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Literature DB >> 15489458

The Aer protein of Escherichia coli forms a homodimer independent of the signaling domain and flavin adenine dinucleotide binding.

Qinhong Ma¹, Francis Roy, Sarah Herrmann, Barry L Taylor, Mark S Johnson.

Abstract

In vivo cross-linking between native cysteines in the Aer receptor of Escherichia coli showed dimer formation at the membrane anchor and in the putative HAMP domain. Dimers also formed in mutants that did not bind flavin adenine dinucleotide and in truncated peptides without a signaling domain and part of the HAMP domain.

Entities: Chemical Gene Species

Mesh：

Substances：

Year: 2004 PMID： 15489458 PMCID： PMC523205 DOI： 10.1128/JB.186.21.7456-7459.2004

Source DB: PubMed Journal: J Bacteriol ISSN： 0021-9193 Impact factor: 3.490

20 in total

Review 1. Polarity in action: asymmetric protein localization in bacteria.

Authors: S R Lybarger; J R Maddock
Journal: J Bacteriol Date: 2001-06 Impact factor: 3.490

2. Dynamic and clustering model of bacterial chemotaxis receptors: structural basis for signaling and high sensitivity.

Authors: Sung-Hou Kim; Weiru Wang; Kyeong Kyu Kim
Journal: Proc Natl Acad Sci U S A Date: 2002-08-19 Impact factor: 11.205

3. Structure of a flavin-binding plant photoreceptor domain: insights into light-mediated signal transduction.

Authors: S Crosson; K Moffat
Journal: Proc Natl Acad Sci U S A Date: 2001-02-27 Impact factor: 11.205

4. Differences in the polar clustering of the high- and low-abundance chemoreceptors of Escherichia coli.

Authors: S R Lybarger; J R Maddock
Journal: Proc Natl Acad Sci U S A Date: 2000-07-05 Impact factor: 11.205

5. Catalytic oxidation of sulfhydryl groups by o-phenanthroline copper complex.

Authors: K Kobashi
Journal: Biochim Biophys Acta Date: 1968-05

6. Lipid phase transitions in cytoplasmic and outer membranes of Escherichia coli.

Authors: P Overath; M Brenner; T Gulik-Krzywicki; E Shechter; L Letellier
Journal: Biochim Biophys Acta Date: 1975-05-06

7. Collaborative signaling by mixed chemoreceptor teams in Escherichia coli.

Authors: Peter Ames; Claudia A Studdert; Rebecca H Reiser; John S Parkinson
Journal: Proc Natl Acad Sci U S A Date: 2002-04-30 Impact factor: 11.205

8. Genetic analysis of the HAMP domain of the Aer aerotaxis sensor localizes flavin adenine dinucleotide-binding determinants to the AS-2 helix.

Authors: Qinhong Ma; Mark S Johnson; Barry L Taylor
Journal: J Bacteriol Date: 2005-01 Impact factor: 3.490

9. PAS domain of the Aer redox sensor requires C-terminal residues for native-fold formation and flavin adenine dinucleotide binding.

Authors: Sarah Herrmann; Qinhong Ma; Mark S Johnson; Alexandre V Repik; Barry L Taylor
Journal: J Bacteriol Date: 2004-10 Impact factor: 3.490

10. Domain organization and flavin adenine dinucleotide-binding determinants in the aerotaxis signal transducer Aer of Escherichia coli.

Authors: S I Bibikov; L A Barnes; Y Gitin; J S Parkinson
Journal: Proc Natl Acad Sci U S A Date: 2000-05-23 Impact factor: 11.205

12 in total

The Aer protein of Escherichia coli forms a homodimer independent of the signaling domain and flavin adenine dinucleotide binding.

Review 1. Polarity in action: asymmetric protein localization in bacteria.

2. Dynamic and clustering model of bacterial chemotaxis receptors: structural basis for signaling and high sensitivity.

3. Structure of a flavin-binding plant photoreceptor domain: insights into light-mediated signal transduction.

4. Differences in the polar clustering of the high- and low-abundance chemoreceptors of Escherichia coli.

5. Catalytic oxidation of sulfhydryl groups by o-phenanthroline copper complex.

6. Lipid phase transitions in cytoplasmic and outer membranes of Escherichia coli.

7. Collaborative signaling by mixed chemoreceptor teams in Escherichia coli.

8. Genetic analysis of the HAMP domain of the Aer aerotaxis sensor localizes flavin adenine dinucleotide-binding determinants to the AS-2 helix.

9. PAS domain of the Aer redox sensor requires C-terminal residues for native-fold formation and flavin adenine dinucleotide binding.

10. Domain organization and flavin adenine dinucleotide-binding determinants in the aerotaxis signal transducer Aer of Escherichia coli.

1. Role of the F1 region in the Escherichia coli aerotaxis receptor Aer.

2. Interactions between the PAS and HAMP domains of the Escherichia coli aerotaxis receptor Aer.

3. Topology and boundaries of the aerotaxis receptor Aer in the membrane of Escherichia coli.

4. Minimal requirements for oxygen sensing by the aerotaxis receptor Aer.

Review 5. Aer on the inside looking out: paradigm for a PAS-HAMP role in sensing oxygen, redox and energy.

6. Organization of the aerotaxis receptor aer in the membrane of Escherichia coli.

7. Different conformations of the kinase-on and kinase-off signaling states in the Aer HAMP domain.

8. Delineating PAS-HAMP interaction surfaces and signalling-associated changes in the aerotaxis receptor Aer.

9. Structure-function relationships in the HAMP and proximal signaling domains of the aerotaxis receptor Aer.

10. Function of the N-terminal cap of the PAS domain in signaling by the aerotaxis receptor Aer.