Dimerization and DNA-dependent aggregation of the Escherichia coli nucleoid protein and chaperone CbpA

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Dimerization and DNA-dependent aggregation of the Escherichia coli nucleoid protein and chaperone CbpA. / Cosgriff, S; Chintakayala, Kiran; Chim, YTA; Chen, X; Allen, S; Lovering, Andrew; Grainger, David.

In: Molecular Microbiology, Vol. 77, No. 5, 01.09.2010, p. 1289-1300.

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@article{6c2ca24d81954e04a9a5734ab8b9d901,
title = "Dimerization and DNA-dependent aggregation of the Escherichia coli nucleoid protein and chaperone CbpA",
abstract = "The Escherichia coli curved DNA-binding protein A (CbpA) is a nucleoid-associated DNA-binding factor and chaperone that is expressed at high levels as cells enter stationary phase. Using a combination of genetics, biochemistry, structural modelling and single-molecule atomic force microscopy we have examined dimerization of, and DNA binding by, CbpA. Our data show that CbpA dimerization is driven by a hydrophobic surface comprising amino acid side chains W287 and L290 located on the same side of an α helix close to the C-terminus of CbpA. Derivatives of CbpA that are unable to dimerize are also unable to bind DNA. Free in solution, CbpA can exist as either a monomer or dimer. However, when bound to DNA, CbpA forms large aggregates that can protect DNA from degradation by nucleases. These CbpA-DNA aggregates are similar in morphology to protein-DNA complexes formed by the DNA-binding protein from starved cells (Dps), the only other stationary phase-specific nucleoid protein. Conversely, protein-DNA complexes formed by Fis, the major growth phase nucleoid protein, have a markedly different appearance.",
author = "S Cosgriff and Kiran Chintakayala and YTA Chim and X Chen and S Allen and Andrew Lovering and David Grainger",
year = "2010",
month = sep,
day = "1",
doi = "10.1111/j.1365-2958.2010.07292.x",
language = "English",
volume = "77",
pages = "1289--1300",
journal = "Molecular Microbiology",
issn = "0950-382X",
publisher = "Wiley",
number = "5",

}

RIS

TY - JOUR

T1 - Dimerization and DNA-dependent aggregation of the Escherichia coli nucleoid protein and chaperone CbpA

AU - Cosgriff, S

AU - Chintakayala, Kiran

AU - Chim, YTA

AU - Chen, X

AU - Allen, S

AU - Lovering, Andrew

AU - Grainger, David

PY - 2010/9/1

Y1 - 2010/9/1

N2 - The Escherichia coli curved DNA-binding protein A (CbpA) is a nucleoid-associated DNA-binding factor and chaperone that is expressed at high levels as cells enter stationary phase. Using a combination of genetics, biochemistry, structural modelling and single-molecule atomic force microscopy we have examined dimerization of, and DNA binding by, CbpA. Our data show that CbpA dimerization is driven by a hydrophobic surface comprising amino acid side chains W287 and L290 located on the same side of an α helix close to the C-terminus of CbpA. Derivatives of CbpA that are unable to dimerize are also unable to bind DNA. Free in solution, CbpA can exist as either a monomer or dimer. However, when bound to DNA, CbpA forms large aggregates that can protect DNA from degradation by nucleases. These CbpA-DNA aggregates are similar in morphology to protein-DNA complexes formed by the DNA-binding protein from starved cells (Dps), the only other stationary phase-specific nucleoid protein. Conversely, protein-DNA complexes formed by Fis, the major growth phase nucleoid protein, have a markedly different appearance.

AB - The Escherichia coli curved DNA-binding protein A (CbpA) is a nucleoid-associated DNA-binding factor and chaperone that is expressed at high levels as cells enter stationary phase. Using a combination of genetics, biochemistry, structural modelling and single-molecule atomic force microscopy we have examined dimerization of, and DNA binding by, CbpA. Our data show that CbpA dimerization is driven by a hydrophobic surface comprising amino acid side chains W287 and L290 located on the same side of an α helix close to the C-terminus of CbpA. Derivatives of CbpA that are unable to dimerize are also unable to bind DNA. Free in solution, CbpA can exist as either a monomer or dimer. However, when bound to DNA, CbpA forms large aggregates that can protect DNA from degradation by nucleases. These CbpA-DNA aggregates are similar in morphology to protein-DNA complexes formed by the DNA-binding protein from starved cells (Dps), the only other stationary phase-specific nucleoid protein. Conversely, protein-DNA complexes formed by Fis, the major growth phase nucleoid protein, have a markedly different appearance.

U2 - 10.1111/j.1365-2958.2010.07292.x

DO - 10.1111/j.1365-2958.2010.07292.x

M3 - Article

C2 - 20633229

VL - 77

SP - 1289

EP - 1300

JO - Molecular Microbiology

JF - Molecular Microbiology

SN - 0950-382X

IS - 5

ER -