Phosphorylation of FtsZ and FtsA by a DNA Damage-Responsive Ser/Thr Protein Kinase Affects Their Functional Interactions in
            <i>Deinococcus radiodurans</i>

Maurya, Ganesh Kumar; Modi, Kruti; Banerjee, Manas; Chaudhary, Reema; Rajpurohit, Yogendra S.; Misra, Hari S.

doi:10.1128/msphere.00325-18

Cited by 35 publications

(52 citation statements)

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“…Ser/Thr/Tyr kinases are required to modulate the activity of Bacillus cell wall hydrolases, in response to peptidoglycan fragments during spore germination [53] and the vegetative stage [54]. The Ser and Thr phosphorylation of Deinococcus radiodurans FtsA and FtsZ cell division proteins affects their functional interactions [55]. DivIVA, the key protein controlling apical growth in the mycelial bacterium Streptomyces , is modulated by the Ser/Thr kinase AfsK [56].…”

Section: Bacterial Proteins and Pathways Modulated By Ser/thr/tyr mentioning

confidence: 99%

Goals and Challenges in Bacterial Phosphoproteomics

Yagüe

Gonzalez-Quiñonez

Fernánez-García

et al. 2019

IJMS

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Reversible protein phosphorylation at serine, threonine and tyrosine is a well-known dynamic post-translational modification with stunning regulatory and signalling functions in eukaryotes. Shotgun phosphoproteomic analyses revealed that this post-translational modification is dramatically lower in bacteria than in eukaryotes. However, Ser/Thr/Tyr phosphorylation is present in all analysed bacteria (24 eubacteria and 1 archaea). It affects central processes, such as primary and secondary metabolism development, sporulation, pathogenicity, virulence or antibiotic resistance. Twenty-nine phosphoprotein orthologues were systematically identified in bacteria: ribosomal proteins, enzymes from glycolysis and gluconeogenesis, elongation factors, cell division proteins, RNA polymerases, ATP synthases and enzymes from the citrate cycle. While Ser/Thr/Tyr phosphorylation exists in bacteria, there is a consensus that histidine phosphorylation is the most abundant protein phosphorylation in prokaryotes. Unfortunately, histidine shotgun phosphorproteomics is not possible due to the reduced phosphohistidine half-life under the acidic pH conditions used in standard LC-MS/MS analysis. However, considering the fast and continuous advances in LC-MS/MS-based phosphoproteomic methodologies, it is expected that further innovations will allow for the study of His phosphoproteomes and a better coverage of bacterial phosphoproteomes. The characterisation of the biological role of bacterial Ser/Thr/Tyr and His phosphorylations might revolutionise our understanding of prokaryotic physiology.

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Section: Bacterial Proteins and Pathways Modulated By Ser/thr/tyr mentioning

confidence: 99%

Goals and Challenges in Bacterial Phosphoproteomics

Yagüe

Gonzalez-Quiñonez

Fernánez-García

et al. 2019

IJMS

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“…Immunoblotting of total proteins was carried out with specific antibodies as described earlier (Maurya et al, 2018). In brief, wild type and C-terminal domain mutant of D. radiodurans were grown overnight in TYG broth and TYG supplemented with kanamycin (8μg/ml) at 32°C.…”

Section: Immunoblotting Of Total Cellular Proteinsmentioning

confidence: 99%

DivIVA is essential in Deinococcus radiodurans and its C terminal domain regulates new septum orientation during cell division

Chaudhary

Kota

Misra

2020

Preprint

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FtsZ assembly at mid cell position in rod shaped bacteria is regulated by gradient of MinCDE complex across the poles. In round shaped bacteria, which lack predefined poles and the next plane of cell division is perpendicular to previous plane, the determination of site for FtsZ assembly is intriguing. Deinococcus radiodurans a coccus shaped bacterium, is characterized for its extraordinary resistance to DNA damage. Here we report that DivIVA a putative component of Min system in this bacterium (drDivIVA) interacts with cognate cell division and genome segregation proteins. The deletion of full length drDivIVA was found to be indispensable while its C-terminal deletion (△divIVAC) was dispensable but produced distinguishable phenotypes like slow growth, altered plane for new septum formation and angular septum. Both wild type and mutant showed FtsZ foci formation and their gamma radiation responses were nearly identical. But unlike in wild type, the FtsZ localization in mutant cells was found to be away from orthogonal axis with respect to plane of previous septum. Notably, DivIVA-RFP localizes to membrane during cell division and then perpendicular to previous plane of cell division. In trans expression of drDivIVA in △divIVAC background could restore the wild type pattern of septum formation perpendicular to previous septum. These results suggested that DivIVA is an essential protein in D. radiodurans and the C-terminal domain that contributes to its interaction with MinC determines the plane of new septum formation, possibly by controlling MinC oscillation through orthogonal axis in the cells.

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“…The functionality of rqkA in phosphorylating DNA repair protein like PprA [56] and RecA [57] of D. radiodurans has been well documented and suggested the enhancement of DNA repair activity of both PprA and RecA in gamma radiation stress. Apart from these DNA repair proteins, the phosphorylation activity of rqkA has also been found to regulate the functional interaction of cell division proteins like FtsZ and FtsA in D. radiodurans [58]. However, no information was found with respect to the functionality of significant pathways enriched in cyan module like polyketide sugar unit and streptomycin biosynthesis for stress adaptation in D. radiodurans.…”

Section: Plos Onementioning

confidence: 99%