligands were identified using a multiple sequence alignment, and substitution of just one was sufficient to cause loss of the iron-sulfur cluster and a reduction in primase enzymatic activity relative to the wild-type protein. The discovery of an iron-sulfur cluster in DNA primase that contributes to enzymatic activity provides the first suggestion that the DNA replication machinery may have redox-sensitive activities. Our results offer new horizons in which to investigate the function of high potential [4Fe-4S] clusters in DNA-processing machinery.
DNA primase synthesizes short RNA primers that are required to initiate DNA synthesis on the parental template strands during DNA replication. Eukaryotic primase contains two subunits, p48 and p58, and is normally tightly associated with DNA polymerase alpha. Despite the fundamental importance of primase in DNA replication, structural data on eukaryotic DNA primase are lacking. The p48/p58 dimer was subjected to limited proteolysis, which produced two stable structural domains: one containing the bulk of p48 and the other corresponding to the C-terminal fragment of p58. These domains were identified by mass spectrometry and N-terminal sequencing. The C-terminal p58 domain (p58C) was expressed, purified, and characterized. CD and NMR spectroscopy experiments demonstrated that p58C forms a well folded structure. The protein has a distinctive brownish color, and evidence from inductively coupled plasma mass spectrometry, UV-visible spectrophotometry, and EPR spectroscopy revealed characteristics consistent with the presence of a [4Fe-4S] high potential iron protein cluster. Four putative cysteine ligands were identified using a multiple sequence alignment, and substitution of just one was sufficient to cause loss of the iron-sulfur cluster and a reduction in primase enzymatic activity relative to the wild-type protein. The discovery of an iron-sulfur cluster in DNA primase that contributes to enzymatic activity provides the first suggestion that the DNA replication machinery may have redox-sensitive activities. Our results offer new horizons in which to investigate the function of high potential [4Fe-4S] clusters in DNA-processing machinery.
DNA primase synthesizes short RNA primers that are required to initiate DNA synthesis on the parental template strands during DNA replication. Eukaryotic primase contains two subunits, p48 and p58, and is normally tightly associated with DNA polymerase α. Despite the fundamental importance of primase in DNA replication, structural data on eukaryotic DNA primase are lacking. The p48/p58 dimer was subjected to limited proteolysis, which produced two stable structural domains: one containing the bulk of p48 and the other corresponding to the C-terminal fragment of p58. These domains were identified by mass spectrometry and N-terminal sequencing. The C-terminal p58 domain (p58C) was expressed, purified, and characterized. CD and NMR spectroscopy experiments demonstrated that p58C forms a well folded structure. The protein has a distinctive brownish color, and evidence from inductively coupled plasma mass spectrometry, UV-visible spectrophotometry, and EPR spectroscopy revealed characteristics consistent with the presence of a [4Fe-4S] high potential iron protein cluster. Four putative cysteine ligands were identified using a multiple sequence alignment, and substitution of just one was sufficient to cause loss of the iron-sulfur cluster and a reduction in primase enzymatic activity relative to the wild-type protein. The discovery of an iron-sulfur cluster in DNA primase that contributes to enzymatic activity provides the first suggestion that the DNA replication machinery may have redox-sensitive activities. Our results offer new horizons in which to investigate the function of high potential [4Fe-4S] clusters in DNA-processing machinery.
Author Chazin, Walter J.
Huang, Hao
Weiner, Brian E.
Fanning, Ellen
Dattilo, Brian M.
Nilges, Mark J.
Author_xml – sequence: 1
  givenname: Brian E.
  surname: Weiner
  fullname: Weiner, Brian E.
  organization: Department of Biochemistry, Vanderbilt University, Nashville, Tennessee, 37232
– sequence: 2
  givenname: Hao
  surname: Huang
  fullname: Huang, Hao
  organization: Department of Biological Sciences, Vanderbilt University, Nashville, Tennessee, 37232
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  givenname: Brian M.
  surname: Dattilo
  fullname: Dattilo, Brian M.
  organization: Department of Biochemistry, Vanderbilt University, Nashville, Tennessee, 37232
– sequence: 4
  givenname: Mark J.
  surname: Nilges
  fullname: Nilges, Mark J.
  organization: Illinois EPR Research Center, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801
– sequence: 5
  givenname: Ellen
  surname: Fanning
  fullname: Fanning, Ellen
  organization: Department of Biological Sciences, Vanderbilt University, Nashville, Tennessee, 37232
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  givenname: Walter J.
  surname: Chazin
  fullname: Chazin, Walter J.
  email: walter.chazin@vanderbilt.edu
  organization: Department of Biochemistry, Vanderbilt University, Nashville, Tennessee, 37232
BackLink https://www.ncbi.nlm.nih.gov/pubmed/17893144$$D View this record in MEDLINE/PubMed
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Snippet DNA primase synthesizes short RNA primers that are required to initiate DNA synthesis on the parental template strands during DNA replication. Eukaryotic...
DNA primase synthesizes short RNA primers that are required to initiate DNA synthesis on the parental template strands during DNA replication. Eukaryotic...
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SubjectTerms Amino Acid Sequence
Circular Dichroism
Cysteine - chemistry
DNA - chemistry
DNA Primase - chemistry
DNA Primase - metabolism
DNA Primase - physiology
Electron Spin Resonance Spectroscopy
Humans
Iron-Sulfur Proteins - chemistry
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Protein Structure, Tertiary
Recombinant Proteins - chemistry
Sequence Homology, Amino Acid
Spectrophotometry - methods
Spectrophotometry, Ultraviolet
Title An Iron-Sulfur Cluster in the C-terminal Domain of the p58 Subunit of Human DNA Primase
URI https://dx.doi.org/10.1074/jbc.M705826200
http://www.jbc.org/content/282/46/33444.abstract
https://www.ncbi.nlm.nih.gov/pubmed/17893144
https://search.proquest.com/docview/20334459
https://search.proquest.com/docview/68491380
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