SEARCH

SEARCH BY CITATION

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.

Please note: As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer-reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors.

FilenameFormatSizeDescription
febs8466_sm_FigsS1-S5-TablesS1-S2.zip2006KSupporting info item

Please note: Wiley Blackwell is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.