The <i>Staphylococcus aureus</i> group II biotin protein ligase BirA is an effective regulator of biotin operon transcription and requires the DNA binding domain for full enzymatic activity

Henke, Sarah K.; Cronan, John E.

doi:10.1111/mmi.13470

Cited by 14 publications

(44 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A putative BirA binding motif is detected upstream of the RNAIII gene (Mäder et al, 2016 ). BirA is a biotin-dependent repressor that downregulates genes implicated in biotin synthesis and transport (Henke and Cronan, 2016 ). In addition, RNAIII is reportedly repressed by SrrAB, a two-component system involved in aerobic to anaerobic adaptation and energy metabolism similar to B. subtilis ResDE (Yarwood et al, 2001 ).…”

Section: Results and Hypothesismentioning

confidence: 99%

Assessment of Bona Fide sRNAs in Staphylococcus aureus

et al. 2018

View full text Add to dashboard Cite

Bacterial regulatory RNAs have been extensively studied for over a decade, and are progressively being integrated into the complex genetic regulatory network. Transcriptomic arrays, recent deep-sequencing data and bioinformatics suggest that bacterial genomes produce hundreds of regulatory RNAs. However, while some have been authenticated, the existence of the others varies according to strains and growth conditions, and their detection fluctuates with the methodologies used for data acquisition and interpretation. For example, several small RNA (sRNA) candidates are now known to be parts of UTR transcripts. Accurate annotation of regulatory RNAs is a complex task essential for molecular and functional studies. We defined bona fide sRNAs as those that (i) likely act in trans and (ii) are not expressed from the opposite strand of a coding gene. Using published data and our own RNA-seq data, we reviewed hundreds of Staphylococcus aureus putative regulatory RNAs using the DETR'PROK computational pipeline and visual inspection of expression data, addressing the question of which transcriptional signals correspond to sRNAs. We conclude that the model strain HG003, a NCTC8325 derivative commonly used for S. aureus genetic regulation studies, has only about 50 bona fide sRNAs, indicating that these RNAs are less numerous than commonly stated. Among them, about half are associated to the S. aureus sp. core genome and a quarter are possibly expressed in other Staphylococci. We hypothesize on their features and regulation using bioinformatic approaches.

show abstract

Section: Results and Hypothesismentioning

confidence: 99%

Assessment of Bona Fide sRNAs in Staphylococcus aureus

et al. 2018

View full text Add to dashboard Cite

show abstract

“…These assays of the interaction between the cAMP-CRP complex and P. putida F1 cti promoter region were done essentially as previously reported (Herrera et al, 2012;Henke and Cronan, 2016). The DNA-binding reaction contained 200 μg ml −1 of bovine serum albumin, 50 mM Tris-HCl (pH 7.5), 100 mM NaCl, 0.1 mM dithiothreitol (DTT), 100 μM cAMP and 1 mM EDTA, 40 nM DNA and the indicated concentrations of Crp.…”

Section: Electrophoretic Mobility Shift Assaysmentioning

confidence: 99%

Transcriptional regulation of fatty acid cis–trans isomerization in the solvent‐tolerant soil bacterium, Pseudomonas putida F1

Kondakova

Cronan

2019

Environmental Microbiology

Self Cite

View full text Add to dashboard Cite

Summary One key to the success of Pseudomonas spp. is their ability to reside in hostile environments. Pseudomonas spp. possess a cis–trans isomerase (Cti) an enzyme that converts the cis‐unsaturated fatty acids (FAs) of the membrane lipids to their trans‐isomers to rigidify the membrane and thereby resist stresses. Whereas the posttranslational Cti regulation has been previously reported, transcriptional cti regulation remains to be studied in more details. Here, we have studied cti transcriptional regulation in the solvent‐tolerant strain Pseudomonas putida F1. Two cti transcriptional start sites (cti‐279 and cti‐77) were identified with cti‐279 transcript being dominant. Expression of cti was found to increase with temperature increase, addition of the organic solvent, octanol and in the stationary growth phase. We found that cti expression was repressed by the cyclic‐AMP receptor protein (Crp) and repression required the cyclic‐AMP ligand of Crp. Production of trans‐unsaturated FAs was found to decrease after 24 h of growth. Although this decrease was accompanied by an increase in cyclopropane FA content, this was not at the expense of trans‐unsaturated FAs demonstrating the absence of competition between Cti and Cfa in FA modification.

show abstract

“…Studies of the Staphylococcus aureus and Bacillus subtilis enzymes provide a mixed picture of the functional energetics of the Biotin Regulatory System in these organisms. Both in vivo and in vitro measurements performed on the B. subtilis BirA ( Bs BirA) indicate that, like the E. coli enzyme ( Ec BirA), transcription regulation and biotin operator binding are very sensitive to biotin concentration . However, measurements of S. aureus BirA ( Sa BirA) binding to its cognate operator site using electrophoretic mobility shift assays (EMSA) indicate a relatively small difference in the overall binding energetics for the bio‐5′‐AMP‐bound and ligand free forms of the protein, a result that predicts little sensitivity of transcription regulation to biotin concentration .…”

Section: Introductionmentioning

confidence: 99%

A conserved regulatory mechanism in bifunctional biotin protein ligases

Wang

Beckett

2017

Protein Science

View full text Add to dashboard Cite

Class II bifunctional biotin protein ligases (BirA), which catalyze post-translational biotinylation and repress transcription initiation, are broadly distributed in eubacteria and archaea. However, it is unclear if these proteins all share the same molecular mechanism of transcription regulation. In Escherichia coli the corepressor biotinoyl-5'-AMP (bio-5'-AMP), which is also the intermediate in biotin transfer, promotes operator binding and resulting transcription repression by enhancing BirA dimerization. Like E. coli BirA (EcBirA), Staphylococcus aureus, and Bacillus subtilis BirA (Sa and BsBirA) repress transcription in vivo in a biotin-dependent manner. In this work, sedimentation equilibrium measurements were performed to investigate the molecular basis of this biotin-responsive transcription regulation. The results reveal that, as observed for EcBirA, Sa, and BsBirA dimerization reactions are significantly enhanced by bio-5'-AMP binding. Thus, the molecular mechanism of the Biotin Regulatory System is conserved in the biotin repressors from these three organisms.

show abstract

The Staphylococcus aureus group II biotin protein ligase BirA is an effective regulator of biotin operon transcription and requires the DNA binding domain for full enzymatic activity

Cited by 14 publications

References 28 publications

Assessment of Bona Fide sRNAs in Staphylococcus aureus

Assessment of Bona Fide sRNAs in Staphylococcus aureus

Transcriptional regulation of fatty acid cis–trans isomerization in the solvent‐tolerant soil bacterium, Pseudomonas putida F1

A conserved regulatory mechanism in bifunctional biotin protein ligases

Contact Info

Product

Resources

About