Enzyme that catalyzes the dephosphorylation of phosphoarginine residues in proteins
Stained B.Subtilis, a gram-positive bacteria, under a microscope. Image by Farida125 / CC By
Protein Arginine Phosphatase (PAPs), also known as Phosphoarginine Phosphatase, is an enzyme that catalyzes the dephosphorylation of phosphoarginine residues in proteins.[1] Protein phosphatases (PPs) are "obligatory heteromers[2]" made up of two maximum catalytic subunits attached to a non-catalytic subunit. Arginine modification is a post-translational protein modification in gram-positive bacteria. McsB and YwIE were recently identified as phosphorylating enzymes in Bacillus Subtilis (B.Subtilis).[3] YwIE was thought to be a protein-tyrosine-phosphatase, and McsB a tyrosine-kinase,[4] however in 2012 Elsholz et al.[3] showed that McsB is a protein-arginine-kinase (PAK) and YwlE is a phosphatase-arginine-phosphatase (PAP).
Many proteins rely on protein phosphatase activity for regulating their stability, localization, and interaction with other proteins.[3] Arginine modification is a post-translational protein modification in gram-positive bacteria, and protein arginine phosphorylation regulates transcription factors, in addition to tagging rogue proteins for degradation in gram-positive bacteria.[5] Like phosphorylation, dephosphorylation is a reversible post-translational event. It is reversible through the action of kinases (enzymes that adds a phosphate group to a protein via phosphorylation), and this antagonist activity of phosphorylation and dephosphorylation of proteins controls all aspect of prokaryotic and eukaryotic life.[5] In general, protein phosphatases play a crucial role in cell signaling regulation in both eukaryotes and prokaryotes. They act by removing a phosphate group from proteins, and their activity counteracts that of protein kinases.[6]
^Fuhrmann, Jakob; Subramanian, Venkataraman; Kojetin, Douglas J.; Thompson, Paul R. (2016-08-18). "Activity-based profiling reveals a regulatory link between oxidative stress and protein arginine phosphorylation". Cell Chemical Biology. 23 (8): 967–977. doi:10.1016/j.chembiol.2016.07.008. ISSN 2451-9456. PMC 5157131. PMID 27524296.
^Bertolotti, Anne (2018-12-12). "The split protein phosphatase system". Biochemical Journal. 475 (23): 3707–3723. doi:10.1042/BCJ20170726. ISSN 0264-6021. PMC 6282683. PMID 30523060.
^ abcElsholz, A. K. W.; Turgay, K.; Michalik, S.; Hessling, B.; Gronau, K.; Oertel, D.; Mader, U.; Bernhardt, J.; Becher, D.; Hecker, M.; Gerth, U. (2012-05-08). "Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis". Proceedings of the National Academy of Sciences. 109 (19): 7451–7456. doi:10.1073/pnas.1117483109. ISSN 0027-8424. PMC 3358850. PMID 22517742.
^Kirstein, Janine; Zühlke, Daniela; Gerth, Ulf; Turgay, Kürşad; Hecker, Michael (2005-10-05). "A tyrosine kinase and its activator control the activity of the CtsR heat shock repressor in B. subtilis". The EMBO Journal. 24 (19): 3435–3445. doi:10.1038/sj.emboj.7600780. ISSN 0261-4189. PMC 1276163. PMID 16163393.
^ abSuskiewicz, M.J.; Heuck, A.; Vu, L.D.; Clausen, T. (2019-02-06). "Protein arginine kinase McsB in the apo state". doi:10.2210/pdb6fh1/pdb. S2CID 145933241. Retrieved 2020-12-07. {{cite journal}}: Cite journal requires |journal= (help)
^Elsholz, A. K. W.; Turgay, K.; Michalik, S.; Hessling, B.; Gronau, K.; Oertel, D.; Mader, U.; Bernhardt, J.; Becher, D.; Hecker, M.; Gerth, U. (2012-05-08). "Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis". Proceedings of the National Academy of Sciences. 109 (19): 7451–7456. doi:10.1073/pnas.1117483109. ISSN 0027-8424. PMC 3358850. PMID 22517742.
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