Structural analysis of the Ras-like G protein MglA and its cognate GAP MglB and implications for bacterial polarity

Miertzschke, Mandy; Koerner, Carolin; Vetter, Ingrid R.; Keilberg, Daniela; Hot, Edina; Leonardy, Simone; Søgaard‐Andersen, Lotte; Wittinghofer, Alfred

doi:10.1038/emboj.2011.291

Cited by 95 publications

(168 citation statements)

References 66 publications

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“…In contrast, MglA did not appear to form oligomers, because the Escherichia coli strain carrying pUT18-mglA and pKTN25-mglA did not turn blue. This observation is consistent with the deduced crystal structure that shows one molecule of MglA forming a complex with two molecules of MglB (25).…”

Section: Single Gliding Motors Frequently Reverse Their Direction Of supporting

confidence: 80%

The polarity of myxobacterial gliding is regulated by direct interactions between the gliding motors and the Ras homolog MglA

Nan¹,

Bandaria

Guo³

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Gliding motility in Myxococcus xanthus is powered by flagella stator homologs that move in helical trajectories using proton motive force. The Frz chemosensory pathway regulates the cell polarity axis through MglA, a Ras family GTPase; however, little is known about how MglA establishes the polarity of gliding, because the gliding motors move simultaneously in opposite directions. Here we examined the localization and dynamics of MglA and gliding motors in high spatial and time resolution. We determined that MglA localizes not only at the cell poles, but also along the cell bodies, forming a decreasing concentration gradient toward the lagging cell pole. MglA directly interacts with the motor protein AglR, and the spatial distribution of AglR reversals is positively correlated with the MglA gradient. Thus, the motors moving toward lagging cell poles are less likely to reverse, generating stronger forward propulsion. MglB, the GTPase-activating protein of MglA, regulates motor reversal by maintaining the MglA gradient. Our results suggest a mechanism whereby bacteria use Ras family proteins to modulate cellular polarity.

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Section: Single Gliding Motors Frequently Reverse Their Direction Of supporting

confidence: 80%

The polarity of myxobacterial gliding is regulated by direct interactions between the gliding motors and the Ras homolog MglA

Nan¹,

Bandaria

Guo³

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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“…For M. xanthus it was shown that this relocation of the ATPase requires parts of the cytoskeleton and a Ras-like G protein, MglA, and its cognate GTPase-activating protein (GAP), MglB (38). Proteins that show homologies to these proteins were also found in T. thermophilus and might be also required for the relocation of PilF from T. thermophilus (41). The multiple cysteine mutations in the tetracysteine motif and the absence of zinc in the mutant PilF complexes might have a significant effect on the structure of the PilF complexes and/or the transfer of structural changes through the PilF complex, thereby affecting the interaction of PilF complexes with cytoskeletal components.…”

Section: Discussionmentioning

confidence: 98%

Zinc and ATP Binding of the Hexameric AAA-ATPase PilF from Thermus thermophilus

Salzer

Herzberg

Nies

et al. 2014

Journal of Biological Chemistry

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Background: Thermus PilF is essential for pilus biogenesis and transformation. Results: Zinc binding is essential for PilF complex stability, piliation, adhesion, and twitching motility. Conclusion: PilF complex thermostability is essential for piliation but not for natural transformation. Significance: This work highlights the role of zinc and ATP in AAA-ATPase stability and provides evidence that T4P and the DNA translocator are distinct systems.

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“…Furthermore, the KaiC-centered signaling systems could be interconnected with other signal transduction pathways, in particular, with two-components systems, via shared domains of input proteins (Fig. 4), and with Ras-like GTPases, either directly through the interaction with Srp102/FtsY or through Roadblock family proteins as described for both bacteria and eukaryotes (58,59). The mode of signaling apparently Below the scheme of predicted protein-protein interaction, selected input, modulator, and output components are listed inside the oval borders, which are colored according to the predicted functions of these components.…”

Section: Resultsmentioning

confidence: 99%

Proposed Role for KaiC-Like ATPases as Major Signal Transduction Hubs in Archaea

Makarova

Galperin

Koonin

2017

mBio

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All organisms must adapt to ever-changing environmental conditions and accordingly have evolved diverse signal transduction systems. In bacteria, the most abundant networks are built around the two-component signal transduction systems that include histidine kinases and receiver domains. In contrast, eukaryotic signal transduction is dominated by serine/threonine/tyrosine protein kinases. Both of these systems are also found in archaea, but they are not as common and diversified as their bacterial and eukaryotic counterparts, suggesting the possibility that archaea have evolved other, still uncharacterized signal transduction networks. Here we propose a role for KaiC family ATPases, known to be key components of the circadian clock in cyanobacteria, in archaeal signal transduction. The KaiC family is notably expanded in most archaeal genomes, and although most of these ATPases remain poorly characterized, members of the KaiC family have been shown to control archaellum assembly and have been found to be a stable component of the gas vesicle system in Halobacteria. Computational analyses described here suggest that KaiC-like ATPases and their homologues with inactivated ATPase domains are involved in many other archaeal signal transduction pathways and comprise major hubs of complex regulatory networks. We predict numerous input and output domains that are linked to KaiC-like proteins, including putative homologues of eukaryotic DEATH domains that could function as adapters in archaeal signaling networks. We further address the relationships of the archaeal family of KaiC homologues to the bona fide KaiC of cyanobacteria and implications for the existence of a KaiCbased circadian clock apparatus in archaea.IMPORTANCE Little is currently known about signal transduction pathways in Archaea. Recent studies indicate that KaiC-like ATPases, known as key components of the circadian clock apparatus in cyanobacteria, are involved in the regulation of archaellum assembly and, likely, type IV pili and the gas vesicle system in Archaea. We performed comprehensive comparative genomic analyses of the KaiC family. A vast protein interaction network was revealed, with KaiC family proteins as hubs for numerous input and output components, many of which are shared with twocomponent signal transduction systems. Putative KaiC-based signal transduction systems are predicted to regulate the activities of membrane-associated complexes and individual proteins, such as signal recognition particle and membrane transporters, and also could be important for oxidative stress response regulation. KaiC-centered signal transduction networks are predicted to play major roles in archaeal physiology, and this work is expected to stimulate their experimental characterization.

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Structural analysis of the Ras-like G protein MglA and its cognate GAP MglB and implications for bacterial polarity

Cited by 95 publications

References 66 publications

The polarity of myxobacterial gliding is regulated by direct interactions between the gliding motors and the Ras homolog MglA

The polarity of myxobacterial gliding is regulated by direct interactions between the gliding motors and the Ras homolog MglA

Zinc and ATP Binding of the Hexameric AAA-ATPase PilF from Thermus thermophilus

Proposed Role for KaiC-Like ATPases as Major Signal Transduction Hubs in Archaea

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