<b>ADP‐ribosylation by the extracellular fibrils of <i>Myxococcus xanthus</i></b>

Hildebrandt, K M; Eastman, Deborah; Dworkin, Martin

doi:10.1046/j.1365-2958.1997.2111575.x

Cited by 13 publications

(6 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Scattered evidence suggests that ADP-ribosylation in bacteria is much more common in regulating important cellular pathways, e.g. development and possibly mediating cell-cell contact in M. xanthus (18, 19), differentiation process in B. subtilis (21), and differentiation and secondary metabolism in Streptomyces (22, 37). Finally, here we suggest the possible involvement of the de-ADP-ribosylation process in the control of S. coelicolor antibiotic production.…”

Section: Discussionmentioning

confidence: 99%

“…Being the best characterized, bacterial DraG (homologue of human ARH1 and ARH3) is a representative of the group of arginine-specific ADP-ribosylhydrolases whose homologues are distributed across all three domains of life. Endogenous ADP-ribosylation has also been reported for some other bacteria, Myxococcus xanthus (18, 19), Mycobacterium smegmatis (20), Bacillus subtilis (21), and Streptomyces representatives (22–25), but little is known about its function in bacteria. Genomic evidence indicates that proteins involved in ADP-ribosylation processing are widespread among bacteria.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Disruption of Macrodomain Protein SCO6735 Increases Antibiotic Production in Streptomyces coelicolor

Lalić¹,

Marjanović²,

Palazzo

et al. 2016

Journal of Biological Chemistry

View full text Add to dashboard Cite

ADP-ribosylation is a post-translational modification that can alter the physical and chemical properties of target proteins and that controls many important cellular processes. Macrodomains are evolutionarily conserved structural domains that bind ADP-ribose derivatives and are found in proteins with diverse cellular functions. Some proteins from the macrodomain family can hydrolyze ADP-ribosylated substrates and therefore reverse this post-translational modification. Bacteria and Streptomyces, in particular, are known to utilize protein ADP-ribosylation, yet very little is known about their enzymes that synthesize and remove this modification. We have determined the crystal structure and characterized, both biochemically and functionally, the macrodomain protein SCO6735 from Streptomyces coelicolor. This protein is a member of an uncharacterized subfamily of macrodomain proteins. Its crystal structure revealed a highly conserved macrodomain fold. We showed that SCO6735 possesses the ability to hydrolyze PARP-dependent protein ADP-ribosylation. Furthermore, we showed that expression of this protein is induced upon DNA damage and that deletion of this protein in S. coelicolor increases antibiotic production. Our results provide the first insights into the molecular basis of its action and impact on Streptomyces metabolism.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Disruption of Macrodomain Protein SCO6735 Increases Antibiotic Production in Streptomyces coelicolor

Lalić¹,

Marjanović²,

Palazzo

et al. 2016

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…We therefore favor the notion that fibrils bind PE and recognition is propagated along the length of the fibril by recursive conformational change via either steric or covalent modification. Covalent modification is particularly intriguing as a 29-kDa fibril protein becomes ADP-ribosylated and could play a role in signal transduction (27).…”

Section: Discussionmentioning

confidence: 99%

Myxococcus xanthus fibril appendages are essential for excitation by a phospholipid attractant

Kearns

Campbell

Shimkets

2000

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

View full text Add to dashboard Cite

Isolated (A-motile) Myxococcus xanthus cells glide over solid surfaces and display excitation, a suppression of direction reversals, when presented with phosphatidylethanolamine (PE) purified from its own membranes or synthetic dilauroyl PE and dioleoyl PE. Although the mechanism of PE signal transduction is unknown, we hypothesized that M. xanthus might use surface-associated factors to detect exogenous PE to prevent endogenous lipids from selfstimulating the sensory system. Peritrichous protein and polysaccharide appendages called fibrils were correlated with dilauroyl PE excitation. Wild-type cells treated with Congo red, an inhibitor of fibril assembly, and mutants defective in fibril biosynthesis showed an elevated reversal period, which suggested that fibrils regulate the gliding motor. Furthermore, the loss of fibrils resulted in loss of excitation to dilauroyl PE but not dioleoyl PE. Restoration of fibril production to these mutants restored the dilauroyl PE response. In addition, the dif cytoplasmic signal transduction system and starvation conditions were required for dilauroyl PE excitation. The chemically specific nature of the response and the dependence on the dif system suggests that fibrils define a novel sensory organelle whose evolution may have been necessary to prevent autostimulation by endogenous membrane lipids. Because the hydrophobic nature of dilauroyl PE would be inaccessible to periplasmic chemosensors, we suggest that fibrils act as extracellular signal transducers to probe surfaces for insoluble chemical signals. Myxococcus xanthus uses two distinct motility systems to glide over solid surfaces (1). The adventurous or A-motility system enables cells to move as individuals. The social or S-motility system requires cell-cell contact because S motile cells (A Ϫ S ϩ ) cannot move as single cells (2). At high cell densities both motility systems operate, and mutation of both systems is required to render the cells nonmotile. The mechanism of A motility is not understood. S motility bears extensive similarity to twitching motility in its dependence on type IV pili (3-5). M. xanthus displays chemotaxis toward phosphatidylethanolamine (PE) purified from its own cell membrane and chemically synthesized dilauroyl (di C12:0) and dioleoyl (di C18:1 9c) PE (6). PE is the first discrete chemoattractant for the gliding bacteria and is the first lipid attractant for any bacterium. How the PE chemotaxis sensory systems are coupled to the operation of the A and S motors is a new frontier.Escherichia coli cells swim through liquid media by using flagella and are chemotactic toward several amino acids and sugars. These attractants are detected by integral membrane methyl-accepting chemotaxis proteins (MCPs) to regulate flagellar rotation (7). Chemotaxis is divided into two processes, excitation and adaptation. E. coli regularly punctuates smooth swimming with periods of erratic tumbling but during excitation by an attractant the tumbling behavior is suppressed. Excitation results in directed movement b...

show abstract

“…Furthermore, the protein substrate for the transferase was also a fibril protein. (24) The surprising finding that the extracellular fibrils contained both the ADP-ribosyl transferase and its protein substrate has provoked us to speculate that the fibrils may be functioning as tactile antennae; and that the ADP-ribosyl transferase may be the enzymatic activity that is activated upon contact of the fibrils with an appropriate receptor on an adjacent cell, thus transmitting a signal back to the cell indicating the proximity of another cell. This speculation is illustrated in Figure 5.…”

Section: Analysis Of Fibril Proteinsmentioning

confidence: 98%

Fibrils as extracellular appendages of bacteria: Their role in contact-mediated cell-cell interactions in Myxococcus xanthus

Dworkin

1999

Bioessays

Self Cite

View full text Add to dashboard Cite

Social behavior in the myxobacterium Myxococcus xanthus involves epicellular, peritrichous appendages called fibrils. These are polysaccharide organelles containing a set of tightly adhering proteins. It is proposed that cell‐cell contact is perceived by the fibrils and is mediated by the action of a fibrillar ADP‐ribosyl transferase. Fibrils or fibril‐like organelles have also been found on a variety of other gram‐negative bacteria and at least one archaeon, and may mediate cell‐cell contact between the bacteria themselves or between the bacteria and their eukaryotic host cells. BioEssays 21:590–595, 1999. © 1999 John Wiley & Sons, Inc.

show abstract

ADP‐ribosylation by the extracellular fibrils of Myxococcus xanthus

Cited by 13 publications

References 19 publications

Disruption of Macrodomain Protein SCO6735 Increases Antibiotic Production in Streptomyces coelicolor

Disruption of Macrodomain Protein SCO6735 Increases Antibiotic Production in Streptomyces coelicolor

Myxococcus xanthus fibril appendages are essential for excitation by a phospholipid attractant

Fibrils as extracellular appendages of bacteria: Their role in contact-mediated cell-cell interactions in Myxococcus xanthus

Contact Info

Product

Resources

About