Flagella stator homologs function as motors for myxobacterial gliding motility by moving in helical trajectories

Nan, Beiyan; Bandaria, Jigar N.; Moghtaderi, Amirpasha; Sun, Im-Hong; Yıldız, Ahmet; Zusman, David R.

doi:10.1073/pnas.1219982110

Cited by 90 publications

(162 citation statements)

References 28 publications

Supporting

Mentioning

160

Contrasting

Order By: Relevance

“…Genomic analysis has shown that the M. xanthus motor complexes, unlike the MotAB complexes of enteric bacteria, lack peptidoglycan-binding domains and thus are free to move within the membrane (7). Consistent with this idea, the motor protein AglR and the motor-associated protein AgmU (GltD) have been observed to decorate a helical macrostructure that rotates as cells move forward (7,8). In addition, tracking the movements of single AglR molecules using single-particle photoactivatable localization microscopy (sptPALM) (22) revealed that the gliding motors containing AglR molecules move in helical trajectories.…”

mentioning

confidence: 78%

“…1A) (7). This model explains evenly distributed traffic jam sites in gliding cells, without invoking that force is transmitted to the surface by breaching the peptidoglycan barrier (21,23); however, how the bidirectional motion of gliding motors generates unidirectional cell movements remains unknown.…”

Section: Significancementioning

confidence: 99%

“…The first mechanism, social motility (S-motility), is powered by the extension and retraction of type IV pili from the leading cell poles (5,6). In contrast, the second mechanism, gliding motility (adventurous or A-motility), uses proton motive force to power the movement of motor complexes containing flagella stator homologs (7)(8)(9)(10)(11). Gliding M. xanthus cells on 1.5% agar plates typically reverse their polarity approximately every 8-12 min (12).…”

mentioning

confidence: 99%

“…In contrast, cell polarity for gliding motility is enigmatic, because the gliding motor complexes, as represented by the MotA homolog AglR and motor-associated proteins, such as AgmU (GltD), localize in blurry patches that move simultaneously in opposite directions along a helical track (7,8,10,11).…”

mentioning

confidence: 99%

“…A subpopulation of motors slow down and accumulate into evenly distributed "traffic jam" clusters at the ventral sides of cells, where they contact surfaces. The traffic jam clusters appear to be stationary in relation to the substratum when cells move forward (7). These clusters were originally called "focal adhesion sites" because of some similarities with eukaryotic motility complexes (9,23).…”

mentioning

confidence: 99%

See 4 more Smart Citations

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.

Self Cite

View full text Add to dashboard Cite

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.

show abstract

mentioning

confidence: 78%

Section: Significancementioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

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.

Self Cite

View full text Add to dashboard Cite

show abstract

Unorthodox regulation of the MglA Ras‐like GTPase controlling polarity in Myxococcus xanthus

Dinet

Mignot

2023

FEBS Letters

View full text Add to dashboard Cite

Motile cells have developed a large array of molecular machineries to actively change their direction of movement in response to spatial cues from their environment. In this process, small GTPases act as molecular switches and work in tandem with regulators and sensors of their guanine nucleotide status (GAP, GEF, GDI and effectors) to dynamically polarize the cell and regulate its motility. In this review, we focus on Myxococcus xanthus as a model organism to elucidate the function of an atypical small Ras GTPase system in the control of directed cell motility. M. xanthus cells direct their motility by reversing their direction of movement through a mechanism involving the redirection of the motility apparatus to the opposite cell pole. The reversal frequency of moving M. xanthus cells is controlled by modular and interconnected protein networks linking the chemosensory‐like frizzy (Frz) pathway – that transmits environmental signals – to the downstream Ras‐like Mgl polarity control system – that comprises the Ras‐like MglA GTPase protein and its regulators. Here, we discuss how variations in the GTPase interactome landscape underlie single‐cell decisions and consequently, multicellular patterns.

show abstract

Bacterial Actins and Their Interactors

Gayathri

2016

Current Topics in Microbiology and Immunology

View full text Add to dashboard Cite

Bacterial actins polymerize in the presence of nucleotide (preferably ATP), form a common arrangement of monomeric interfaces within a protofilament, and undergo ATP hydrolysis-dependent change in stability of the filament-all of which contribute to performing their respective functions. The relative stability of the filament in the ADP-bound form compared to that of ATP and the rate of addition of monomers at the two ends decide the filament dynamics. One of the major differences between eukaryotic actin and bacterial actins is the variety in protofilament arrangements and dynamics exhibited by the latter. The filament structure and the polymerization dynamics enable them to perform various functions such as shape determination in rod-shaped bacteria (MreB), cell division (FtsA), plasmid segregation (ParM family of actin-like proteins), and organelle positioning (MamK). Though the architecture and dynamics of a few representative filaments have been studied, information on the effect of interacting partners on bacterial actin filament dynamics is not very well known. The chapter reviews some of the structural and functional aspects of bacterial actins, with special focus on the effect that interacting partners exert on the dynamics of bacterial actins, and how these assist them to carry out the functions within the bacterial cell.

show abstract

Flagella stator homologs function as motors for myxobacterial gliding motility by moving in helical trajectories

Cited by 90 publications

References 28 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

Unorthodox regulation of the MglA Ras‐like GTPase controlling polarity in Myxococcus xanthus

Bacterial Actins and Their Interactors

Contact Info

Product

Resources

About