Identification of FacZ as a division site placement factor in Staphylococcus aureus
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Abstract
Staphylococcus aureus is a gram-positive pathogen responsible for life-threatening infections that are difficult to treat due to antibiotic resistance. The identification of new vulnerabilities in essential processes like cell envelope biogenesis represents a promising avenue towards the development of anti-staphylococcal therapies that overcome resistance. To this end, we performed cell sorting-based enrichments for S. aureus mutants with defects in envelope integrity and cell division. We identified many known envelope biogenesis factors as well as a large collection of new factors with roles in this process. Mutants inactivated for one of the hits, the uncharacterized SAOUHSC_01855 protein, displayed aberrant membrane invaginations and multiple FtsZ cytokinetic ring structures. This factor is broadly distributed among Firmicutes, and its inactivation in B. subtilis similarly caused division and membrane defects. We therefore renamed the protein FacZ ( F irmicute- a ssociated c oordinator of Z -rings). In S. aureus , inactivation of the conserved cell division protein GpsB suppressed the division and morphological defects of facZ mutants. Additionally, FacZ and GpsB were found to interact directly in a purified system. Thus, FacZ is a novel antagonist of GpsB function with a conserved role in controlling division site placement in S. aureus and other Firmicutes.
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Thank you so much for this great work! I really enjoyed your paper. I can tell how much work and effort you have put into it. Kudos for producing really high quality science! I was fascinated by the FacZ protein and the modeling and biochemistry you have done. First it's really cool that you were able to show the predicted binding between the FacZ motif and a part of GpsB. It's a fantastic example of combining our modern tools, such as AlphaFold, and also empirically demonstrating the validity of the predictions. I do have a couple of questions about FacZ. It's not a very big protein at 18 kDa but it seems that it may have lots of functions. 1) Do you have any hypotheses about the role of the FacZ exoplasm extension? What could it be doing there? 2) The portion of the FacZ that interacts with GpsB is very small (6 residues). What do you …
Thank you so much for this great work! I really enjoyed your paper. I can tell how much work and effort you have put into it. Kudos for producing really high quality science! I was fascinated by the FacZ protein and the modeling and biochemistry you have done. First it's really cool that you were able to show the predicted binding between the FacZ motif and a part of GpsB. It's a fantastic example of combining our modern tools, such as AlphaFold, and also empirically demonstrating the validity of the predictions. I do have a couple of questions about FacZ. It's not a very big protein at 18 kDa but it seems that it may have lots of functions. 1) Do you have any hypotheses about the role of the FacZ exoplasm extension? What could it be doing there? 2) The portion of the FacZ that interacts with GpsB is very small (6 residues). What do you think the rest of the cytoplasmic portion does? Do you think there are other binding partners? Or may be it's necessary for membrane interactions? (it would be super cool to identify a membrane association motif!!!) Or perhaps most of the cytoplasmic portion is involved in the oligomerization of FacZ? Really excited about FacZ! Thank you for your time!
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