DksA2, a zinc-independent structural analog of the transcription factor DksA

Ran Furman; Tapan Biswas; Eric M. Danhart; Mark P. Foster; Oleg V. Tsodikov; Irina Artsimovitch

doi:10.1016/j.febslet.2013.01.073

DksA2, a zinc-independent structural analog of the transcription factor DksA

Ran Furman, Tapan Biswas, Eric M. Danhart, Mark P. Foster, Oleg V. Tsodikov, Irina Artsimovitch

Research output: Contribution to journal › Article › peer-review

31 Scopus citations

Abstract

Transcription factor DksA contains a four-Cys Zn^{2 +}-finger motif thought to be responsible for structural integrity and the relative disposition of its domains. Pseudomonas aeruginosa encodes an additional DksA paralog (DksA2) that is expressed selectively under Zn²⁺ limitation. Although DksA2 does not bind Zn²⁺, it complements the Escherichia coli dksA deletion and has similar effects on transcription in vitro. In this study, structural and biochemical analyses reveal that DksA2 has a similar fold, domain structure and RNA polymerase binding properties to those of the E. coli DksA despite the lack of the stabilizing metal ion. Structured summary of protein interactions: RNAP and DksA2 bind by biochemical (View interaction) DksA and RNAP bind by biochemical (View interaction) DksA2 and DksA2 bind by X-ray crystallography (View interaction).

Original language	English
Pages (from-to)	614-619
Number of pages	6
Journal	FEBS Letters
Volume	587
Issue number	6
DOIs	https://doi.org/10.1016/j.febslet.2013.01.073
State	Published - Mar 18 2013

Bibliographical note

Funding Information:
We thank Tom Magliery for comments on the manuscript and stimulating discussions, the staff of sector LS-CAT of the Advanced Photon Source for their assistance with the data collection, and Ben Blowers for assistance with optimization of crystallization conditions. This work was supported by grants from the National Science Foundation ( MCB-0949569 ; to I.A.) and National Institutes of Health ( R01 GM077234 ; to M.P.F.) and by University of Michigan College of Pharmacy start-up funds to O.V.T.

Keywords

Cysteine
DksA
DksA2
RNA polymerase
Zinc

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2013.01.073

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title = "DksA2, a zinc-independent structural analog of the transcription factor DksA",

abstract = "Transcription factor DksA contains a four-Cys Zn2 +-finger motif thought to be responsible for structural integrity and the relative disposition of its domains. Pseudomonas aeruginosa encodes an additional DksA paralog (DksA2) that is expressed selectively under Zn2+ limitation. Although DksA2 does not bind Zn2+, it complements the Escherichia coli dksA deletion and has similar effects on transcription in vitro. In this study, structural and biochemical analyses reveal that DksA2 has a similar fold, domain structure and RNA polymerase binding properties to those of the E. coli DksA despite the lack of the stabilizing metal ion. Structured summary of protein interactions: RNAP and DksA2 bind by biochemical (View interaction) DksA and RNAP bind by biochemical (View interaction) DksA2 and DksA2 bind by X-ray crystallography (View interaction).",

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author = "Ran Furman and Tapan Biswas and Danhart, {Eric M.} and Foster, {Mark P.} and Tsodikov, {Oleg V.} and Irina Artsimovitch",

note = "Funding Information: We thank Tom Magliery for comments on the manuscript and stimulating discussions, the staff of sector LS-CAT of the Advanced Photon Source for their assistance with the data collection, and Ben Blowers for assistance with optimization of crystallization conditions. This work was supported by grants from the National Science Foundation ( MCB-0949569 ; to I.A.) and National Institutes of Health ( R01 GM077234 ; to M.P.F.) and by University of Michigan College of Pharmacy start-up funds to O.V.T. ",

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AU - Tsodikov, Oleg V.

AU - Artsimovitch, Irina

N1 - Funding Information: We thank Tom Magliery for comments on the manuscript and stimulating discussions, the staff of sector LS-CAT of the Advanced Photon Source for their assistance with the data collection, and Ben Blowers for assistance with optimization of crystallization conditions. This work was supported by grants from the National Science Foundation ( MCB-0949569 ; to I.A.) and National Institutes of Health ( R01 GM077234 ; to M.P.F.) and by University of Michigan College of Pharmacy start-up funds to O.V.T.

PY - 2013/3/18

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N2 - Transcription factor DksA contains a four-Cys Zn2 +-finger motif thought to be responsible for structural integrity and the relative disposition of its domains. Pseudomonas aeruginosa encodes an additional DksA paralog (DksA2) that is expressed selectively under Zn2+ limitation. Although DksA2 does not bind Zn2+, it complements the Escherichia coli dksA deletion and has similar effects on transcription in vitro. In this study, structural and biochemical analyses reveal that DksA2 has a similar fold, domain structure and RNA polymerase binding properties to those of the E. coli DksA despite the lack of the stabilizing metal ion. Structured summary of protein interactions: RNAP and DksA2 bind by biochemical (View interaction) DksA and RNAP bind by biochemical (View interaction) DksA2 and DksA2 bind by X-ray crystallography (View interaction).

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DksA2, a zinc-independent structural analog of the transcription factor DksA

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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