Nucleoprotein architecture and ColE1 dimer resolution: a hypothesis (Q30431349)

21 June 2017

title

Nucleoprotein architecture and ColE1 dimer resolution: a hypothesis (English)

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21 June 2017

Hodgman TC

1

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21 June 2017

Griffiths H

series ordinal

2

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Summers DK

series ordinal

3

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language of work or name

English

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publication date

1 July 1998

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21 June 2017

published in

Molecular Microbiology

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volume

29

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issue

2

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page(s)

545-558

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Direct interaction of aminopeptidase A with recombination site DNA in Xer site-specific recombination

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DNA sequence of recombinase-binding sites can determine Xer site-specific recombination outcome.

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Determinants of selectivity in Xer site-specific recombination

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carP, involved in pyrimidine regulation of the Escherichia coli carbamoylphosphate synthetase operon encodes a sequence-specific DNA-binding protein identical to XerB and PepA, also required for resolution of ColEI multimers

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Protein motifs that recognize structural features of DNA

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Plasmid pSC101 harbors a recombination site, psi, which is able to resolve plasmid multimers and to substitute for the analogous chromosomal Escherichia coli site dif.

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Involvement of ArgR and PepA in the pairing of ColE1 dimer resolution sites

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Accessory proteins impose site selectivity during ColE1 dimer resolution.

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Structure of Cre recombinase complexed with DNA in a site-specific recombination synapse

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Recombinase binding specificity at the chromosome dimer resolution site dif of Escherichia coli.

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Peptidase activity of Escherichia coli aminopeptidase A is not required for its role in Xer site-specific recombination.

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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Structure of the oligomerization and L-arginine binding domain of the arginine repressor of Escherichia coli

21 January 2018

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10.1046/J.1365-2958.1998.00948.X

21 January 2018

Identifiers

DOI

1 reference

21 June 2017

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