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The DnaA N-terminal domain interacts with Hda to facilitate replicase clamp-mediated inactivation of DnaA.

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Title: The DnaA N-terminal domain interacts with Hda to facilitate replicase clamp-mediated inactivation of DnaA.
Authors: Su'etsugu, Masayuki1, Harada, Yuji1, Keyamura, Kenji1, Matsunaga, Chika1, Kasho, Kazutoshi1, Abe, Yoshito2, Ueda, Tadashi2, Katayama, Tsutomu1
Source: Environmental Microbiology. Dec2013, Vol. 15 Issue 12, p3183-3195. 13p.
Subjects: DNA, DNA replication, Escherichia coli, Adenosine triphosphate, Solvolysis, Hydrolysis, Molecular biology
Abstract: DnaA activity for replication initiation of the Escherichia coli chromosome is negatively regulated by feedback from the DNA-loaded form of the replicase clamp. In this process, called RIDA (regulatory inactivation of DnaA), ATP-bound DnaA transiently assembles into a complex consisting of Hda and the DNA-clamp, which promotes inter- AAA+ domain association between Hda and DnaA and stimulates hydrolysis of DnaA-bound ATP, producing inactive ADP- DnaA. Using a truncated DnaA mutant, we previously demonstrated that the DnaA N-terminal domain is involved in RIDA. However, the precise role of the N-terminal domain in RIDA has remained largely unclear. Here, we used an in vitro reconstituted system to demonstrate that the Asn-44 residue in the N-terminal domain of DnaA is crucial for RIDA but not for replication initiation. Moreover, an assay termed PDAX (pull-down after cross-linking) revealed an unstable interaction between a DnaA- N44 A mutant and Hda. In vivo, this mutant exhibited an increase in the cellular level of ATP-bound DnaA. These results establish a model in which interaction between DnaA Asn-44 and Hda stabilizes the association between the AAA+ domains of DnaA and Hda to facilitate DnaA- ATP hydrolysis during RIDA. [ABSTRACT FROM AUTHOR]
Copyright of Environmental Microbiology is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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DbLabel: Engineering Source
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  Data: The DnaA N-terminal domain interacts with Hda to facilitate replicase clamp-mediated inactivation of DnaA.
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  Data: <searchLink fieldCode="AR" term="%22Su'etsugu%2C+Masayuki%22">Su'etsugu, Masayuki</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Harada%2C+Yuji%22">Harada, Yuji</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Keyamura%2C+Kenji%22">Keyamura, Kenji</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Matsunaga%2C+Chika%22">Matsunaga, Chika</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Kasho%2C+Kazutoshi%22">Kasho, Kazutoshi</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Abe%2C+Yoshito%22">Abe, Yoshito</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Ueda%2C+Tadashi%22">Ueda, Tadashi</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Katayama%2C+Tsutomu%22">Katayama, Tsutomu</searchLink><relatesTo>1</relatesTo>
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  Data: <searchLink fieldCode="JN" term="%22Environmental+Microbiology%22">Environmental Microbiology</searchLink>. Dec2013, Vol. 15 Issue 12, p3183-3195. 13p.
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  Data: <searchLink fieldCode="DE" term="%22DNA%22">DNA</searchLink><br /><searchLink fieldCode="DE" term="%22DNA+replication%22">DNA replication</searchLink><br /><searchLink fieldCode="DE" term="%22Escherichia+coli%22">Escherichia coli</searchLink><br /><searchLink fieldCode="DE" term="%22Adenosine+triphosphate%22">Adenosine triphosphate</searchLink><br /><searchLink fieldCode="DE" term="%22Solvolysis%22">Solvolysis</searchLink><br /><searchLink fieldCode="DE" term="%22Hydrolysis%22">Hydrolysis</searchLink><br /><searchLink fieldCode="DE" term="%22Molecular+biology%22">Molecular biology</searchLink>
– Name: Abstract
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  Data: DnaA activity for replication initiation of the Escherichia coli chromosome is negatively regulated by feedback from the DNA-loaded form of the replicase clamp. In this process, called RIDA (regulatory inactivation of DnaA), ATP-bound DnaA transiently assembles into a complex consisting of Hda and the DNA-clamp, which promotes inter- AAA+ domain association between Hda and DnaA and stimulates hydrolysis of DnaA-bound ATP, producing inactive ADP- DnaA. Using a truncated DnaA mutant, we previously demonstrated that the DnaA N-terminal domain is involved in RIDA. However, the precise role of the N-terminal domain in RIDA has remained largely unclear. Here, we used an in vitro reconstituted system to demonstrate that the Asn-44 residue in the N-terminal domain of DnaA is crucial for RIDA but not for replication initiation. Moreover, an assay termed PDAX (pull-down after cross-linking) revealed an unstable interaction between a DnaA- N44 A mutant and Hda. In vivo, this mutant exhibited an increase in the cellular level of ATP-bound DnaA. These results establish a model in which interaction between DnaA Asn-44 and Hda stabilizes the association between the AAA+ domains of DnaA and Hda to facilitate DnaA- ATP hydrolysis during RIDA. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
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  Data: <i>Copyright of Environmental Microbiology is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1111/1462-2920.12147
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        Text: English
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        StartPage: 3183
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        Type: general
      – SubjectFull: DNA replication
        Type: general
      – SubjectFull: Escherichia coli
        Type: general
      – SubjectFull: Adenosine triphosphate
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      – SubjectFull: Solvolysis
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      – SubjectFull: Hydrolysis
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      – SubjectFull: Molecular biology
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      – TitleFull: The DnaA N-terminal domain interacts with Hda to facilitate replicase clamp-mediated inactivation of DnaA.
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            – D: 01
              M: 12
              Text: Dec2013
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              Y: 2013
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