Abstract:
Straube suggests that a model that reflects the bifunctional nature of the cycle enzyme uridylyltransferase/uridylyl-removing enzyme (UTase/UR) should be used, in which the UT and UR activities are distinct and reciprocally regulated activity states of the enzyme, and notes that if such a model is used, the effects of retroactivity at intermediate stimulation will be different. However, such a model does not accurately match the observed enzyme regulatory properties and fails to predict the ultrasensitive response obtained in the experiments. Here, we argue that modeling the UTase/UR enzyme as a bifunctional enzyme with reciprocally regulated activity states misses important aspects of the system.
Registro:
Documento: |
Artículo
|
Título: | Theoretical biology: Response to comment on "'Load-induced modulation of signal transduction networks': Reconciling ultrasensitivity with bifunctionality?" |
Autor: | Jiang, P.; Ventura, A.C.; Sontag, E.D.; Merajver, S.D.; Ninfa, A.J.; Del Vecchio, D. |
Filiación: | Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, MI 48109-0606, United States Instituto de Fisiología, Biología Molecular Y Neurosciencias, Universidad de Buenos Aires, Ciudad Universitaria, Pabellón 2, Buenos Aires C1428EHA, Argentina Department of Mathematics, Rutgers University, New Brunswick, NJ 08854-8019, United States Department of Internal Medicine, Comprehensive Cancer Center, University of Michigan, Ann Arbor, MI 48109, United States Department of Mechanical Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, United States
|
Palabras clave: | hexose 1 phosphate uridylyltransferase; article; enzyme activation; enzyme activity; enzyme regulation; Escherichia coli; modulation; nonhuman; prediction; priority journal; signal transduction |
Año: | 2012
|
Volumen: | 5
|
Número: | 205
|
DOI: |
http://dx.doi.org/10.1126/scisignal.2002716 |
Título revista: | Science Signaling
|
Título revista abreviado: | Sci. Signal.
|
ISSN: | 19450877
|
CAS: | hexose 1 phosphate uridylyltransferase, 50864-66-9, 9026-21-5
|
Registro: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_19450877_v5_n205_p_Jiang |
Referencias:
- Ortega, F., Acerenza, L., Westerhoff, H.V., Mas, F., Cascante, M., Product dependence and bifunctionality compromise the ultrasensitivity of signal transduction cascades (2002) Proc. Natl. Acad. Sci. U.S.A., 99, pp. 1170-1175
- Straube, R., Comment on "Load-induced modulation of signal transduction networks": Reconciling ultrasensitivity with bifunctionality? (2012) Sci. Signal., 5, pp. lc1
- Goldbeter, A., Koshland Jr., D.E., Ultrasensitivity in biochemical systems controlled by covalent modification. Interplay between zero-order and multistep effects (1984) J. Biol. Chem., 259, pp. 14441-14447
- Guidi, G.M., Carlier, M.F., Goldbeter, A., Bistability in the isocitrate dehydrogenase reaction: An experimentally based theoretical study (1998) Biophys. J., 74, pp. 1229-1240
- Jiang, P., Ventura, A.C., Sontag, E.D., Merajver, S.D., Ninfa, A.J., Del Vecchio, D., Load-induced modulation of signal transduction networks (2011) Sci. Signal., 4, pp. ra67
- Jiang, P., Peliska, J.A., Ninfa, A.J., Enzymological characterization of the signal-transducing uridylyltransferase/uridylyl-removing enzyme (EC 2.7.7.59) of Escherichia coli and its interaction with the PII protein (1998) Biochemistry, 37, pp. 12782-12794
- Jiang, P., Mayo, A.E., Ninfa, A.J., Escherichia coli glutamine synthetase adenylyltransferase (ATase, EC 2.7.7.49): Kinetic characterization of regulation by PII, PII-UMP, glutamine, and α-ketoglutarate (2007) Biochemistry, 46, pp. 4133-4146
- Jiang, P., Atkinson, M.R., Srisawat, C., Sun, Q., Ninfa, A.J., Functional dissection of the dimerization and enzymatic activities of Escherichia coli nitrogen regulator II and their regulation by the PII protein (2000) Biochemistry, 39, pp. 13433-13449
- Ventura, A.C., Jiang, P., Van Wassenhove, L., Del Vecchio, D., Merajver, S.D., Ninfa, A.J., Signaling properties of a covalent modification cycle are altered by a downstream target (2010) Proc. Natl. Acad. Sci. U.S.A., 107, pp. 10032-10037
Citas:
---------- APA ----------
Jiang, P., Ventura, A.C., Sontag, E.D., Merajver, S.D., Ninfa, A.J. & Del Vecchio, D.
(2012)
. Theoretical biology: Response to comment on "'Load-induced modulation of signal transduction networks': Reconciling ultrasensitivity with bifunctionality?". Science Signaling, 5(205).
http://dx.doi.org/10.1126/scisignal.2002716---------- CHICAGO ----------
Jiang, P., Ventura, A.C., Sontag, E.D., Merajver, S.D., Ninfa, A.J., Del Vecchio, D.
"Theoretical biology: Response to comment on "'Load-induced modulation of signal transduction networks': Reconciling ultrasensitivity with bifunctionality?""
. Science Signaling 5, no. 205
(2012).
http://dx.doi.org/10.1126/scisignal.2002716---------- MLA ----------
Jiang, P., Ventura, A.C., Sontag, E.D., Merajver, S.D., Ninfa, A.J., Del Vecchio, D.
"Theoretical biology: Response to comment on "'Load-induced modulation of signal transduction networks': Reconciling ultrasensitivity with bifunctionality?""
. Science Signaling, vol. 5, no. 205, 2012.
http://dx.doi.org/10.1126/scisignal.2002716---------- VANCOUVER ----------
Jiang, P., Ventura, A.C., Sontag, E.D., Merajver, S.D., Ninfa, A.J., Del Vecchio, D. Theoretical biology: Response to comment on "'Load-induced modulation of signal transduction networks': Reconciling ultrasensitivity with bifunctionality?". Sci. Signal. 2012;5(205).
http://dx.doi.org/10.1126/scisignal.2002716