Crystal Structures of the ADP and ATP Bound Forms of the Bacillus Anti-σ Factor SpoIIAB in Complex with the Anti-anti-σ SpoIIAA

Masuda, Shoko; Murakami, Katsuhiko; Wang, Sheng; Olson, Connor A.; Donigian, Jill R.; Leon, F.; Darst, Seth A.; Campbell, Elizabeth A.

doi:10.1016/j.jmb.2004.05.040

Cited by 63 publications

(86 citation statements)

References 37 publications

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“…PA3346C was found to be a homolog of SpoIIAB. SpoIIAB performs the dual function of a Ser protein kinase and an anti-factor (46). This study has shown that PA3346C behaves like SpoIIAB, exhibiting a Ser protein kinase activity capable of phosphorylating PA3347 and an antiantagonist binding activity.…”

Section: Discussionmentioning

confidence: 82%

Histidine-containing Phosphotransfer Protein-B (HptB) Regulates Swarming Motility through Partner-switching System in Pseudomonas aeruginosa PAO1 Strain

Bhuwan

Lee

Peng

et al. 2012

Journal of Biological Chemistry

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Background: This study investigates how histidine phosphotransfer protein-B (HptB) regulates Pseudomonas aeruginosa swarming. Results: HptB regulates the protein phosphatase activity of PA3346, which in turn controls the flagellar gene expression through interaction with PA3347. Conclusion: Our results reveal a partner-switching mechanism regulating the 28 -dependent motility genes. Significance: The interplay between a two-component system and 28 has been established.

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Section: Discussionmentioning

confidence: 82%

Histidine-containing Phosphotransfer Protein-B (HptB) Regulates Swarming Motility through Partner-switching System in Pseudomonas aeruginosa PAO1 Strain

Bhuwan

Lee

Peng

et al. 2012

Journal of Biological Chemistry

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“…Thus, the functional and structural diversity of anti-σ's reflect the need of bacteria to relay a wide variety of environmental cues to the core transcriptional apparatus via regulation of the structurally conserved σ factors. [34,35]. This figure illustrates that the asymmetric binding of σ F 3 (blue surface representation, the other σ domains were present but disordered in the σ F /AB 2 crystal structure) to the AB 2 results in one AB protomer (AB1, on the right, colored magenta) being more accessible for binding to AA (colored green).…”

Section: Discussionmentioning

confidence: 93%

“…The structure of σ F in complex with AB revealed that AB monomers form a symmetric homodimer that is in complex with a single σ F molecule, giving rise to an asymmetric complex whereby the RNAP-binding determinants of σ F are occluded [34]. Several structures of AB in complex with AA have now been solved [35]. These data provided structural evidence for the previously proposed docking model [34,36] that describes how AA induces σ F release from the σ F /AB complex ( Figure 2a).…”

Section: Regulation Of σ F Activity During Sporulationmentioning

confidence: 99%

Regulation of bacterial RNA polymerase σ factor activity: a structural perspective

Campbell

Westblade

Darst

2008

Current Opinion in Microbiology

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126

119

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SummaryIn bacteria, σ factors are essential for the promoter DNA-binding specificity of RNA polymerase. The σ factors themselves are regulated by anti-σ factors that bind and inhibit their cognate σ factor, and 'appropriators' that deploy a particular σ-associated RNA polymerase to a specific promoter class. Adding to the complexity is the regulation of anti-σ factors by both anti-anti-σ factors, which turn on σ factor activity, and co-anti-σ factors that act in concert with their partner anti-σ factor to inhibit or redirect σ activity. While σ factor structure and function is highly conserved, recent results highlight the diversity of structures and mechanisms that bacteria use to regulate σ factor activity, reflecting the diversity of environmental cues that the bacterial transcription system has evolved to respond to.

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“…Phosphorylated SpoIIAA can then be dephosphorylated by phosphatase SpoIIE (summarized in Ref. 21). However, the GTP-binding and hydrolase activities of SpoIIAA (22) have unclear physiological functions, and no known relationship to either sporulation or the growth-promoting functions of the ribosome-associated GTPase, Obg (23).…”

mentioning

confidence: 99%

“…The structure of SpoIIAA has been solved by heteronuclear NMR in solution (24), and x-ray crystallography (25) in phosphorylated and unphosphorylated forms, and in complex with SpoIIAB bound to either ADP or ATP (21). Published prelim-inary structures of additional STAS domain proteins include the NMR solution structure of Thermotoga maritima putative anti-antagonist TM1442 in phosphorylated and unphosphorylated states (26), the NMR and crystal structures of T. maritima putative anti-antagonist TM1081 (27), and the crystal structure of the putative stressosome component RsbS from Moorella thermoacetica (28).…”

mentioning

confidence: 99%

Solution Structure of the Guanine Nucleotide-binding STAS Domain of SLC26-related SulP Protein Rv1739c from Mycobacterium tuberculosis

Sharma

Baer

et al. 2011

Journal of Biological Chemistry

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The structure and intrinsic activities of conserved STAS domains of the ubiquitous SulP/SLC26 anion transporter superfamily have until recently remained unknown. Here we report the heteronuclear, multidimensional NMR spectroscopy solution structure of the STAS domain from the SulP/SLC26 putative anion transporter Rv1739c of Mycobacterium tuberculosis. The 0.87-Å root mean square deviation structure revealed a four-stranded ␤-sheet with five interspersed ␣-helices, resembling the anti-factor antagonist fold. Rv1739c STAS was shown to be a guanine nucleotide-binding protein, as revealed by nucleotide-dependent quench of intrinsic STAS fluorescence and photoaffinity labeling. NMR chemical shift perturbation analysis partnered with in silico docking calculations identified solvent-exposed STAS residues involved in nucleotide binding. Rv1739c STAS was not an in vitro substrate of mycobacterial kinases or anti-factors. These results demonstrate that Rv1739c STAS binds guanine nucleotides at physiological concentrations and undergoes a ligand-induced conformational change but, unlike anti-factor antagonists, may not mediate signals via phosphorylation.

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Crystal Structures of the ADP and ATP Bound Forms of the Bacillus Anti-σ Factor SpoIIAB in Complex with the Anti-anti-σ SpoIIAA

Cited by 63 publications

References 37 publications

Histidine-containing Phosphotransfer Protein-B (HptB) Regulates Swarming Motility through Partner-switching System in Pseudomonas aeruginosa PAO1 Strain

Histidine-containing Phosphotransfer Protein-B (HptB) Regulates Swarming Motility through Partner-switching System in Pseudomonas aeruginosa PAO1 Strain

Regulation of bacterial RNA polymerase σ factor activity: a structural perspective

Solution Structure of the Guanine Nucleotide-binding STAS Domain of SLC26-related SulP Protein Rv1739c from Mycobacterium tuberculosis

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