Determinants for substrate specificity of the bacterial PP2C protein phosphatase tPphA from Thermosynechococcus elongatus
Article first published online: 23 JAN 2012
© 2011 The Authors Journal compilation © 2011 FEBS
Special Issue: Protein Phosphatases: From Molecules to Networks
Volume 280, Issue 2, pages 694–707, January 2013
How to Cite
Su, J. and Forchhammer, K. (2013), Determinants for substrate specificity of the bacterial PP2C protein phosphatase tPphA from Thermosynechococcus elongatus. FEBS Journal, 280: 694–707. doi: 10.1111/j.1742-4658.2011.08466.x
- Issue published online: 22 JAN 2013
- Article first published online: 23 JAN 2012
- Accepted manuscript online: 23 DEC 2011 11:52AM EST
- (Received 12 September 2011, revised 7 November 2011, accepted 19 December 2011)
Fig. S1. (A), (B) Time course assay ofPII-P dephosphorylation by tPphA variants. (C) Timecourse assay of PII-P dephosphorylation by tPphA, humanPP2Cα and chimera A.
Fig. S2. Mn2+binding to tPphA,chimera A and human PP2Cα studied by isothermal titration calorimetry.
Fig. S3. (A) Inhibitory effect ofCa2+ on the relative activities of tPphA towardspNPP, pT-peptide, T-loop peptide and PII-P. (B)Inhibitory effect of Ca2+ on the dephosphorylation ofPII-P by wild-type tPphA.
Fig. S4. Glutaraldehyde (GDA) crosslinkingfollowed by Ni-NTA affinity purification (pull-down, PD) usingHis-tPphA (10 μg) with PII-P(0.5 μg).
Fig. S5. Recovery of tPphA from the pull-down assays shown in Fig. 6(A).
Table S1. The affinity and thermodynamicparameters of tPphA, chimera A and human PP2Cα from ITC assay.
Table S2. Primers used for PCR amplification of tPphA and for site-directed mutagenesis.
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