The General Phosphotransferase System Proteins Localize to Sites of Strong Negative Curvature in Bacterial Cells

Govindarajan, Sutharsan; Elisha, Yair; Nevo‐Dinur, Keren; Amster‐Choder, Orna

doi:10.1128/mbio.00443-13

Cited by 38 publications

(36 citation statements)

References 75 publications

(107 reference statements)

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“…These include FtsH, which localizes to the septum in B. subtilis (81); PtsI, which clusters at the poles in E. coli and B. subtilis (82)(83)(84); and ClpX, which clusters in cytoplasmic foci in multiple bacteria (85)(86)(87)(88) and whose localization is crucial for its function (89). Further work will address whether there is similar compartmentalization of proteins encoded by core PBr genes, along with the contribution of fatty acid metabolism, nutrient acquisition, and stress responses in how S. pyogenes maintains its ability to secrete toxins in response to challenge with CAPs.…”

Section: Discussionmentioning

confidence: 99%

Streptococcus pyogenes Polymyxin B-Resistant Mutants Display Enhanced ExPortal Integrity

et al. 2014

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The ExPortal protein secretion organelle in Streptococcus pyogenes is an anionic phospholipid-containing membrane microdomain enriched in Sec translocons and postsecretion protein biogenesis factors. Polymyxin B binds to and disrupts ExPortal integrity, resulting in defective secretion of several toxins. To gain insight into factors that influence ExPortal organization, a genetic screen was conducted to select for spontaneous polymyxin B-resistant mutants displaying enhanced ExPortal integrity. Whole-genome resequencing of 25 resistant mutants revealed from one to four mutations per mutant genome clustered primarily within a core set of 10 gene groups. Construction of mutants with individual deletions or insertions demonstrated that 7 core genes confer resistance and enhanced ExPortal integrity through loss of function, while 3 were likely due to gain of function and/or combinatorial effects. Core resistance genes include a transcriptional regulator of lipid biosynthesis, several genes involved in nutrient acquisition, and a variety of genes involved in stress responses. Two members of the latter class also function as novel regulators of the secreted SpeB cysteine protease. Analysis of the most frequently isolated mutation, a single nucleotide deletion in a track of 9 consecutive adenine residues in pstS, encoding a component of a high-affinity P i transporter, suggests that this sequence functions as a molecular switch to facilitate stress adaptation. Together, these data suggest the existence of a membrane stress response that promotes enhanced ExPortal integrity and resistance to cationic antimicrobial peptides.

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Section: Discussionmentioning

confidence: 99%

Streptococcus pyogenes Polymyxin B-Resistant Mutants Display Enhanced ExPortal Integrity

et al. 2014

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“…During cell division, the region at which the division septum meets the lateral edge can display high two-dimensional concave curvature. Several reports have identified concave membrane curvature as a beacon that recruits certain shape-sensing proteins to reside preferentially at the poles, division septum, or along the lateral surface (Govindarajan et al, 2013; Lenarcic et al, 2009; Ramamurthi and Losick, 2009; Renner et al, 2013; Strahl et al, 2015; Ursell et al, 2014). …”

Section: Introductionmentioning

confidence: 99%

Dash-and-Recruit Mechanism Drives Membrane Curvature Recognition by the Small Bacterial Protein SpoVM

et al. 2017

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In Bacillus subtilis, sporulation requires that the 26-amino acid protein SpoVM embeds specifically into the forespore membrane, a structure with convex curvature. How this nanometer-sized protein can detect curves on a micrometer scale is not well understood. Here, we report that SpoVM exploits a "dash-and-recruit" mechanism to preferentially accumulate on the forespore. Using time-resolved imaging and flow cytometry, we observe that SpoVM exhibits a faster adsorption rate onto membranes of higher convex curvature. This preferential adsorption is accurately modeled as a two-step process: first, an initial binding event occurs with a faster on rate, then cooperative recruitment of additional SpoVM molecules follows. We demonstrate that both this biochemical process and effective sporulation in vivo require an unstructured and flexible SpoVM N terminus. We propose that this two-pronged strategy of fast adsorption followed by recruitment of subsequent molecules is a general mechanism that allows small proteins to detect subtle curves with a radius 1,000-fold their size.

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“…A few studies have examined localization of various PTS proteins. The general PTS proteins, EI and HPr, were found to localize primarily to cell poles (64, 65). Localization of EII sugar permeases has been less studied, but there is recent evidence that these proteins cluster together around the cell membrane (66).…”

Section: Discussionmentioning

confidence: 99%

Cryptic prophage-encoded small protein DicB protectsEscherichia colifrom phage infection by inhibiting inner membrane receptor proteins

Ragunathan

Vanderpool

2019

Preprint

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14Bacterial genomes harbor cryptic prophages that have lost genes required for induction, 15 excision from host chromosomes, or production of phage progeny. Escherichia coli K12 strains 16 contain a cryptic prophage Qin that encodes a small RNA, DicF, and small protein, DicB, that 17 have been implicated in control of bacterial metabolism and cell division. Since DicB and DicF 18 are encoded in the Qin immunity region, we tested whether these gene products could protect 19 the E. coli host from bacteriophage infection. Transient expression of the dicBF operon yielded 20 cells that were ~100-fold more resistant to infection by λ phage than control cells, and the 21 phenotype was DicB-dependent. DicB specifically inhibited infection by λ and other phages that 22 use ManYZ membrane proteins for cytoplasmic entry of phage DNA. In addition to blocking 23ManYZ-dependent phage infection, DicB also inhibited the canonical sugar transport activity of 24ManYZ. Previous studies demonstrated that DicB interacts with MinC, an FtsZ polymerization 25 inhibitor, causing MinC localization to mid-cell and preventing Z ring formation and cell division. 26In strains producing mutant MinC proteins that do not interact with DicB, both DicB-dependent 27 phenotypes involving ManYZ were lost. These results suggest that DicB is a pleiotropic 28 regulator of bacterial physiology and cell division, and that these effects are mediated by a key 29 molecular interaction with the cell division protein MinC. 30 31 32 33 Importance 34Temperate bacteriophages can integrate their genomes into the bacterial host chromosome and 35 exist as prophages whose gene products play key roles in bacterial fitness and interactions with 36 eukaryotic host organisms. Most bacterial chromosomes contain "cryptic" prophages that have 37 lost genes required for production of phage progeny but retain genes of unknown function that 38 may be important for regulating bacterial host physiology. This study provides such an example 39 -where a cryptic prophage-encoded product can perform multiple roles in the bacterial host and 40 influence processes including metabolism, cell division, and susceptibility to phage infection. 41 Further functional characterization of cryptic prophage-encoded functions will shed new light on 42 host-phage interactions and their cellular physiological implications. 43 44 (prophage) is called a lysogen. Changes in host metabolic conditions or external environmental 55 triggers can induce the prophage, which then excises out of the host chromosome and resumes 56 a lytic lifecycle (4, 5). 57 Nearly half of all sequenced bacterial genomes have been found to contain at least one 58 prophage, with many genomes containing multiple prophages (6). Lysogeny comes at a cost to 59 the bacterial host due to the extra burden of replication of prophage DNA and the threat of 60 lysogen induction which is lethal to the host cell. On the other hand, there are many well-61 documented examples of lysogenic conversion, where prophage-encoded products confer ...

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The General Phosphotransferase System Proteins Localize to Sites of Strong Negative Curvature in Bacterial Cells

Cited by 38 publications

References 75 publications

Streptococcus pyogenes Polymyxin B-Resistant Mutants Display Enhanced ExPortal Integrity

Streptococcus pyogenes Polymyxin B-Resistant Mutants Display Enhanced ExPortal Integrity

Dash-and-Recruit Mechanism Drives Membrane Curvature Recognition by the Small Bacterial Protein SpoVM

Cryptic prophage-encoded small protein DicB protectsEscherichia colifrom phage infection by inhibiting inner membrane receptor proteins

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