Literature DB >> 25743475

Proteomic analyses of iron-responsive, Clp-dependent changes in Staphylococcus aureus.

Allison J Farrand1, David B Friedman2, Michelle L Reniere3, Hanne Ingmer4, Dorte Frees4, Eric P Skaar5.   

Abstract

Staphylococcus aureus is a frequent human pathogen that is capable of causing a wide range of life-threatening infections. A promising antibacterial target is the Clp proteolytic system, which performs the vital function of maintaining protein turnover within the cell. This system primarily impacts the bacterial response to various stresses by degrading specific proteins but can also regulate a number of physiological processes through protein degradation. A critical stress to which S. aureus must adapt during infection of a vertebrate host is nutrient iron limitation. We have previously shown that the Clp system impacts expression of genes required for heme-iron acquisition during iron limitation and is required for staphylococcal infection. Based on these data, we sought to further define the Clp-dependent impact on S. aureus during iron limitation by characterizing the proteomic profiles of mutants inactivated for components of the Clp protease, including ClpP, ClpC and ClpX, in high- and low-iron conditions. Our results reveal numerous proteins altered in abundance in the clp mutants and provide new insights into the staphylococcal proteolytic network during nutrient iron limitation. © FEMS 2015. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.

Entities:  

Keywords:  2D-DIGE; degradation; protein

Mesh:

Substances:

Year:  2015        PMID: 25743475      PMCID: PMC4542840          DOI: 10.1093/femspd/ftv004

Source DB:  PubMed          Journal:  Pathog Dis        ISSN: 2049-632X            Impact factor:   3.166


  24 in total

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4.  Identification of Staphylococcus aureus virulence genes in a murine model of bacteraemia using signature-tagged mutagenesis.

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Journal:  Mol Microbiol       Date:  1997-10       Impact factor: 3.501

5.  Passage of heme-iron across the envelope of Staphylococcus aureus.

Authors:  Sarkis K Mazmanian; Eric P Skaar; Andrew H Gaspar; Munir Humayun; Piotr Gornicki; Joanna Jelenska; Andrzej Joachmiak; Dominique M Missiakas; Olaf Schneewind
Journal:  Science       Date:  2003-02-07       Impact factor: 47.728

6.  Two-component system VraSR positively modulates the regulation of cell-wall biosynthesis pathway in Staphylococcus aureus.

Authors:  Makoto Kuroda; Hiroko Kuroda; Taku Oshima; Fumihiko Takeuchi; Hirotada Mori; Keiichi Hiramatsu
Journal:  Mol Microbiol       Date:  2003-08       Impact factor: 3.501

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Journal:  Mol Microbiol       Date:  1996-02       Impact factor: 3.501

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Authors:  Y Katayama-Fujimura; S Gottesman; M R Maurizi
Journal:  J Biol Chem       Date:  1987-04-05       Impact factor: 5.157

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Authors:  Dorte Frees; Saara N A Qazi; Philip J Hill; Hanne Ingmer
Journal:  Mol Microbiol       Date:  2003-06       Impact factor: 3.501

10.  The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone.

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Journal:  EMBO J       Date:  1995-05-01       Impact factor: 11.598

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  6 in total

1.  Contribution of YjbIH to Virulence Factor Expression and Host Colonization in Staphylococcus aureus.

Authors:  Crystal M Austin; Siamak Garabaglu; Christina N Krute; Miranda J Ridder; Nichole A Seawell; Mary A Markiewicz; Jeffrey M Boyd; Jeffrey L Bose
Journal:  Infect Immun       Date:  2019-05-21       Impact factor: 3.441

2.  Listeria monocytogenes utilizes the ClpP1/2 proteolytic machinery for fine-tuned substrate degradation at elevated temperatures.

Authors:  Dóra Balogh; Konstantin Eckel; Christian Fetzer; Stephan A Sieber
Journal:  RSC Chem Biol       Date:  2022-05-31

3.  Systematic identification of molecular mediators of interspecies sensing in a community of two frequently coinfecting bacterial pathogens.

Authors:  Tiffany M Zarrella; Anupama Khare
Journal:  PLoS Biol       Date:  2022-06-21       Impact factor: 9.593

4.  The ClpXP protease is dispensable for degradation of unfolded proteins in Staphylococcus aureus.

Authors:  Steen G Stahlhut; Abdulelah A Alqarzaee; Camilla Jensen; Niclas S Fisker; Ana R Pereira; Mariana G Pinho; Vinai Chittezham Thomas; Dorte Frees
Journal:  Sci Rep       Date:  2017-09-18       Impact factor: 4.379

Review 5.  The Bacterial ClpXP-ClpB Family Is Enriched with RNA-Binding Protein Complexes.

Authors:  Georg Auburger; Jana Key; Suzana Gispert
Journal:  Cells       Date:  2022-08-02       Impact factor: 7.666

6.  Staphylococcus aureus ClpX localizes at the division septum and impacts transcription of genes involved in cell division, T7-secretion, and SaPI5-excision.

Authors:  Camilla Jensen; Marie J Fosberg; Ida Thalsø-Madsen; Kristoffer T Bæk; Dorte Frees
Journal:  Sci Rep       Date:  2019-11-11       Impact factor: 4.379

  6 in total

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