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Literature DB >> 12076799

The membrane-associated F(0)F(1) ATPase is essential for the viability of Streptococcus pneumoniae.

María José Ferrándiz¹, Adela G de la Campa.

Abstract

Genetic studies aimed at eliminating expression of the atp operon (F(0)F(1) H(+)-ATPase) of Streptococcus pneumoniae by genetic disruption of atpC, the first gene of the operon, with a chloramphenicol-resistance cassette were performed. Resistant transformants were obtained only when the recipient strain had a duplication of atpC, recombination occurring in such a way that transcription of the operon from its own promoter was allowed. These results imply that the atp operon is essential for the viability of the cells.

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Year: 2002 PMID： 12076799 DOI： 10.1111/j.1574-6968.2002.tb11256.x

Source DB: PubMed Journal: FEMS Microbiol Lett ISSN： 0378-1097 Impact factor: 2.742

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Cited

11 in total

1. Molecular characterization of disease-associated streptococci of the mitis group that are optochin susceptible.

Authors: Luz Balsalobre; Antonia Hernández-Madrid; Daniel Llull; Antonio J Martín-Galiano; Ernesto García; Asunción Fenoll; Adela G de la Campa
Journal: J Clin Microbiol Date: 2006-09-13 Impact factor: 5.948

2. Turbine enzyme's structure in the crosshairs to target tuberculosis.

Authors: Thomas M Duncan
Journal: Proc Natl Acad Sci U S A Date: 2019-02-19 Impact factor: 11.205

3. Novel antibiotics targeting respiratory ATP synthesis in Gram-positive pathogenic bacteria.

Authors: Wendy Balemans; Luc Vranckx; Nacer Lounis; Ovidiu Pop; Jérôme Guillemont; Karen Vergauwen; Selena Mol; Ron Gilissen; Magali Motte; David Lançois; Miguel De Bolle; Kristien Bonroy; Holger Lill; Koen Andries; Dirk Bald; Anil Koul
Journal: Antimicrob Agents Chemother Date: 2012-05-21 Impact factor: 5.191

4. Genetic characterization of optochin-susceptible viridans group streptococci.

Authors: Antonio J Martín-Galiano; Luz Balsalobre; Asunción Fenoll; Adela G de la Campa
Journal: Antimicrob Agents Chemother Date: 2003-10 Impact factor: 5.191

Review 5. The regulatory subunit ε in Escherichia coli F_OF₁-ATP synthase.

Authors: Hendrik Sielaff; Thomas M Duncan; Michael Börsch
Journal: Biochim Biophys Acta Bioenerg Date: 2018-06-20 Impact factor: 3.991

6. A new type of Na(+)-driven ATP synthase membrane rotor with a two-carboxylate ion-coupling motif.

Authors: Sarah Schulz; Marina Iglesias-Cans; Alexander Krah; Ozkan Yildiz; Vanessa Leone; Doreen Matthies; Gregory M Cook; José D Faraldo-Gómez; Thomas Meier
Journal: PLoS Biol Date: 2013-06-25 Impact factor: 8.029

7. High-resolution definition of the Vibrio cholerae essential gene set with hidden Markov model-based analyses of transposon-insertion sequencing data.

Authors: Michael C Chao; Justin R Pritchard; Yanjia J Zhang; Eric J Rubin; Jonathan Livny; Brigid M Davis; Matthew K Waldor
Journal: Nucleic Acids Res Date: 2013-07-30 Impact factor: 16.971

The membrane-associated F(0)F(1) ATPase is essential for the viability of Streptococcus pneumoniae.

1. Molecular characterization of disease-associated streptococci of the mitis group that are optochin susceptible.

2. Turbine enzyme's structure in the crosshairs to target tuberculosis.

3. Novel antibiotics targeting respiratory ATP synthesis in Gram-positive pathogenic bacteria.

4. Genetic characterization of optochin-susceptible viridans group streptococci.

Review 5. The regulatory subunit ε in Escherichia coli F_OF₁-ATP synthase.

6. A new type of Na(+)-driven ATP synthase membrane rotor with a two-carboxylate ion-coupling motif.

7. High-resolution definition of the Vibrio cholerae essential gene set with hidden Markov model-based analyses of transposon-insertion sequencing data.

8. Structure of the ATP synthase catalytic complex (F(1)) from Escherichia coli in an autoinhibited conformation.

9. Cryo-EM reveals distinct conformations of E. coli ATP synthase on exposure to ATP.

10. Atypical Pneumococcal Isolate from Blood.

Review 5. The regulatory subunit ε in Escherichia coli FOF1-ATP synthase.

Review 5. The regulatory subunit ε in Escherichia coli F_OF₁-ATP synthase.