Differential thermodynamic behaviours of the extra-cellular regions of two Ser/Thr PrkC kinases revealed by calorimetric studies(128 visite) Berisio R, Squeglia F, Ruggiero A, Petraccone L, Stellato MI, Del Vecchio P
Parole chiave: Dsc, Eukaryotic-Type Serine Threonine Kinases, Thermal Unfolding Of Multi-Domain Proteins, Bacillus Subtilis, Posibacteria, Staphylococcus Aureus, Bacterial Enzyme, Protein Serine Threonine Kinase, Article, Calorimetry, Circular Dichroism, Differential Scanning Calorimetry, Enzyme Analysis, Extracellular Space, Melting Point, Nonhuman, Priority Journal, Protein Folding, Protein Unfolding, Thermodynamics, Protein Kinase C, Amino Acid Sequence, Chemistry, Enzymology, Models, Molecular, Molecular Sequence Data, Protein Stability, Protein Structure, Tertiary, Sequence Homology,
Affiliazioni:
*** IBB - CNR *** Institute of Biostructures and Bioimaging, CNR, via Mezzocannone 16Napoli, Italy Department of Chemical Sciences, University of Naples Federico II, via CintiaNapoli, Italy Consiglio Nazionale delle Ricerche Universita degli Studi di Napoli Federico II
Riferimenti:
Madec, E., Laszkiewicz, A., Iwanicki, A., Obuchowski, M., Seror, S., Characterization of a membrane-linked Ser/Thr protein kinase in Bacillus subtilis, implicated in developmental processes (2002) Mol. Microbiol., 46, pp. 571-58
Fiuza, M., Canova, M.J., Zanella-Cleon, I., Becchi, M., Cozzone, A.J., Mateos, L.M., Kremer, L., Molle, V., From the characterization of the four serine/threonine protein kinases (PknA/B/G/L) of Corynebacterium glutamicum toward the role of PknA and PknB in cell division (2008) J. Biol. Chem., 283, pp. 18099-18112
Madec, E., Stensballe, A., Kjellstrom, S., Cladiere, L., Obuchowski, M., Jensen, O.N., Seror, S.J., Mass spectrometry and site-directed mutagenesis identify several autophosphorylated residues required for the activity of PrkC, a Ser/Thr kinase from Bacillus subtilis (2003) J. Mol. Biol., 330, pp. 459-472
Absalon, C., Obuchowski, M., Madec, E., Delattre, D., Holland, I.B., Seror, S.J., CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis (2009) Microbiology, 155, pp. 932-943
Ruggiero, A., De Simone, P., Smaldone, G., Squeglia, F., Berisio, R., Bacterial cell division regulation by Ser/Thr kinases: A structural perspective (2012) Curr. Protein Pept. Sci., 13, pp. 756-766
Molle, V., Kremer, L., Division and cell envelope regulation by Ser/Thr phosphorylation: Mycobacterium shows the way (2010) Mol. Microbiol., 75, pp. 1064-1077
Beltramini, A.M., Mukhopadhyay, C.D., Pancholi, V., Modulation of cell wall structure and antimicrobial susceptibility by a Staphylococcus aureus eukaryote-like serine/ threonine kinase and phosphatase (2009) Infect. Immun., 77, pp. 1406-1416
Hempel, A.M., Cantlay, S., Molle, V., Wang, S.B., Naldrett, M.J., Parker, J.L., Richards, D.M., Flardh, K., The Ser/Thr protein kinase AfsK regulates polar growth and hyphal branching in the filamentous bacteria Streptomyces (2012) Proc. Natl. Acad. Sci. U. S. A., 109, pp. E2371-E2379
Shah, I.M., Laaberki, M.H., Popham, D.L., Dworkin, J., A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments (2008) Cell, 135, pp. 486-496
Shah, I.M., Dworkin, J., Induction and regulation of a secreted peptidoglycan hydrolase by a membrane Ser/Thr kinase that detects muropeptides (2010) Mol. Microbiol., 75 (5), pp. 1232-1243
Kana, B.D., Mizrahi, V., Resuscitation-promoting factors as lytic enzymes for bacterial growth and signaling (2010) FEMS Immunol. Med. Microbiol., 58, pp. 39-50
Warner, D.F., Mizrahi, V., The survival kit of Mycobacterium tuberculosis (2007) Nat. Med., 13, pp. 282-284
Keep, N.H., Ward, J.M., Cohen-Gonsaud, M., Henderson, B., Wake up! Peptidoglycan lysis and bacterial non-growth states (2006) Trends Microbiol., 14, pp. 271-276
Hett, E.C., Rubin, E.J., Bacterial growth and cell division: A mycobacterial perspective (2008) Microbiol. Mol. Biol. Rev., 72, pp. 126-156
Ruggiero, A., Marasco, D., Squeglia, F., Soldini, S., Pedone, E., Pedone, C., Berisio, R., Structure and functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation (2010) Structure, 18, pp. 1184-1190
Squeglia, F., Marchetti, R., Ruggiero, A., Lanzetta, R., Marasco, D., Dworkin, J., Petoukhov, M., Silipo, A., Chemical basis of peptidoglycan discrimination by PrkC, a key kinase involved in bacterial resuscitation from dormancy (2011) J. Am. Chem. Soc., 133, pp. 20676-20679
McGahee, W., Lowy, F.D., Staphylococcal infections in the intensive care unit (2000) Semin. Respir. Infect., 15, pp. 308-313
Ohlsen, K., Donat, S., The impact of serine/threonine phosphorylation in Staphylococcus aureus (2010) Int. J. Med. Microbiol., 300, pp. 137-141
Cotter, P.D., Hill, C., Surviving the acid test: Responses of gram-positive bacteria to low pH (2003) Microbiol. Mol. Biol. Rev., 67, pp. 429-453. , table of contents
Magill, N.G., Cowan, A.E., Koppel, D.E., Setlow, P., The internal pH of the forespore compartment of Bacillus megaterium decreases by about 1 pH unit during sporulation (1994) J. Bacteriol., 176, pp. 2252-2258
Yeats, C., Finn, R.D., Bateman, A., The PASTA domain: A beta-lactam-binding domain (2002) Trends Biochem. Sci., 27, p. 438
Ruggiero, A., Squeglia, F., Marasco, D., Marchetti, R., Molinaro, A., Berisio, R., X-ray structural studies of the entire extracellular region of the serine/threonine kinase PrkC from Staphylococcus aureus (2011) Biochem. J., 435, pp. 33-41
Privalov, P.L., Stability of proteins. Proteinswhich do not present a single cooperative system (1982) Adv. Protein Chem., 35, pp. 1-104
Gill, S.C., Von Hippel, P.H., Calculation of protein extinction coefficients from amino acid sequence data (1989) Anal. Biochem., 182, pp. 319-326
Eswar, N., Eramian, D., Webb, B., Shen, M.Y., Sali, A., Protein structure modeling with MODELLER (2008) Methods Mol. Biol., 426, pp. 145-159
Pronk, S., Pall, S., Schulz, R., Larsson, P., Bjelkmar, P., Apostolov, R., Shirts, M.R., Lindahl, E., GROMACS 4.5: A high-throughput and highly parallel open source molecular simulation toolkit (2013) Bioinformatics, 29, pp. 845-854
Laskowski, R.A., MacArthur, M.W., Moss, D.S., Thornton, J.M., PROCHECK: A programto check the stereochemical quality of protein structures (1993) J. Appl. Crystallogr., 26, pp. 283-291
Johnson, C.M., Differential scanning calorimetry as a tool for protein folding and stability (2013) Arch. Biochem. Biophys., 531, pp. 100-109
Privalov, P.L., Microcalorimetry of proteins and their complexes (2009) Methods Mol. Biol., 490, pp. 1-39
Apic, G., Gough, J., Teichmann, S.A., Domain combinations in archaeal, eubacterial and eukaryotic proteomes (2001) J. Mol. Biol., 310, pp. 311-325
42 Records (40 escludendo Abstract e Conferenze). Impact factor totale: 169.726 (163.599 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 158.075 (151.729 escludendo Abstract e Conferenze).
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