The intrinsic ATPase activity of Mycobacterium tuberculosis DnaA promotes rapid oligomerization of DnaA on oriC (Q28487494)

24 January 2017

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18 January 2020

title

The intrinsic ATPase activity of Mycobacterium tuberculosis DnaA promotes rapid oligomerization of DnaA on oriC (English)

2 references

24 January 2017

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Mycobacterium tuberculosis

18 January 2020

main subject

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author

Julia E Grimwade

6

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18 January 2020

author name string

Meredith Moomey

2

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24 January 2017

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18 January 2020

Syed Muniruzzaman

4

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18 January 2020

Kohji Yamamoto

5

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18 January 2020

Malini Rajagopalan

7

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18 January 2020

Murty V V S Madiraju

1

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18 January 2020

Pierre F Neuenschwander

3

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language of work or name

English

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publication date

1 March 2006

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18 January 2020

published in

Molecular Microbiology

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18 January 2020

volume

59

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18 January 2020

issue

6

2 references

DOI.org query endpoint

https://doi.org/10.1162%2F089892900564073

26 March 2017

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page(s)

1876-1890

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Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence

18 January 2020

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Hda inactivation of DnaA is the predominant mechanism preventing hyperinitiation of Escherichia coli DNA replication

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Replicatively active complexes of DnaA protein and the Escherichia coli chromosomal origin observed in the electron microscope

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Mutations in the CCGTTCACA DnaA box of Mycobacterium tuberculosis oriC that abolish replication of oriC plasmids are tolerated on the chromosome

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Conditional expression of Mycobacterium smegmatis dnaA, an essential DNA replication gene

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IHF redistributes bound initiator protein, DnaA, on supercoiled oriC of Escherichia coli

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Feedback controls restrain the initiation of Escherichia coli chromosomal replication.

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The initiator function of DnaA protein is negatively regulated by the sliding clamp of the E. coli chromosomal replicase.

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Hda, a novel DnaA-related protein, regulates the replication cycle in Escherichia coli

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Formation of an ATP-DnaA-specific initiation complex requires DnaA Arginine 285, a conserved motif in the AAA+ protein family.

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ATPase switches controlling DNA replication initiation.

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Two discriminatory binding sites in the Escherichia coli replication origin are required for DNA strand opening by initiator DnaA-ATP.

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A nucleotide switch in the Escherichia coli DnaA protein initiates chromosomal replication: evidnece from a mutant DnaA protein defective in regulatory ATP hydrolysis in vitro and in vivo

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Use of a flexible cassette method to generate a double unmarked Mycobacterium tuberculosis tlyA plcABC mutant by gene replacement

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18 January 2020

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Consolidated OpenCitations Corpus – April 2017

2 references

Consolidated OpenCitations Corpus – April 2017